(en)The present invention relates to all facets of novel polynucleotides, the polypeptides they encode, antibodies and specific binding partners thereto, and their applications to research, diagnosis, drug discovery, therapy, clinical medicine, forensic science and medicine, etc. The polynucleotides are differentially-regulated in prostate cancer and are therefore useful in variety of ways, including, but not limited to, as molecular markers, as drug targets, and for detecting, diagnosing, staging, monitoring, prognosticating, preventing or treating, determining predisposition to, etc., diseases and conditions, to prostate cancer.

1.ApplicationNumber: US-14419802-A
1.PublishNumber: US-6833247-B2
2.Date Publish: 20041221
3.Inventor: SUN ZAIREN
LI XUAN
JAY GILBERT

4.Inventor Harmonized: SUN ZAIREN(US)
LI XUAN(US)
JAY GILBERT(US)

5.Country: US
6.Claims:
(en)The present invention relates to all facets of novel polynucleotides, the polypeptides they encode, antibodies and specific binding partners thereto, and their applications to research, diagnosis, drug discovery, therapy, clinical medicine, forensic science and medicine, etc. The polynucleotides are differentially-regulated in prostate cancer and are therefore useful in variety of ways, including, but not limited to, as molecular markers, as drug targets, and for detecting, diagnosing, staging, monitoring, prognosticating, preventing or treating, determining predisposition to, etc., diseases and conditions, to prostate cancer.

7.Description:
(en)DESCRIPTION OF THE DRAWINGS
FIGS. 1-11 show amino acid sequence alignments between polypeptides of the present invention, and polypeptides listed in public databases. SEQ ID NOS for the polypeptides of the present invention are listed in Table 3. Others are as follows:
FIGS. 1A and 1B KIAA0803 (SEQ ID NO31);
FIG. 2 KIAA0408 (SEQ ID NO 32);
FIG. 3 NM — 030817 (SEQ ID NO 33);
FIGS. 4A-4E NM — 015384 (SEQ ID NO34);
FIGS. 4A-4E NM — 133433 (SEQ ID NO 35);
FIGS. 5A-5B XM — 033473 (SEQ ID NO 36);
FIG. 6 XM — 059862 (SEQ ID NO 37);
FIGS. 7A-7B NM — 012062 (SEQ ID NO 38);
FIGS. 7A-7B NM — 012063 (SEQ ID NO 39);
FIGS. 7A-7B NM — 005690 (SEQ ID NO 40);
FIGS. 8A-8B XM — 042775 (SEQ ID NO 41);
FIG. 9 NM — 000125 (SEQ ID NO 42);
FIGS. 10A-10B XM — 094949 (SEQ ID NO 43);
FIGS. 11A-11C XM — 050424 (SEQ ID NO 44).


DESCRIPTION OF THE INVENTION
The present invention relates to all facets of novel polynucleotides, the polypeptides they encode, antibodies and specific binding partners thereto, and their applications to research, diagnosis, drug discovery, therapy, clinical medicine, forensic science and medicine, etc. The polynucleotides are differentially regulated in prostate cancer and are therefore useful in variety of ways, including, but not limited to, as molecular markers, as drug targets, and for detecting, diagnosing, staging, monitoring, prognosticating, preventing or treating, determining predisposition to, etc., diseases and conditions, such as cancer, especially relating to prostate. The identification of specific genes, and groups of genes, expressed in pathways physiologically relevant to prostate permits the definition of functional and disease pathways, and the delineation of targets in these pathways which are useful in diagnostic, therapeutic, and clinical applications. The present invention also relates to methods of using the polynucleotides and related products (proteins, antibodies, etc.) in business and computer-related methods, e.g., advertising, displaying, offering, selling, etc., such products for sale, commercial use, licensing, etc.
Prostate cancer is the most common form of cancer diagnosed in the American male, occurring predominantly in males over age 50. The number of men diagnosed with prostate cancer has steadily increased as a result of the increasing population of older men. In the US, approximately 198,000 men were diagnosed with prostate cancer in 2001, and an estimated 31,500 men in the US died from the disease. In comparison, 1998 estimates for lung cancer in men were 171,500 cases and 160,100 deaths, and for colorectal cancer, the estimates were 131,600 cases and 56,000 deaths. Despite these high numbers, 89 percent of men diagnosed with the disease will survive at least five years and 63 percent will survive at least 10 years.
Patients having prostate cancer display a wide range of phenotypes. In some men, following detection, the tumor remains a latent histological tumor and does not become clinically significant. However, in other men, the tumor progresses rapidly, metastasizing and killing the patient in a relatively short time. Prostate cancer can be cured if the tumor is confined to a small region of the gland and is discovered at early stage. In such cases, radiation or surgical removal often results in complete elimination of the disease. Frequently, however, the prostate cancer has already spread to surrounding tissue and metastasized to remote locations. In these cases, radiation and other therapies, are less likely to effect a complete cure.
Androgen deprivation is a conventional therapy to treat prostate cancer. Androgen blockade can be achieved through several different routes. Androgen suppressive drugs include, e.g., Lupron (leuprolide acetate), Casodex (bicalutamide), Eulexin (flutamide), Nilandron (nilutamide), Zoladex (goserelin acetate implant), and Viadur (leuprolide acetate), which act through several different mechanisms. While these drugs may offer remission and tumor regression in many cases, often the therapeutic effects are only temporary. Prostate tumors lose their sensitivity to such treatments, and become androgen-independent. Thus, new therapies are clearly needed.
The first clinical symptoms of prostate cancer are typically urinary disturbances, including painful and more frequent urination. Diagnosis for prostate cancer is usually accomplished using a combination of different procedures. Since the prostate is located next to the rectum, rectal digital examination allows the prostate to be examined manually for the presence of hyperplasia and abnormal tissue masses. Usually, this is the first line of detection. If a palpable mass is observed, a blood specimen can be assayed for prostate-specific antigen (PSA). Very little PSA is present in the blood of a healthy individual, but BPH and prostate cancer can cause large amounts of PSA to be released into the blood, indicating the presence of diseased tissue. Definitive diagnosis is generally accomplished by biopsy of the prostate tissue.
No single gene or protein has been identified which is responsible for the etiology of all prostate cancers. Although PSA is widely used as a diagnostic reagent, it has limitations in its sensitivity and its ability to detect early cancers. It is estimated that approximately 20% to 30% of tumors will be missed when PSA is used alone. It is likely that diagnostic and prognostic markers for prostate cancer disease will involve the identification and use of many different genes and gene products to reflect its multifactorial origin.
A continuing goal is to characterize the gene expression patterns of the various prostate cancers to genetically differentiate them, providing important guidance in preventing and treating cancers. Molecular pictures of cancer, such as the pattern of differentially-regulated genes identified herein, provide an important tool for molecularly dissecting and classifying cancer, identifying drug targets, providing prognosis and therapeutic information, etc. For instance, an array of polynucleotides corresponding to genes differentially regulated in prostate cancer can be used to screen tissue samples for the existence of cancer, to categorize the cancer (e.g., by the particular pattern observed), to grade the cancer (e.g., by the number of differentially-regulated genes and their amounts of expression), to identify the source of a secondary tumor, to screen for metastatic cells, etc. These arrays can be used in combination with other markers, e.g., PSA, PMSA (prostate membrane specific antigen), or any of the grading systems used in clinical medicine.
As indicated by these studies, cancer is a highly diverse disease. Although all cancers share certain characteristics, the underlying cause and disease progression can differ significantly from patient to patient. So far, over a dozen distinct genes have been identified which, when mutant, result in a cancer. In breast cancer, alone, a handful of different genes have been isolated which either cause the cancer, or produce a predisposition to it. As a consequence, disease phenotypes for a particular cancer do not look all the same. In addition to the differences in the gene(s) responsible for the cancer, heterogeneity among individuals, e.g., in age, health, sex, and genetic background, can also influence the disease and its progression. Gene penetrance, in particular, can vary widely among population members. Recent studies have shown tremendous diversity in gene expression patterns among cancer patients. For these and other reasons, one gene/polypeptide target alone can be insufficient to diagnose or treat a cancer. Even a gene which is highly differentially-expressed and penetrant in cancer patients may not be so highly expressed in all patients and at all stages of the cancer. By selecting a set of genes and/or the polypeptides they encode, cancer diagnostics and therapeutics can be designed which effectively diagnose and treat a population of diseased individuals, rather than only a small handful when single genes are targeted.
Table 1 is a list of the genes, the cellular locations of the polypeptides coded for by the genes, and their corresponding functional and structural polypeptide domains. The polynucleotide and polypeptide sequences are shown in FIGS. 1-11 and SEQ ID NOS 1-30.
Membrane (i.e., cell-surface) proteins coded for by up-regulated genes (e.g., PCP0816) are useful targets for antibodies and other binding partners (e.g., ligands, aptamers, small peptides, etc.) to selectively target agents to a breast cancer tissue for any purpose, included, but not limited to, imaging, therapeutic, diagnostic, drug delivery, gene therapy, etc. For example, binding partners, such as antibodies, can be used to treat carcinomas in analogy to how c-erbB-2 antibodies are used to prostate cancer. Membrane (e.g., when shed into the blood and other fluid) and extracellular proteins (e.g., PCP0389) can also be used as diagnostic markers for cancer, and to assess the progress of the disease, e.g., in analogy to how PSA levels are used to diagnose prostate cancer. Useful antibodies or other binding partners include those that are specific for parts of the polypeptide which are exposed extracellularly as indicated in Table 1. Table 3 summarizes the expression profile of these genes.
Polynucleotides of the present invention can also be used to detect metastatic cells in the blood. For instance, PCP0389, PCP0814, PCP0424, PC0382, PCP0840, and PCP0842 are absent from peripheral blood cells, and can therefore be used in diagnostic tests to assess whether prostate cancer cells have metastasized from the primary site.
Polynucleotides of the present invention have been mapped to specific chromosomal bands. Different human disorders are associated with these chromosome locations. See, Table 2. The polynucleotides and polypeptides they encode can be used as linkage markers, diagnostic targets, therapeutic targets, for any of the mentioned disorders, as well as any disorders or genes mapping in proximity to them. Of particular interest are those genes which map to cancer loci, such as PCP0749, PCP0814 and PCP0816.
The present invention relates to the complete polynucleotide and polypeptide sequences disclosed herein, as well as fragments thereof. Useful fragments include those which are unique and which do not overlap any known gene (e.g., amino acid residues 1-394 of SEQ ID NO 2 of PCP0749), which overlap with a known sequence (e.g., amino acids residues 395-1564 of SEQ ID NO 2 of PCP0749, which span alternative splice junctions (e.g., comprising amino acid residues 585-586 of PCP0424A of SEQ ID NO 18), which are unique to a public sequence as indicated in the Figures (e.g., e.g., amino acids residues 2149-2265 of NM — 133433 of SEQ ID NO 35), which span an alternative splice junction of a public sequence (e.g., 532-533 of NM — 005690 of SEQ ID NO 40), etc. Unique sequences can also be described as being specific for a gene because they are characteristic of the gene, but not related genes. The unique or specific sequences included polypeptide sequences, coding nucleotide sequences (e.g., as illustrated in the figures), and non-coding nucleotide sequences.
Below, for illustration, are some examples of polypeptides (included are the polynucleotides which encode them); however, the present invention includes all fragments, especially of the categories mentioned above are exemplified below.
PCP0749 (SEQ ID NO 1-2):polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-394, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0389 (SEQ ID NO 5-6): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-1-117, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0814 (SEQ ID NO 9-10): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-33, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0623 (SEQ ID NO 11-12): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-539, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0815 (SEQ ID NO 13-14): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-22, 964-1010, 1011-1041, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0840 (SEQ ID NO 15-16): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-129, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0424A (SEQ ID NO 17-18): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-53, 585-586, 586-611, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0424B (SEQ ID NO 19-20): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-53, 585-586, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0424C (SEQ ID NO 21-22): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-53, 585-586, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0816 (SEQ ID NO 25-26): polypeptides comprising, consisting of, or consisting essentially of about amino acids 268-317, 623, 992-1013, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0480 (SEQ ID NO 27-28): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-151, 152-171, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PC0382 (SEQ ID NO 23-24): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-9, polypeptide fragments thereof, and polynucleotides encoding said polypeptides;
PCP0842 (SEQ ID NO 29-30): polypeptides comprising, consisting of, or consisting essentially of about amino acids 1-454, polypeptide fragments thereof, and polynucleotides encoding said polypeptides.
Nucleic Acids
In accordance with the present invention, genes have been identified which are differentially expressed in prostate cancer. These genes can be further divided into groups based on additional characteristics of their expression and the tissues in which they are expressed. For instance, genes can be further subdivided based on the stage and/or grade of the cancer in which they are expressed. Genes can also be grouped based on their penetrance in a prostate cancer, e.g., expressed in all prostate cancer examined, expressed in a certain percentage of prostate cancer examined, etc. These groupings do not restrict or limit the use such genes in therapeutic, diagnostic, prognostic, etc., applications. For instance, a gene which is expressed in only some cancers (e.g., incompletely penetrant) may be useful in therapeutic applications to treat a subset of cancers. Similarly, a co-penetrant gene, or a gene which is expressed in prostate cancer and other normal tissues, may be useful as a therapeutic or diagnostic, even if its expression pattern is not highly prostate specific. Thus, the uses of the genes or their products are not limited by their patterns of expression.
By the phrase “differential expression,” it is meant that the levels of expression of a gene, as measured by its transcription or translation product, are different depending upon the specific cell-type or tissue (e.g., in an averaging assay that looks at a population of cells). There are no absolute amounts by which the gene expression levels must vary, as long as the differences are measurable.
The phrase “up-regulated” indicates that an mRNA transcript or other nucleic acid corresponding to a polynucleotide of the present invention is expressed in larger amounts in a cancer as compared to the same transcript expressed in normal cells from which the cancer was derived. In general, up-regulation can be assessed by any suitable method, including any of the nucleic acid detection and hybridization methods mentioned below, as well as polypeptide-based methods. Up-regulation also includes going from substantially no expression in a normal tissue, from detectable expression in a normal tissue, from significant expression in a normal tissue, to higher levels in the cancer.
The phrase “down-regulated” indicates that an mRNA transcript or other nucleic acid corresponding to a polynucleotide of the present invention is expressed in lower amounts in a cancer as compared to the same transcript expressed in normal cells from which the cancer was derived. A down-regulated gene can show no detectable expression, or any amount of expression which is less than the gene's expression in normal tissue.
Differential regulation can be determined by any suitable method, e.g., by comparing its abundance per gram of RNA (e.g., total RNA, polyadenylated mRNA, etc.) extracted from a prostate tissue in comparison to the corresponding normal tissue. The normal tissue can be from the same or different individual or source. For convenience, it can be supplied as a separate component or in a kit in combination with probes and other reagents for detecting genes. The quantity by which a nucleic acid is differentially-regulated can be any value, e.g., about 10% more or less of normal expression, about 50% more or less of normal expression, 2-fold more or less, 5-fold more or less, 10-fold more or less, etc.
The amount of transcript can also be compared to a different gene in the same sample, especially a gene whose abundance is known and substantially no different in its expression between normal and cancer cells (e.g., a “control” gene). If represented as a ratio, with the quantity of differentially-regulated gene transcript in the numerator and the control gene transcript in the denominator, the ratio would be larger, e.g., in breast cancer than in a sample from normal breast tissue.
Differential-regulation can arise through a number of different mechanisms. The present invention is not bound by any specific way through which it occurs. Differential-regulation of a polynucleotide can occur, e.g., by modulating (1) transcriptional rate of the gene (e.g., increasing its rate, inducing or stimulating its transcription from a basal, low-level rate, etc.), (2) the post-transcriptional processing of RNA transcripts, (3) the transport of RNA from the nucleus into the cytoplasm, (4) the RNA nuclear and cytoplasmic turnover (e.g., by virtue of having higher stability or resistance to degradation), and combinations thereof. See, e.g., Tollervey and Caceras, Cell , 103:703-709, 2000.
A differentially-regulated polynucleotide is useful in a variety of different applications as described in greater details below. Because it is more abundant in cancer, it and its expression products can be used in a diagnostic test to assay for the presence of cancer, e.g., in tissue sections, in a biopsy sample, in total RNA, in lymph, in blood, etc. Differentially-regulated polynucleotides and polypeptides can be used individually, or in groups, to assess the cancer, e.g., to determine the specific type of cancer, its stage of development, the nature of the genetic defect, etc., or to assess the efficacy of a treatment modality. How to use polynucleotides in diagnostic and prognostic assays is discussed below. In addition, the polynucleotides and the polypeptides they encode, can serve as a target for therapy or drug discovery. A polypeptide, coded for by a differentially-regulated polynucleotide, which is displayed on the cell-surface, can be a target for immunotherapy to destroy, inhibit, etc., the diseased tissue. Differentially-regulated transcripts can also be used in drug discovery schemes to identify pharmacological agents which suppress, inhibit, etc., their differential-regulation, thereby preventing the phenotype associated with their expression. Thus, a differentially-regulated polynucleotide and its expression products of the present invention have significant applications in diagnostic, therapeutic, prognostic, drug development, and related areas.
The expression patterns of the differentially expressed genes disclosed herein can be described as a “fingerprint” in that they are a distinctive pattern displayed by a cancer. Just as with a fingerprint, an expression pattern can be used as a unique identifier to characterize the status of a tissue sample. The list of genes represented by SEQ ID NOS 1-30 provides an example of a cell expression profile for a prostate cancer. It can be used as a point of reference to compare and characterize unknown samples and samples for which further information is sought. Tissue fingerprints can be used in many ways, e.g., to classify an unknown tissue as being a prostate cancer, to determine the origin of a particular cancer (e.g., the origin of metastatic cells), to determine the presence of a cancer in a biopsy sample, to assess the efficacy of a cancer therapy in a human patient or a non-human animal model, to detect circulating cancer cells in blood or a lymph node biopsy, etc. While the expression profile of the complete gene set represented by SEQ ID NOS 1-30 may be most informative, a fingerprint containing expression information from less than the full collection can be useful, as well. In the same way that an incomplete fingerprint may contain enough of the pattern of whorls, arches, loops, and ridges, to identify the individual, a cell expression fingerprint containing less than the full complement may be adequate to provide useful and unique identifying and other information about the sample. Moreover, cancer is a multifactorial disease, involving genetic aberrations in more than gene locus. This multifaceted nature may be reflected in different cell expression profiles associated with breast cancers arising in different individuals, in different locations in the same individual, or even within the same cancer locus. As a result, a complete match with a particular cell expression profile, as shown herein, is not necessary to classify a cancer as being of the same type or stage. Similarity to one cell expression profile, e.g., as compared to another, can be adequate to classify cancer types, grades, and stages.
A mammalian polynucleotide, or fragment thereof, of the present invention is a polynucleotide having a nucleotide sequence obtainable from a natural source. When the species name is used, e.g., human, it indicates that the polynucleotide or polypeptide is obtainable from a natural source. It therefore includes naturally-occurring normal It therefore includes naturally-occurring normal, naturally-occurring mutant, and naturally-occurring polymorphic alleles (e.g., SNPs), differentially-spliced transcripts, splice-variants, etc. By the term “naturally-occurring,” it is meant that the polynucleotide is obtainable from a natural source, e.g., animal tissue and cells, body fluids, tissue culture cells, forensic samples. Natural sources include, e.g., living cells obtained from tissues and whole organisms, tumors, cultured cell lines, including primary and immortalized cell lines. Naturally-occurring mutations can include deletions (e.g., a truncated amino- or carboxy-terminus), substitutions, inversions, or additions of nucleotide sequence. These genes can be detected and isolated by polynucleotide hybridization according to methods which one skilled in the art would know, e.g., as discussed below.
A polynucleotide according to the present invention can be obtained from a variety of different sources. It can be obtained from DNA or RNA, such as polyadenylated mRNA or total RNA, e.g., isolated from tissues, cells, or whole organism. The polynucleotide can be obtained directly from DNA or RNA, from a cDNA library, from a genomic library, etc. The polynucleotide can be obtained from a cell or tissue (e.g., from an embryonic or adult tissues) at a particular stage of development, having a desired genotype, phenotype, disease status, etc.
The polynucleotides described in SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29 can be partial sequences that correspond to full-length, naturally-occurring transcripts. The present invention includes, as well, full-length polynucleotides that comprise these partial sequences, e.g., genomic DNAs and polynucleotides comprising a start and stop codon, a start codon and a polyA tail, a transcription start and a polyA tail, etc. These sequences can be obtained by any suitable method, e.g., using a partial sequence as a probe to select a full-length cDNA from a library containing full-length inserts. A polynucleotide which “codes without interruption” refers to a polynucleotide having a continuous open reading frame (“ORF”) as compared to an ORF which is interrupted by introns or other noncoding sequences.
Polynucleotides and polypeptides (including any part of regulated prostate gene) can be excluded as compositions from the present invention if, e.g., listed in a publicly available databases on the day this application was filed and/or disclosed in a patent application having an earlier filing or priority date than this application and/or conceived and/or reduced to practice earlier than a polynucleotide in this application.
As described herein, the phrase “an isolated polynucleotide which is SEQ ID NO,” or “an isolated polynucleotide which is selected from SEQ ID NO,” refers to an isolated nucleic acid molecule from which the recited sequence was derived (e.g., a cDNA derived from mRNA; cDNA derived from genomic DNA). Because of sequencing errors, typographical errors, etc., the actual naturally-occurring sequence may differ from a SEQ ID listed herein. Thus, the phrase indicates the specific molecule from which the sequence was derived, rather than a molecule having that exact recited nucleotide sequence, analogously to how a culture depository number refers to a specific cloned fragment in a cryotube.
As explained in more detail below, a polynucleotide sequence of the invention can contain the complete sequence as shown in SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17,19, 21, 23, 25, 27, and 29, degenerate sequences thereof, anti-sense, muteins thereof, genes comprising said sequences, full-length cDNAs comprising said sequences, complete genomic sequences, fragments thereof, homologs, primers, nucleic acid molecules which hybridize thereto, derivatives thereof, etc.
Genomic
The present invention also relates genomic DNA from which the polynucleotides of the present invention can be derived. A genomic DNA coding for a human, mouse, or other mammalian polynucleotide, can be obtained routinely, for example, by screening a genomic library (e.g., a YAC library) with a polynucleotide of the present invention, or by searching nucleotide databases, such as GenBank and EMBL, for matches. Promoter and other regulatory regions (including both 5′ and 3′ regions, as well introns) can be identified upstream or downstream of coding and expressed RNAs, and assayed routinely for activity, e.g., by joining to a reporter gene (e.g., CAT, GFP, alkaline phosphatase, luciferase, galatosidase). A promoter obtained from a prostate selective gene can be used, e.g., in gene therapy to obtain tissue-specific expression of a heterologous gene (e.g., coding for a therapeutic product or cytotoxin). 5′ and 3′ sequences (including, UTRs and introns) can be used to modulate or regulate stability, transcription, and translation of nucleic acids, including the sequence to which is attached in nature, as well as heterologous nucleic acids.
Constructs
A polynucleotide of the present invention can comprise additional polynucleotide sequences, e.g., sequences to enhance expression, detection, uptake, cataloging, tagging, etc. A polynucleotide can include only coding sequence; a coding sequence and additional non-naturally occurring or heterologous coding sequence (e.g., sequences coding for leader, signal, secretory, targeting, enzymatic, fluorescent, antibiotic resistance, and other functional or diagnostic peptides); coding sequences and non-coding sequences, e.g., untranslated sequences at either a 5′ or 3′ end, or dispersed in the coding sequence, e.g., introns.
A polynucleotide according to the present invention also can comprise an expression control sequence operably linked to a polynucleotide as described above. The phrase “expression control sequence” means a polynucleotide sequence that regulates expression of a polypeptide coded for by a polynucleotide to which it is functionally (“operably”) linked. Expression can be regulated at the level of the mRNA or polypeptide. Thus, the expression control sequence includes mRNA-related elements and protein-related elements. Such elements include promoters, enhancers (viral or cellular), ribosome binding sequences, transcriptional terminators, etc. An expression control sequence is operably linked to a nucleotide coding sequence when the expression control sequence is positioned in such a manner to effect or achieve expression of the coding sequence. For example, when a promoter is operably linked 5′ to a coding sequence, expression of the coding sequence is driven by the promoter. Expression control sequences can include an initiation codon and additional nucleotides to place a partial nucleotide sequence of the present invention in-frame in order to produce a polypeptide (e.g., pET vectors from Promega have been designed to permit a molecule to be inserted into all three reading frames to identify the one that results in polypeptide expression). Expression control sequences can be heterologous or endogenous to the normal gene.
A polynucleotide of the present invention can also comprise nucleic acid vector sequences, e.g., for cloning, expression, amplification, selection, etc. Any effective vector can be used. A vector is, e.g., a polynucleotide molecule which can replicate autonomously in a host cell, e.g., containing an origin of replication. Vectors can be useful to perform manipulations, to propagate, and/or obtain large quantities of the recombinant molecule in a desired host. A skilled worker can select a vector depending on the purpose desired, e.g., to propagate the recombinant molecule in bacteria, yeast, insect, or mammalian cells. The following vectors are provided by way of example. Bacterial: pQE70, pQE60, pQE-9 (Qiagen), pBS, pD10, Phagescript, phiX174, pBK Phagemid, pNH8A, pNH16a, pNH18Z, pNH46A (Stratagene); Bluescript KS+II (Stratagene); ptrc99a, pKK223-3, pKK233-3, pDR54 0, pRIT5 (Pharmacia). Eukaryotic: PWLNEO, pSV2CAT, pOG44, pXT1, pSG (Stratagene), pSVK3, PBPV, PMSG, pSVL (Pharmacia), pCR2.1/TOPO, pCRII/TOPO, pCR4/TOPO, pTrcHisB, pCMV6-XL4, etc. However, any other vector, e.g., plasmids, viruses, or parts thereof, may be used as long as they are replicable and viable in the desired host. The vector can also comprise sequences which enable it to replicate in the host whose genome is to be modified.
Hybridization
Polynucleotide hybridization, as discussed in more detail below, is useful in a variety of applications, including, in gene detection methods, for identifying mutations, for making mutations, to identify homologs in the same and different species, to identify related members of the same gene family, in diagnostic and prognostic assays, in therapeutic applications (e.g., where an antisense polynucleotide is used to inhibit expression), etc.
The ability of two single-stranded polynucleotide preparations to hybridize together is a measure of their nucleotide sequence complementarity, e.g., base-pairing between nucleotides, such as A-T, G-C, etc. The invention thus also relates to polynucleotides, and their complements, which hybridize to a polynucleotide comprising a nucleotide sequence as set forth in SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29 and genomic sequences thereof. A nucleotide sequence hybridizing to the latter sequence will have a complementary polynucleotide strand, or act as a template for one in the presence of a polymerase (i.e., an appropriate polynucleotide synthesizing enzyme). The present invention includes both strands of polynucleotide, e.g., a sense strand and an anti-sense strand.
Hybridization conditions can be chosen to select polynucleotides which have a desired amount of nucleotide complementarity with the nucleotide sequences set forth in SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29 and genomic sequences thereof. A polynucleotide capable of hybridizing to such sequence, preferably, possesses, e.g., about 70%, 75%, 80%, 85%, 87%, 90%, 92%, 95%, 97%, 99%, or 100% complementarity, between the sequences. The present invention particularly relates to polynucleotide sequences which hybridize to the nucleotide sequences set forth in SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29 or genomic sequences thereof, under low or high stringency conditions. These conditions can be used, e.g., to select corresponding homologs in non-human species.
Polynucleotides which hybridize to polynucleotides of the present invention can be selected in various ways. Filter-type blots (i.e., matrices containing polynucleotide, such as nitrocellulose), glass chips, and other matrices and substrates comprising polynucleotides (short or long) of interest, can be incubated in a prehybridization solution (e.g., 6×SSC, 0.5% SDS, 100 μg/ml denatured salmon sperm DNA, 5× Denhardt's solution, and 50% formamide), at 22-68° C., overnight, and then hybridized with a detectable polynucleotide probe under conditions appropriate to achieve the desired stringency. In general, when high homology or sequence identity is desired, a high temperature can be used (e.g., 65° C.). As the homology drops, lower washing temperatures are used. For salt concentrations, the lower the salt concentration, the higher the stringency. The length of the probe is another consideration. Very short probes (e.g., less than 100 base pairs) are washed at lower temperatures, even if the homology is high. With short probes, formamide can be omitted. See, e.g., Current Protocols in Molecular Biology , Chapter 6, Screening of Recombinant Libraries; Sambrook et al., Molecular Cloning , 1989, Chapter 9.
For instance, high stringency conditions can be achieved by incubating the blot overnight (e.g., at least 12 hours) with a long polynucleotide probe in a hybridization solution containing, e.g., about 5×SSC, 0.5% SDS, 100 μg/ml denatured salmon sperm DNA and 50% formamide, at 42° C. Blots can be washed at high stringency conditions that allow, e.g., for less than 5% bp mismatch (e.g., wash twice in 0.1% SSC and 0.1% SDS for 30 min at 65° C.), i.e., selecting sequences having 95% or greater sequence identity.
Other non-limiting examples of high stringency conditions includes a final wash at 65° C. in aqueous buffer containing 30 mM NaCl and 0.5% SDS. Another example of high stringent conditions is hybridization in 7% SDS, 0.5 M NaPO 4 , pH 7, 1 mM EDTA at 50° C., e.g., overnight, followed by one or more washes with a 1% SDS solution at 42° C. Whereas high stringency washes can allow for less than 5% mismatch, reduced or low stringency conditions can permit up to 20% nucleotide mismatch. Hybridization at low stringency can be accomplished as above, but using lower formamide conditions, lower temperatures and/or lower salt concentrations, as well as longer periods of incubation time.
Hybridization can also be based on a calculation of melting temperature (Tm) of the hybrid formed between the probe and its target, as described in Sambrook et al. Generally, the temperature Tm at which a short oligonucleotide (containing 18 nucleotides or fewer) will melt from its target sequence is given by the following equation: Tm=(number of A's and T's)×2° C.+(number of C's and G's)×4° C. For longer molecules, Tm=81.5+16.6 log 10 [Na + ]+0.41(% GC)−600/N where [Na + ] is the molar concentration of sodium ions, % GC is the percentage of GC base pairs in the probe, and N is the length. Hybridization can be carried out at several degrees below this temperature to ensure that the probe and target can hybridize. Mismatches can be allowed for by lowering the temperature even further.
Stringent conditions can be selected to isolate sequences, and their complements, which have, e.g., at least about 90%, 95%, or 97%, nucleotide complementarity between the probe (e.g., a short polynucleotide of SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29 or genomic sequences thereof) and a target polynucleotide.
Other homologs of polynucleotides of the present invention can be obtained from mammalian and non-mammalian sources according to various methods. For example, hybridization with a polynucleotide can be employed to select homologs, e.g., as described in Sambrook et al., Molecular Cloning , Chapter 11, 1989. Such homologs can have varying amounts of nucleotide and amino acid sequence identity and similarity to such polynucleotides of the present invention. Mammalian organisms include, e.g., mice, rats, monkeys, pigs, cows, etc. Non-mammalian organisms include, e.g., vertebrates, invertebrates, zebra fish, chicken, Drosophila, C. elegans, Xenopus , yeast such as S. pombe, S. cerevisiae , roundworms, prokaryotes, plants, Arabidopsis , artemia, viruses, etc. The degree of nucleotide sequence identity between human and mouse can be about, e.g. 70% or more, 85% or more for open reading frames, etc.
Alignment
Alignments can be accomplished by using any effective algorithm. For pairwise alignments of DNA sequences, the methods described by Wilbur-Lipman (e.g., Wilbur and Lipman, Proc. Natl. Acad. Sci ., 80:726-730, 1983) or Martinez/Needleman-Wunsch (e.g., Martinez, Nucleic Acid Res ., 11:4629-4634, 1983) can be used. For instance, if the Martinez/Needleman-Wunsch DNA alignment is applied, the minimum match can be set at 9, gap penalty at 1.10, and gap length penalty at 0.33. The results can be calculated as a similarity index, equal to the sum of the matching residues divided by the sum of all residues and gap characters, and then multiplied by 100 to express as a percent. Similarity index for related genes at the nucleotide level in accordance with the present invention can be greater than 70%, 80%, 85%, 90%, 95%, 99%, or more. Pairs of protein sequences can be aligned by the Lipman-Pearson method (e.g., Lipman and Pearson, Science , 227:1435-1441, 1985) with k-tuple set at 2, gap penalty set at 4, and gap length penalty set at 12. Results can be expressed as percent similarity index, where related genes at the amino acid level in accordance with the present invention can be greater than 65%, 70%, 75%, 80%, 85%, 90%, 95%, 99%, or more. Various commercial and free sources of alignment programs are available, e.g., MegAlign by DNA Star, BLAST (National Center for Biotechnology Information), BCM (Baylor College of Medicine) Launcher, etc. BLAST can be used to calculate amino acid sequence identity, amino acid sequence homology, and nucleotide sequence identity. These calculations can be made along the entire length of each of the target sequences which are to be compared.
Percent sequence identity can also be determined by other conventional methods, e.g., as described in Altschul et al., Bull. Math. Bio , 48: 603-616, 1986 and Henikoff and Henikoff, Proc. Natl. Acad. Sci . USA 89:10915-10919, 1992.
Specific Polynucleotide Probes
A polynucleotide of the present invention can comprise any continuous nucleotide sequence of SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29, sequences which share sequence identity thereto, or complements thereof. The term “probe” refers to any substance that can be used to detect, identify, isolate, etc., another substance. A polynucleotide probe is comprised of nucleic acid can be used to detect, identify, etc., other nucleic acids, such as DNA and RNA.
These polynucleotides can be of any desired size that is effective to achieve the specificity desired. For example, a probe can be from about 7 or 8 nucleotides to several thousand nucleotides, depending upon its use and purpose. For instance, a probe used as a primer PCR can be shorter than a probe used in an ordered array of polynucleotide probes. Probe sizes vary, and the invention is not limited in any way by their size, e.g., probes can be from about 7-2000 nucleotides, 7-1000, 8-700, 8-600, 8-500, 8-400, 8-300, 8-150, 8-100, 8-7-50, 10-25, 14-16, at least about 8, at least about 10, at least about 15, at least about 25, etc. The polynucleotides can have non-naturally-occurring nucleotides, e.g., inosine, AZT, 3TC, etc. The polynucleotides can have 100% sequence identity or complementarity to a sequence of SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29, or it can have mismatches or nucleotide substitutions, e.g., 1, 2, 3, 4, or 5 substitutions. The probes can be single-stranded or double-stranded.
In accordance with the present invention, a polynucleotide can be present in a kit, where the kit includes, e.g., one or more polynucleotides, a desired buffer (e.g., phosphate, tris, etc.), detection compositions, RNA or cDNA from different tissues to be used as controls, libraries, etc. The polynucleotide can be labeled or unlabeled, with radioactive or non-radioactive labels as known in the art. Kits can comprise one or more pairs of polynucleotides for amplifying nucleic acids specific for differentially-regulated genes of the present invention, e.g., comprising a forward and reverse primer effective in PCR. These include both sense and anti-sense orientations. For instance, in PCR-based methods (such as RT-PCR), a pair of primers are typically used, one having a sense sequence and the other having an antisense sequence.
Another aspect of the present invention is a nucleotide sequence that is specific to, or for, a selective polynucleotide. The phrases “specific for” or “specific to” a polynucleotide have a functional meaning that the polynucleotide can be used to identify the presence of one or more target genes in a sample and distinguish them from non-target genes. It is specific in the sense that it can be used to detect polynucleotides above background noise (“non-specific binding”). A specific sequence is a defined order of nucleotides (or amino acid sequences, if it is a polypeptide sequence) which occurs in the polynucleotide, e.g., in the nucleotide sequences of SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29, and which is characteristic of that target sequence, and substantially no non-target sequences. A probe or mixture of probes can comprise a sequence or sequences that are specific to a plurality of target sequences, e.g., where the sequence is a consensus sequence, a functional domain, etc., e.g., capable of recognizing a family of related genes. Such sequences can be used as probes in any of the methods described herein or incorporated by reference. Both sense and antisense nucleotide sequences are included. A specific polynucleotide according to the present invention can be determined routinely.
A polynucleotide comprising a specific sequence can be used as a hybridization probe to identify the presence of, e.g., human or mouse polynucleotide, in a sample comprising a mixture of polynucleotides, e.g., on a Northern blot. Hybridization can be performed under high stringent conditions (see, above) to select polynucleotides (and their complements which can contain the coding sequence) having at least 90%, 95%, 99%, etc., identity (i.e., complementarity) to the probe, but less stringent conditions can also be used. A specific polynucleotide sequence can also be fused in-frame, at either its 5′ or 3′ end, to various nucleotide sequences as mentioned throughout the patent, including coding sequences for enzymes, detectable markers, GFP, etc, expression control sequences, etc.
A polynucleotide probe, especially one that is specific to a polynucleotide of the present invention, can be used in gene detection and hybridization methods as already described. In one embodiment, a specific polynucleotide probe can be used to detect whether a particular tissue or cell-type is present in a target sample. To carry out such a method, a selective polynucleotide can be chosen which is characteristic of the desired target tissue. Such polynucleotide is preferably chosen so that it is expressed or displayed in the target tissue, but not in other tissues which are present in the sample. For instance, if detection of prostate is desired, it may not matter whether the selective polynucleotide is expressed in other tissues, as long as it is not expressed in cells normally present in blood, e.g., peripheral blood mononuclear cells. Starting from the selective polynucleotide, a specific polynucleotide probe can be designed which hybridizes (if hybridization is the basis of the assay) under the hybridization conditions to the selective polynucleotide, whereby the presence of the selective polynucleotide can be determined.
Probes which are specific for polynucleotides of the present invention can also be prepared using involve transcription-based systems, e.g., incorporating an RNA polymerase promoter into a selective polynucleotide of the present invention, and then transcribing anti-sense RNA using the polynucleotide as a template. See, e.g., U.S. Pat. No. 5,545,522.
Polynucleotide Composition
A polynucleotide according to the present invention can comprise, e.g., DNA, RNA, synthetic polynucleotide, peptide polynucleotide, modified nucleotides, dsDNA, ssDNA, ssRNA, dsRNA, and mixtures thereof. A polynucleotide can be single- or double-stranded, triplex, DNA:RNA, duplexes, comprise hairpins, and other secondary structures, etc. Nucleotides comprising a polynucleotide can be joined via various known linkages, e.g., ester, sulfamate, sulfamide, phosphorothioate, phosphoramidate, methylphosphonate, carbamate, etc., depending on the desired purpose, e.g., resistance to nucleases, such as RNAse H, improved in vivo stability, etc. See, e.g., U.S. Pat. No. 5,378,825. Any desired nucleotide or nucleotide analog can be incorporated, e.g., 6-mercaptoguanine, 8-oxo-guanine, etc.
Various modifications can be made to the polynucleotides, such as attaching detectable markers (avidin, biotin, radioactive elements, fluorescent tags and dyes, energy transfer labels, energy-emitting labels, binding partners, etc.) or moieties which improve hybridization, detection, and/or stability. The polynucleotides can also be attached to solid supports, e.g., nitrocellulose, magnetic or paramagnetic microspheres (e.g., as described in U.S. Pat. Nos. 5,411,863; 5,543,289; for instance, comprising ferromagnetic, supermagnetic, paramagnetic, superparamagnetic, iron oxide and polysaccharide), nylon, agarose, diazotized cellulose, latex solid microspheres, polyacrylamides, etc., according to a desired method. See, e.g., U.S. Pat. Nos. 5,470,967, 5,476,925, and 5,478,893.
Polynucleotide according to the present invention can be labeled according to any desired method. The polynucleotide can be labeled using radioactive tracers such as 32 P, 35 S, 3 H, or 14 C, to mention some commonly used tracers. The radioactive labeling can be carried out according to any method, such as, for example, terminal labeling at the 3′ or 5′ end using a radiolabeled nueleotide, polynucleotide kinase (with or without dephosphorylation with a phosphatase) or a ligase (depending on the end to be labeled). A non-radioactive labeling can also be used, combining a polynucleotide of the present invention with residues having immunological properties (antigens, haptens), a specific affinity for certain reagents (ligands), properties enabling detectable enzyme reactions to be completed (enzymes or coenzymes, enzyme substrates, or other substances involved in an enzymatic reaction), or characteristic physical properties, such as fluorescence or the emission or absorption of light at a desired wavelength, etc.
Nucleic Acid Detection Methods
Another aspect of the present invention relates to methods and processes for detecting differentially-regulated genes of the present invention. Detection methods have a variety of applications, including for diagnostic, prognostic, forensic, and research applications. To accomplish gene detection, a polynucleotide in accordance with the present invention can be used as a “probe.” The term “probe” or “polynucleotide probe” has its customary meaning in the art, e.g., a polynucleotide which is effective to identify (e.g., by hybridization), when used in an appropriate process, the presence of a target polynucleotide to which it is designed. Identification can involve simply determining presence or absence, or it can be quantitative, e.g., in assessing amounts of a gene or gene transcript present in a sample. Probes can be useful in a variety of ways, such as for diagnostic purposes, to identify homologs, and to detect, quantitate, or isolate a polynucleotide of the present invention in a test sample.
Assays can be utilized which permit quantification and/or presence/absence detection of a target nucleic acid in a sample. Assays can be performed at the single-cell level, or in a sample comprising many cells, where the assay is “averaging” expression over the entire collection of cells and tissue present in the sample. Any suitable assay format can be used, including, but not limited to, e.g., Southern blot analysis, Northern blot analysis, polymerase chain reaction (“PCR”) (e.g., Saiki et al., Science , 241:53, 1988; U.S. Pat. Nos. 4,683,195, 4,683,202, and 6,040,166 ; PCR Protocols: A Guide to Methods and Applications , Innis et al., eds., Academic Press, New York, 1990), reverse transcriptase polymerase chain reaction (“RT-PCR”), anchored PCR, rapid amplification of cDNA ends (“RACE”) (e.g., Schaefer in Gene Cloning and Analysis: Current Innovations , Pages 99-115, 1997), ligase chain reaction (“LCR”) (EP 320 308), one-sided PCR (Ohara et al., Proc. Natl. Acad. Sci ., 86:5673-5677, 1989), indexing methods (e.g., U.S. Pat. No. 5,508,169), in situ hybridization, differential display (e.g., Liang et al., Nucl. Acid. Res ., 21:3269-3275, 1993; U.S. Pat. Nos. 5,262,311, 5,599,672 and 5,965,409; WO97/18454; Prashar and Weissman, Proc. Natl. Acad. Sci ., 93:659-663, and U.S. Pat. Nos. 6,010,850 and 5,712,126; Welsh et al., Nucleic Acid Res ., 20:4965-4970, 1992, and U.S. Pat. No. 5,487,985) and other RNA fingerprinting techniques, nucleic acid sequence based amplification (“NASBA”) and other transcription based amplification systems (e.g., U.S. Pat. Nos. 5,409,818 and 5,554,527; WO 88/10315), polynucleotide arrays (e.g., U.S. Pat. Nos. 5,143,854, 5,424,186; 5,700,637, 5,874,219, and 6,054,270; PCT WO 92/10092; PCT WO 90/15070), Qbeta Replicase (PCT/US87/00880), Strand Displacement Amplification (“SDA”), Repair Chain Reaction (“RCR”), nuclease protection assays, subtraction-based methods, Rapid-Scan™, etc. Additional useful methods include, but are not limited to, e.g., template-based amplification methods, competitive PCR (e.g., U.S. Pat. No. 5,747,251), redox-based assays (e.g., U.S. Pat. No. 5,871,918), Taqman-based assays (e.g., Holland et al., Proc. Natl. Acad, Sci ., 88:7276-7280, 1991; U.S. Pat. Nos. 5,210,015 and 5,994,063), real-time fluorescence-based monitoring (e.g., U.S. Pat. No. 5,928,907), molecular energy transfer labels (e.g., U.S. Pat. Nos. 5,348,853, 5,532,129, 5,565,322, 6,030,787, and 6,117,635; Tyagi and Kramer, Nature Biotech ., 14:303-309, 1996). Any method suitable for single cell analysis of gene or protein expression can be used, including in situ hybridization, immunocytochemistry, MACS, FACS, flow cytometry, etc. For single cell assays, expression products can be measured using antibodies, PCR, or other types of nucleic acid amplification (e.g., Brady et al., Methods Mol . & Cell. Biol . 2, 17-25, 1990; Eberwine et al., 1992 , Proc. Natl. Acad. Sci ., 89, 3010-3014, 1992; U.S. Pat. No. 5,723,290). These and other methods can be carried out conventionally, e.g., as described in the mentioned publications.
Many of such methods may require that the polynucleotide is labeled, or comprises a particular nucleotide type useful for detection. The present invention includes such modified polynucleotides that are necessary to carry out such methods. Thus, polynucleotides can be DNA, RNA, DNA:RNA hybrids, PNA, etc., and can comprise any modification or substituent which is effective to achieve detection.
Detection can be desirable for a variety of different purposes, including research, diagnostic, prognostic, and forensic. For diagnostic purposes, it may be desirable to identify the presence or quantity of a polynucleotide sequence in a sample, where the sample is obtained from tissue, cells, body fluids, etc. In a preferred method as described in more detail below, the present invention relates to a method of detecting a polynucleotide comprising, contacting a target polynucleotide in a test sample with a polynucleotide probe under conditions effective to achieve hybridization between the target and probe; and detecting hybridization.
Any test sample in which it is desired to identify a polynucleotide or polypeptide thereof can be used, including, e.g., blood, urine, saliva, stool (for extracting nucleic acid, see, e.g., U.S. Pat. No. 6,177,251), swabs comprising tissue, biopsied tissue, tissue sections, cultured cells, etc.
Detection can be accomplished in combination with polynucleotide probes for other genes, e.g., genes which are expressed in other disease states, tissues, cells, such as brain, heart, kidney, spleen, thymus, liver, stomach, small intestine, colon, muscle, lung, testis, placenta, pituitary, thyroid, skin, adrenal gland, pancreas, salivary gland, uterus, ovary, prostate gland, peripheral blood cells (T-cells, lymphocytes, etc.), embryo, normal breast fat, adult and embryonic stem cells, specific cell-types, such as endothelial, epithelial, myocytes, adipose, luminal epithelial, basoepithelial, myoepithelial, stromal cells, etc.
Polynucleotides can be used in wide range of methods and compositions, including for detecting, diagnosing, staging, grading, assessing, prognosticating, etc. diseases and disorders associated with differentially-regulated genes of the present invention, for monitoring or assessing therapeutic and/or preventative measures, in ordered arrays, etc. Any method of detecting genes and polynucleotides of SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29 can be used; certainly, the present invention is not to be limited how such methods are implemented.
Along these lines, the present invention relates to methods of detecting differentially-regulated genes described herein in a sample comprising nucleic acid. Such methods can comprise one or more the following steps in any effective order, e.g., contacting said sample with a polynucleotide probe under conditions effective for said probe to hybridize specifically to nucleic acid in said sample, and detecting the presence or absence of probe hybridized to nucleic acid in said sample, wherein said probe is a polynucleotide which is SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29, a polynucleotide having, e.g., about 70%, 80%, 85%, 90%, 95%, 99%, or more sequence identity thereto, effective or specific fragments thereof, or complements thereto. The detection method can be applied to any sample, e.g., cultured primary, secondary, or established cell lines, tissue biopsy, blood, urine, stool, cerebral spinal fluid, and other bodily fluids, for any purpose.
Contacting the sample with probe can be carried out by any effective means in any effective environment. It can be accomplished in a solid, liquid, frozen, gaseous, amorphous, solidified, coagulated, colloid, etc., mixtures thereof, matrix. For instance, a probe in an aqueous medium can be contacted with a sample which is also in an aqueous medium, or which is affixed to a solid matrix, or vice-versa.
Generally, as used throughout the specification, the term “effective conditions” means, e.g., the particular milieu in which the desired effect is achieved. Such a milieu, includes, e.g., appropriate buffers, oxidizing agents, reducing agents, pH, co-factors, temperature, ion concentrations, suitable age and/or stage of cell (such as, in particular part of the cell cycle, or at a particular stage where particular genes are being expressed) where cells are being used, culture conditions (including substrate, oxygen, carbon dioxide, etc.). When hybridization is the chosen means of achieving detection, the probe and sample can be combined such that the resulting conditions are functional for said probe to hybridize specifically to nucleic acid in said sample.
The phrase “hybridize specifically” indicates that the hybridization between single-stranded polynucleotides is based on nucleotide sequence complementarity. The effective conditions are selected such that the probe hybridizes to a preselected and/or definite target nucleic acid in the sample. For instance, if detection of a polynucleotide set forth in SEQ ID NOS 1,3,5,7,9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29 is desired, aprobe can be selected which can hybridize to such target gene under high stringent conditions, without significant hybridization to other genes in the sample. To detect homologs of a polynucleotide set forth in SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29, the effective hybridization conditions can be less stringent, and/or the probe can comprise codon degeneracy, such that a homolog is detected in the sample.
As already mentioned, the methods can be carried out by any effective process, e.g., by Northern blot analysis, polymerase chain reaction (PCR), reverse transcriptase PCR, RACE PCR, in situ hybridization, etc., as indicated above. When PCR based techniques are used, two or more probes are generally used. One probe can be specific for a defined sequence which is characteristic of a selective polynucleotide, but the other probe can be specific for the selective polynucleotide, or specific for a more general sequence, e.g., a sequence such as polyA which is characteristic of mRNA, a sequence which is specific for a promoter, ribosome binding site, or other transcriptional features, a consensus sequence (e.g., representing a functional domain). For the former aspects, 5′ and 3′ probes (e.g., polyA, Kozak, etc.) are preferred which are capable of specifically hybridizing to the ends of transcripts. When PCR is utilized, the probes can also be referred to as “primers” in that they can prime a DNA polymerase reaction.
In addition to testing for the presence or absence of polynucleotides, the present invention also relates to determining the amounts at which polynucleotides of the present invention are expressed in sample and determining the differential expression of such polynucleotides in samples. Such methods can involve substantially the same steps as described above for presence/absence detection, e.g., contacting with probe, hybridizing, and detecting hybridized probe, but using more quantitative methods and/or comparisons to standards.
The amount of hybridization between the probe and target can be determined by any suitable methods, e.g., PCR, RT-PCR, RACE PCR, Northern blot, polynucleotide microarrays, Rapid-Scan, etc., and includes both quantitative and qualitative measurements. For further details, see the hybridization methods described above and below. Determining by such hybridization whether the target is differentially expressed (e.g., up-regulated or down-regulated) in the sample can also be accomplished by any effective means. For instance, the target's expression pattern in the sample can be compared to its pattern in a known standard, such as in a normal tissue, or it can be compared to another gene in the same sample. When a second sample is utilized for the comparison, it can be a sample of normal tissue that is known not to contain diseased cells. The comparison can be performed on samples which contain the same amount of RNA (such as polyadenylated RNA or total RNA), or, on RNA extracted from the same amounts of starting tissue. Such a second sample can also be referred to as a control or standard. Hybridization can also be compared to a second target in the same tissue sample. Experiments can be performed that determine a ratio between the target nucleic acid and a second nucleic acid (a standard or control), e.g., in a normal tissue. When the ratio between the target and control are substantially the same in a normal and sample, the sample is determined or diagnosed not to contain cells. However, if the ratio is different between the normal and sample tissues, the sample is determined to contain cancer cells. The approaches can be combined, and one or more second samples, or second targets can be used. Any second target nucleic acid can be used as a comparison, including “housekeeping” genes, such as beta-actin, alcohol dehydrogenase, or any other gene whose expression does not vary depending upon the disease status of the cell.
Methods of Identifying Polymorphisms, Mutations, etc., of a Differentially-Regulated Gene
Polynucleotides of the present invention can also be utilized to identify mutant alleles, SNPs, gene rearrangements and modifications, and other polymorphisms of the wild-type gene. Mutant alleles, polymorphisms, SNPs, etc., can be identified and isolated from cancers that are known, or suspected to have, a genetic component. Identification of such genes can be carried out routinely (see, above for more guidance), e.g., using PCR, hybridization techniques, direct sequencing, mismatch reactions (see, e.g., above), RFLP analysis, SSCP (e.g., Orita et al., Proc. Natl. Acad. Sci ., 86:2766, 1992), etc., where a polynucleotide having a sequence selected from SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29 is used as a probe. The selected mutant alleles, SNPs, polymorphisms, etc., can be used diagnostically to determine whether a subject has, or is susceptible to a disorder associated with a differentially-regulated gene, as well as to design therapies and predict the outcome of the disorder. Methods involve, e.g., diagnosing a disorder associated with a differentially-regulated gene or determining susceptibility to a disorder, comprising, detecting the presence of a mutation in a gene represented by a polynucleotide selected from SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29. The detecting can be carried out by any effective method, e.g., obtaining cells from a subject, determining the gene sequence or structure of a target gene (using, e.g., mRNA, cDNA, genomic DNA, etc), comparing the sequence or structure of the target gene to the structure of the normal gene, whereby a difference in sequence or structure indicates a mutation in the gene in the subject. Polynucleotides can also be used to test for mutations, SNPs, polymorphisms, etc., e.g., using mismatch DNA repair technology as described in U.S. Pat. No. 5,683,877; U.S. Pat. No. 5,656,430; Wu et al., Proc. Natl. Acad. Sci ., 89:8779-8783, 1992.
The present invention also relates to methods of detecting polymorphisms in a differentially-regulated gene, comprising, e.g., comparing the structure of: genomic DNA comprising all or part of said gene, mRNA comprising all or part of said gene, cDNA comprising all or part of said gene, or a polypeptide comprising all or part of said gene, with the structure of said gene as set forth herein. The methods can be carried out on a sample from any source, e.g., cells, tissues, body fluids, blood, urine, stool, hair, egg, sperm, etc.
These methods can be implemented in many different ways. For example, “comparing the structure” steps include, but are not limited to, comparing restriction maps, nucleotide sequences, amino acid sequences, RFLPs, DNAse sites, DNA methylation fingerprints (e.g., U.S. Pat. No. 6,214,556), protein cleavage sites, molecular weights, electrophoretic mobilities, charges, ion mobility, etc., between a standard gene and a test gene. The term “structure” can refer to any physical characteristics or configurations which can be used to distinguish between nucleic acids and polypeptides. The methods and instruments used to accomplish the comparing step depends upon the physical characteristics which are to be compared. Thus, various techniques are contemplated, including, e.g., sequencing machines (both amino acid and polynucleotide), electrophoresis, mass spectrometer (U.S. Pat. Nos. 6,093,541, 6,002,127), liquid chromatography, HPLC, etc.
To carry out such methods, “all or part” of the gene or polypeptide can be compared. For example, if nucleotide sequencing is utilized, the entire gene can be sequenced, including promoter, introns, and exons, or only parts of it can be sequenced and compared, e.g., exon 1, exon 2, etc.
Mutagenesis
Mutated polynucleotide sequences of the present invention are useful for various purposes, e.g., to create mutations of the polypeptides they encode, to identify functional regions of genomic DNA, to produce probes for screening libraries, etc. Mutagenesis can be carried out routinely according to any effective method, e.g., oligonucleotide-directed (Smith, M., Ann. Rev. Genet . 19:423-463, 1985), degenerate oligonucleotide-directed (Hill et al., Method Enzymology , 155:558-568, 1987), region-specific (Myers et al., Science , 229:242-246, 1985; Derbyshire et al., Gene , 46:145, 1986; Ner et al., DNA, 7:127, 1988), linker-scanning (McKnight and Kingsbury, Science , 217:316-324, 1982), directed using PCR, recursive ensemble mutagenesis (Arkin and Yourvan, Proc. Natl. Acad. Sci ., 89:7811-7815, 1992), random mutagenesis (e.g., U.S. Pat. Nos. 5,096,815; 5,198,346; and 5,223,409), site-directed mutagenesis (e.g., Walder et al., Gene , 42:133, 1986; Bauer et al., Gene , 37:73, 1985; Craik, Bio Techniques , Jan. 12-19, 1985; Smith et al., Genetic Engineering: Principles and Methods , Plenum Press, 1981), phage display (e.g., Lowman et al., Biochem . 30:10832-10837, 1991; Ladner et al., U.S. Pat. No. 5,223,409; Huse, WIPO Publication WO 92/06204), etc. Desired sequences can also be produced by the assembly of target sequences using mutually priming oligonucleotides (Uhlmann, Gene , 71:29-40, 1988). For directed mutagenesis methods, analysis of the three-dimensional structure of the polypeptide can be used to guide and facilitate making mutants which effect polypeptide activity. Sites of substrate-enzyme interaction or other biological activities can also be determined by analysis of crystal structure as determined by such techniques as nuclear magnetic resonance, crystallography or photoaffinity labeling. See, for example, de Vos et al., Science 255:306-312, 1992; Smith et al., J. Mol. Biol. 224:899-904, 1992; Wlodaver et al., FEBS Lett. 309:59-64, 1992.
In addition, libraries of differentially-regulated genes and fragments thereof can be used for screening and selection of gene variants. For instance, a library of coding sequences can be generated by treating a double-stranded DNA with a nuclease under conditions where the nicking occurs, e.g., only once per molecule, denaturing the double-stranded DNA, renaturing it to for double-stranded DNA that can include sense/antisense pairs from different nicked products, removing single-stranded portions from reformed duplexes by treatment with S1 nuclease, and ligating the resulting DNAs into an expression vecore. By this method, expression libraries can be made comprising “mutagenized” differentially-regulated genes. The entire coding sequence or parts thereof can be used.
Polynucleotide Expression, Polypeptides Produced thereby, and Specific-binding Partners Thereto
A polynucleotide according to the present invention can be expressed in a variety of different systems, in vitro and in vivo, according to the desired purpose. For example, a polynucleotide can be inserted into an expression vector, introduced into a desired host, and cultured under conditions effective to achieve expression of a polypeptide coded for by the polynucleotide, to search for specific binding partners. Effective conditions include any culture conditions which are suitable for achieving production of the polypeptide by the host cell, including effective temperatures, pH, medium, additives to the media in which the host cell is cultured (e.g., additives which amplify or induce expression such as butyrate, or methotrexate if the coding polynucleotide is adjacent to a dhfr gene), cycloheximide, cell densities, culture dishes, etc. A polynucleotide can be introduced into the cell by any effective method including, e.g., naked DNA, calcium phosphate precipitation, electroporation, injection, DEAE-Dextran mediated transfection, fusion with liposomes, association with agents which enhance its uptake into cells, viral transfection. A cell into which a polynucleotide of the present invention has been introduced is a transformed host cell. The polynucleotide can be extrachromosomal or integrated into a chromosome(s) of the host cell. It can be stable or transient. An expression vector is selected for its compatibility with the host cell. Host cells include, mammalian cells, e.g., COS, CV1, BHK, CHO, HeLa, LTK, NIH 3T3, PC-3 (CRL-1435), LNCaP (CRL-1740), CA-HPV-10 (CRL-2220), PZ-HPV-7 (CRL-2221), MDA-PCa 2b (CRL-2422), 22Rvl (CRL2505), NCI-H660 (CRL-5813), HS 804.Sk (CRL-7535), LNCaP-FGF (CRL-10995), RWPE-1 (CRL-11609), RWPE-2 (CRL-11610), PWR-1E (CRL 11611), rat MAT-Ly-LuB-2 (CRL-2376), and other primary and established prostate and prostate cancer cell lines, insect cells, such as Sf9 ( S. frugipeda ) and Drosophila , bacteria, such as E. coli, Streptococcus, bacillus , yeast, such as Sacharomyces, S. cerevisiae , fungal cells, plant cells, embryonic or adult stem cells (e.g., mammalian, such as mouse or human).
Expression control sequences are similarly selected for host compatibility and a desired purpose, e.g., high copy number, high amounts, induction, amplification, controlled expression. Other sequences which can be employed include enhancers such as from SV40, CMV, RSV, inducible promoters, cell-type specific elements, or sequences which allow selective or specific cell expression. Promoters that can be used to drive its expression, include, e.g., the endogenous promoter, MMTV, SV40, trp, lac, tac, or T7 promoters for bacterial hosts; or alpha factor, alcohol oxidase, or PGH promoters for yeast. RNA promoters can be used to produced RNA transcripts, such as T7 or SP6. See, e.g., Melton et al., Polynucleotide Res ., 12(18):7035-7056, 1984; Dunn and Studier. J Mol. Bio ., 166:477-435, 1984; U.S. Pat. No. 5,891,636; Studier et al., Gene Expression Technology, Methods in Enzymology , 85:60-89, 1987. In addition, as discussed above, translational signals (including in-frame insertions) can be included.
When a polynucleotide is expressed as a heterologous gene in a transfected cell line, the gene is introduced into a cell as described above, under effective conditions in which the gene is expressed. The term “heterologous” means that the gene has been introduced into the cell line by the “hand-of-man.” Introduction of a gene into a cell line is discussed above. The transfected (or transformed) cell expressing the gene can be lysed or the cell line can be used intact.
For expression and other purposes, a polynucleotide can contain codons found in a naturally-occurring gene, transcript, or cDNA, for example, e.g., as set forth in SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29, or it can contain degenerate codons coding for the same amino acid sequences. For instance, it may be desirable to change the codons in the sequence to optimize the sequence for expression in a desired host. See, e.g., U.S. Pat. Nos. 5,567,600 and 5,567,862.
A polypeptide according to the present invention can be recovered from natural sources, transformed host cells (culture medium or cells) according to the usual methods, including, detergent extraction (e.g., non-ionic detergent, Triton X-100, CHAPS, octylglucoside, Igepal CA-630), ammonium sulfate or ethanol precipitation, acid extraction, anion or cation exchange chromatography, phosphocellulose chromatography, hydrophobic interaction chromatography, hydroxyapatite chromatography, lectin chromatography, gel electrophoresis. Protein refolding steps can be used, as necessary, in completing the configuration of the mature protein. Finally, high performance liquid chromatography (HPLC) can be employed for purification steps. Another approach is express the polypeptide recombinantly with an affinity tag (Flag epitope, HA epitope, myc epitope, 6×His, maltose binding protein, chitinase, etc) and then purify by anti-tag antibody-conjugated affinity chromatography.
The present invention also relates to antibodies, and other specific-binding partners, which are specific for polypeptides encoded by polynucleotides of the present invention. Antibodies, e.g., polyclonal, monoclonal, recombinant, chimeric, humanized, single-chain, Fab, and fragments thereof, can be prepared according to any desired method. See, also, screening recombinant immunoglobulin libraries (e.g., Orlandi et al., Proc. Natl. Acad. Sci ., 86:3833-3837, 1989; Huse et al., Science , 256:1275-1281, 1989); in vitro stimulation of lymphocyte populations; Winter and Milstein, Nature , 349: 293-299, 1991. The antibodies can be Ig, IgG, subtypes, IgG2a, IgG1, etc. Antibodies, and immune responses, can also be generated by administering naked DNA See, e.g., U.S. Pat. Nos. 5,703,055; 5,589,466; 5,580,859. Antibodies can be used from any source, including, goat, rabbit, mouse, chicken (e.g., IgY; see, Duan, W0/029444 for methods of making antibodies in avian hosts, and harvesting the antibodies from the eggs). An antibody specific for a polypeptide means that the antibody recognizes a defined sequence of amino acids within or including the polypeptide. Other specific binding partners include, e.g., aptamers and PNA, can be prepared against specific epitopes or domains of differentially regulated genes.
The preparation of polyclonal antibodies is well-known to those skilled in the art. See, for example, Green et al., Production of Polyclonal Antisera, in IMMUNOCHEMICAL PROTOCOLS (Manson, ed.), pages 1-5 (Humana Press 1992); Coligan et al., Production of Polyclonal Antisera in Rabbits, Rats, Mice and Hamsters, in CURRENT PROTOCOLS IN IMMUNOLOGY, section 2.4.1 (1992). The preparation of monoclonal antibodies likewise is conventional. See, for example, Kohler & Milstein, Nature 256:495 (1975); Coligan et al., sections 2.5.1-2.6.7; and Harlow et al., ANTIBODIES: A LABORATORY MANUAL, page 726 (Cold Spring Harbor Pub. 1988).
Antibodies can also be humanized, e.g., where they are to be used therapeutically. Humanized monoclonal antibodies are produced by transferring mouse complementarity determining regions from heavy and light variable chains of the mouse immunoglobulin into a human variable domain, and then substituting human residues in the framework regions of the murine counterparts. The use of antibody components derived from humanized monoclonal antibodies obviates potential problems associated with the immunogenicity of murine constant regions. General techniques for cloning murine immunoglobulin variable domains are described, for example, by Orlandi et al., Proc. Nat'l Acad. Sci. USA 86:3833 (1989), which is hereby incorporated in its entirety by reference. Techniques for producing humanized monoclonal antibodies are described, for example, in U.S. Pat. No. 6,054,297, Jones et al., Nature 321: 522 (1986); Riechmann et al., Nature 332: 323 (1988); Verhoeyen et al., Science 239: 1534 (1988); Carter et al., Proc. Nat'l Acad. Sci. USA 89: 4285 (1992); Sandhu, Crit. Rev. Biotech. 12: 437 (1992); and Singer et al., J. Immunol. 150: 2844 (1993).
Antibodies of the invention also may be derived from human antibody fragments isolated from a combinatorial immunoglobulin library. See, for example, Barbas et al., METHODS: A COMPANION TO METHODS IN ENZYMOLOGY, VOL. 2, page 119 (1991); Winter et al., Ann. Rev. Immunol. 12:433 (1994). Cloning and expression vectors that are useful for producing a human immunoglobulin phage library can be obtained commercially, for example, from STRATAGENE Cloning Systems (La Jolla, Calif.).
In addition, antibodies of the present invention may be derived from a human monoclonal antibody. Such antibodies are obtained from transgenic mice that have been “engineered” to produce specific human antibodies in response to antigenic challenge. In this technique, elements of the human heavy and light chain loci are introduced into strains of mice derived from embryonic stem cell lines that contain targeted disruptions of the endogenous heavy and light chain loci. The transgenic mice can synthesize human antibodies specific for human antigens and can be used to produce human antibody-secreting hybridomas. Methods for obtaining human antibodies from transgenic mice are described, e.g., in Green et al., Nature Genet. 7:13 (1994); Lonberg et al., Nature 368:856 (1994); and Taylor et al., Int. Immunol. 6:579 (1994).
Antibody fragments of the present invention can be prepared by proteolytic hydrolysis of the antibody or by expression in E. coli of nucleic acid encoding the fragment. Antibody fragments can be obtained by pepsin or papain digestion of whole antibodies by conventional methods. For example, antibody fragments can be produced by enzymatic cleavage of antibodies with pepsin to provide a 5S fragment denoted F(ab′).sub.2. This fragment can be further cleaved using a thiol reducing agent, and optionally a blocking group for the sulfhydryl groups resulting from cleavage of disulfide linkages, to produce 3.5S Fab′ monovalent fragments. Alternatively, an enzymatic cleavage using pepsin produces two monovalent Fab′ fragments and an Fc fragment directly. These methods are described, for example, by Goldenberg, U.S. Pat. Nos. 4,036,945 and 4,331,647, and references contained therein. These patents are hereby incorporated in their entireties by reference. See also Nisoiihoff et al., Arch. Biochem. Biophys. 89:230 (1960); Porter, Biochem. J. 73:119 (1959); Edelman et al, METHODS IN ENZYMOLOGY, VOL. 1, page 422 (Academic Press 1967); and Coligan et al. at sections 2.8.1-2.8.10 and 2.10.1-2.10.4.
Other methods of cleaving antibodies, such as separation of heavy chains to form monovalent light-heavy chain fragments, further cleavage of fragments, or other enzymatic, chemical, or genetic techniques can also be used. For example, Fv fragments comprise an association of V.sub.H and V.sub.L chains. This association may be noncovalent, as described in Inbar et al., Proc. Nat'l Acad. Sci. USA 69:2659 (1972). Alternatively, the variable chains can be linked by an intermolecular disulfide bond or cross-linked by chemicals such as glutaraldehyde. See, e.g., Sandhu, supra. Preferably, the Fv fragments comprise V.sub.H and V.sub.L chains connected by a peptide linker. These single-chain antigen binding proteins (sFv) are prepared by constructing a structural gene comprising nucleic acid sequences encoding the V.sub.H and V.sub.L domains connected by an oligonucleotide. The structural gene is inserted into an expression vector, which is subsequently introduced into a host cell such as E. coli . The recombinant host cells synthesize a single polypeptide chain with a linker peptide bridging the two V domains. Methods for producing sFvs are described, for example, by Whitlow et al., METHODS: A COMPANION TO METHODS IN ENZYMOLOGY, VOL. 2, page 97 (1991); Bird et al., Science 242:423-426 (1988); Ladneret al., U.S. Pat. No. 4,946,778; Pack et al., Bio/Technology 11:1271-77 (1993); and Sandhu, supra.
Another form of an antibody fragment is a peptide coding for a single complementarity-determining region (CDR). CDR peptides (“minimal recognition units”) can be obtained by constructing genes encoding the CDR of an antibody of interest. Such genes are prepared, for example, by using the polymerase chain reaction to synthesize the variable region from RNA of antibody-producing cells. See, for example, Larrick et al., METHODS: A COMPANION TO METHODS IN ENZYMOLOGY, VOL. 2, page 106 (1991).
The term “antibody” as used herein includes intact molecules as well as fragments thereof, such as Fab, F(ab′)2, and Fv which are capable of binding to an epitopic determinant present in Bin1 polypeptide. Such antibody fragments retain some ability to selectively bind with its antigen or receptor. The term “epitope” refers to an antigenic determinant on an antigen to which the paratope of an antibody binds. Epitopic determinants usually consist of chemically active surface groupings of molecules such as amino acids or sugar side chains and usually have specific three dimensional structural characteristics, as well as specific charge characteristics. Antibodies can be prepared against specific epitopes or polypeptide domains.
Antibodies which bind to a differentially-regulated polypeptide of the present invention can be prepared using an intact polypeptide or fragments containing small peptides of interest as the immunizing antigen. For example, it may be desirable to produce antibodies that specifically bind to the N- or C-terminal domains of said polypeptide. The polypeptide or peptide used to immunize an animal which is derived from translated cDNA or chemically synthesized which can be conjugated to a carrier protein, if desired. Such commonly used carriers which are chemically coupled to the immunizing peptide include keyhole limpet hemocyanin (KLH), thyroglobulin, bovine serum albumin (BSA), and tetanus toxoid.
Polyclonal or monoclonal antibodies can be further purified, for example, by binding to and elution from a matrix to which the polypeptide or a peptide to which the antibodies were raised is bound. Those of skill in the art will know of various techniques common in the immunology arts for purification and/or concentration of polyclonal antibodies, as well as monoclonal antibodies (See for example, Coligan, et al., Unit 9 , Current Protocols in Immunology , Wiley Interscience, 1994, incorporated by reference).
Anti-idiotype technology can also be used to produce invention monoclonal antibodies which mimic an epitope. For example, an anti-idiotypic monoclonal antibody made to a first monoclonal antibody will have a binding domain in the hypervariable region which is the “image” of the epitope bound by the first monoclonal antibody.
Methods of Detecting Polypeptides
Polypeptides coded for by a differentially-regulated gene of the present invention can be detected, visualized, determined, quantitated, etc. according to any effective method. useful methods include, e.g., but are not limited to, immunoassays, RIA (radioimmunassay), ELISA, (enzyme-linked-immunosorbent assay), immunoflourescence, flow cytometry, histology, electron microscopy, light microscopy, in situ assays, immunoprecipitation, Western blot, etc.
Immunoassays may be carried in liquid or on biological support. For instance, a sample (e.g., blood, stool, urine, cells, tissue, body fluids, etc.) can be brought in contact with and immobilized onto a solid phase support or carrier such as nitrocellulose, or other solid support that is capable of immobilizing cells, cell particles or soluble proteins. The support may then be washed with suitable buffers followed by treatment with the detectably labeled differentially-regulated gene specific antibody. The solid phase support can then be washed with a buffer a second time to remove unbound antibody. The amount of bound label on solid support may then be detected by conventional means.
A “solid phase support or carrier” includes any support capable of binding an antigen, antibody, or other specific binding partner. Supports or carriers include glass, polystyrene, polypropylene, polyethylene, dextran, nylon, amylases, natural and modified celluloses, polyacrylamides, and magnetite. A support material can have any structural or physical configuration. Thus, the support configuration may be spherical, as in a bead, or cylindrical, as in the inside surface of a test tube, or the external surface of a rod. Alternatively, the surface may be flat such as a sheet, test strip, etc. Preferred supports include polystyrene beads
One of the many ways in which gene peptide-specific antibody can be detectably labeled is by linking it to an enzyme and using it in an enzyme immunoassay (EIA). See, e.g., Voller, A., “The Enzyme Linked Immunosorbent Assay (ELISA),” 1978, Diagnostic Horizons 2, 1-7, Microbiological Associates Quarterly Publication, Walkersville, Md.); Voller, A. et al., 1978, J. Clin. Pathol. 31, 507-520; Butler, J. E., 1981, Meth. Enzymol. 73, 482-523; Maggio, E. (ed.), 1980, Enzyme Immunoassay, CRC Press, Boca Raton, Fla. The enzyme which is bound to the antibody will react with an appropriate substrate, preferably a chromogenic substrate, in such a manner as to produce a chemical moiety that can be detected, for example, by spectrophotometric, fluorimetric or by visual means. Enzymes that can be used to detectably label the antibody include, but are not limited to, malate dehydrogenase, staphylococcal nuclease, delta-5-steroid isomerase, yeast alcohol dehydrogenase, .alpha.-glycerophosphate, dehydrogenase, triose phosphate isomerase, horseradish peroxidase, alkaline phosphatase, asparaginase, glucose oxidase, .beta.-galactosidase, ribonuclease, urease, catalase, glucose-6-phosphate dehydrogenase, glucoamylase and acetylcholinesterase. The detection can be accomplished by calorimetric methods that employ a chromogenic substrate for the enzyme. Detection may also be accomplished by visual comparison of the extent of enzymatic reaction of a substrate in comparison with similarly prepared standards.
Detection may also be accomplished using any of a variety of other immunoassays. For example, by radioactively labeling the antibodies or antibody fragments, it is possible to detect differentially-regulated peptides through the use of a radioimmunoassay (RIA). See, e.g., Weintraub, B., Principles of Radioimmunoassays, Seventh Training Course on Radioligand Assay Techniques, The Endocrine Society, March, 1986. The radioactive isotope can be detected by such means as the use of a gamma counter or a scintillation counter or by autoradiography.
It is also possible to label the antibody with a fluorescent compound. When the fluorescently labeled antibody is exposed to light of the proper wave length, its presence can then be detected due to fluorescence. Among the most commonly used fluorescent labeling compounds are fluorescein isothiocyanate, rhodamine, phycoerythrin, phycocyanin, allophycocyanin, o-phthaldehyde and fluorescamine. The antibody can also be detectably labeled using fluorescence emitting metals such as those in the lanthanide series. These metals can be attached to the antibody using such metal chelating groups as diethylenetriaminepentacetic acid (DTPA) or ethylenediaminetetraacetic acid (EDTA).
The antibody also can be detectably labeled by coupling it to a chemiluminescent compound. The presence of the chemiluminescent-tagged antibody is then determined by detecting the presence of luminescence that arises during the course of a chemical reaction. Examples of useful chemiluminescent labeling compounds are luminol, isoluminol, theromatic acridinium ester, imidazole, acridinium salt and oxalate ester.
Likewise, a bioluminescent compound may be used to label the antibody of the present invention. Bioluminescence is a type of chemiluminescence found in biological systems in which a catalytic protein increases the efficiency of the chemiluminescent reaction. The presence of a bioluminescent protein is determined by detecting the presence of luminescence. Important bioluminescent compounds for purposes of labeling are luciferin, luciferase and aequorin.
Tissue and Disease
Tissue and Disease
The prostate is a secretory organ surrounding the neck of the bladder and urethra. Its primary function is to produce fluids and other materials necessary for sperm transport and maintenance. Structurally, it has both glandular and nonglandular components. The glandular component is predominantly comprised of ducts and acini responsible for the production and transport prostatic fluids. Epithelial cells are the main identifiable cell found in these regions, primarily of the basal and secretory types, but also endocrine-paracrine and transitional epithelial. The non-glandular component contains the capsular and muscle tissues, which, respectively, hold the organ together and function in fluid discharge. See, e.g., Histology for Pathologists , Sternberg, S. S., editor, Raven Press, NY, 1992, Chapter 40.
The major diseases of the prostate include, e.g., prostatic hyperplasia (BPH), prostatitis, and prostate cancer (e.g., prostatic adenocarcinoma). BPH is a benign, proliferative disease of the prostatic epithelial cells. While it may cause urinary tract obstruction in some patients, for the most part, it is generally asymptomatic. Prostate cancer, on the other hand, is the most common form of cancer in white males in the United States, occurring predominantly in males over age 50. The prevalence of prostate diseases, such as prostate cancer, has made the discovery of prostate selective markers and gene expression patterns of great importance.
The most common scale of assessing prostate pathology is the Gleason grading system. See, e.g., Bostwick, Am. J. Clin. Path ., 102: s38-s56, 1994. Once the cancer is identified, staging can assess the size, location, and extent of the cancer. Several different staging scales are commonly used, including stages A-D, and Tumor-Nodes-Metastases (TNM). For treatment, diagnosis, staging, etc., of prostate conditions, methods can be carried out analogously to, and in combination with, U.S. Pat. Nos. 6,107,090; 6,057,116; 6,034,218; 6,004,267; 5,919,638; 5,882,864; 5,763,202; 5,747,264; 5,688,649; 5,552,277.
In addition, the present invention relates to methods of assessing a therapeutic or preventative intervention in a subject having a prostate cancer, comprising, e.g., detecting the expression levels of differentially-regulated target genes, wherein the target genes comprise a gene which is represented by a sequence selected from Tables 1 and 2, or, a gene represented by a sequence having 95% sequence identity or more to a sequence selected from Tables 1 and 2. By “therapeutic or preventative intervention,” it is meant, e.g., a drug administered a patient, surgery, radiation, chemotherapy, and other measures taken to prevent a cancer or treat a cancer.
Grading, Staging, Comparing, Assessing, Methods and Compositions
The present invention also relates to methods and compositions for staging and grading cancers. As already defined, staging relates to determining the extent of a cancer's spread, including its size and the degree to which other tissues, such as lymph nodes are involved in the cancer. Grading refers to the degree of a cell's retention of the characteristics of the tissue of its origin. A lower grade cancer comprises tumor cells that more closely resemble normal cells than a medium or higher grade cancer. Grading can be a useful diagnostic and prognostic tool. Higher grade cancers usually behave more aggressively than lower grade cancers. Thus, knowledge of the cancer grade, as well as its stage, can be a significant factor in the choice of the appropriate therapeutic intervention for the particular patient, e.g., surgery, radiation, chemotherapy, etc. Staging and grading can also be used in conjunction with a therapy to assess its efficacy, to determine prognosis, to determine effective dosages, etc.
Various methods of staging and grading cancers can be employed in accordance with the present invention. A “cell expression profile” or “cell expression fingerprint” is a representation of the expression of various different genes in a given cell or sample comprising cells. These cell expression profiles can be useful as reference standards. The cell expression fingerprints can be used alone for grading, or in combination with other grading methods.
The present invention also relates to methods and compositions for diagnosing a prostate cancer, or determining susceptibility to a prostate cancer, using polynucleotides, polypeptides, and specific-binding partners of the present invention to detect, assess, determine, etc., differentially-regulated genes of the present invention. In such methods, the gene can serve as a marker for prostate cancer, e.g., where the gene, when mutant, is a direct cause of the prostate cancer; where the gene is affected by another gene(s) which is directly responsible for the prostate cancer, e.g., when the gene is part of the same signaling pathway as the directly responsible gene; and, where the gene is chromosomally linked to the gene(s) directly responsible for the prostate cancer, and segregates with it. Many other situations are possible. To detect, assess, determine, etc., a probe specific for the gene can be employed as described above and below. Any method of detecting and/or assessing the gene can be used, including detecting expression of the gene using polynucleotides, antibodies, or other specific-binding partners.
The present invention relates to methods of diagnosing a disorder associated with prostate cancer, or determining a subject's susceptibility to such prostate cancer, comprising, e.g., assessing the expression of a differentially-regulated gene in a tissue sample comprising tissue or cells suspected of having a prostate cancer (e.g., where the sample comprises prostate). The phrase “diagnosing” indicates that it is determined whether the sample has prostate cancer. “Determining a subject's susceptibility to a prostate cancer” indicates that the subject is assessed for whether s/he is predisposed to get such a disease or disorder, where the predisposition is indicated by abnormal expression of the gene (e.g., gene mutation, gene expression pattern is not normal, etc.). Predisposition or susceptibility to a disease may result when a such disease is influenced by epigenetic, environmental, etc., factors. This includes prenatal screening where samples from the fetus or embryo (e.g., via amniocentesis or CV sampling) are analyzed for the expression of the genes.
By the phrase “assessing expression of a differentially-regulated gene,” it is meant that the functional status of the gene is evaluated. This includes, but is not limited to, measuring expression levels of said gene, determining the genomic structure of said gene, determining the mRNA structure of transcripts from said gene, or measuring the expression levels of polypeptide coded for by said gene. Thus, the term “assessing expression” includes evaluating the all aspects of the transcriptional and translational machinery of the gene. For instance, if a promoter defect causes, or is suspected of causing, the disorder, then a sample can be evaluated (i.e., “assessed”) by looking (e.g., sequencing or restriction mapping) at the promoter sequence in the gene, by detecting transcription products (e.g., RNA), by detecting translation product (e.g., polypeptide). Any measure of whether the gene is functional can be used, including, polypeptide, polynucleotide, and functional assays for the gene's biological activity.
In making the assessment, it can be useful to compare the results to a normal gene, e.g., a gene which is not associated with the disorder. The nature of the comparison can be determined routinely, depending upon how the assessing is accomplished. If, for example, the mRNA levels of a sample is detected, then the mRNA levels of a normal can serve as a comparison, or a gene which is known not to be affected by the disorder. Methods of detecting mRNA are well known, and discussed above, e.g., but not limited to, Northern blot analysis, polymerase chain reaction (PCR), reverse transcriptase PCR, RACE PCR, etc. Similarly, if polypeptide production is used to evaluate the gene, then the polypeptide in a normal tissue sample can be used as a comparison, or, polypeptide from a different gene whose expression is known not to be affected by the disorder. These are only examples of how such a method could be carried out.
Assessing the effects of therapeutic and preventative interventions (e.g., administration of a drug, chemotherapy, radiation, etc.) on prostate cancer is a major effort in drug discovery, clinical medicine, and pharmacogenomics. The evaluation of therapeutic and preventative measures, whether experimental or already in clinical use, has broad applicability, e.g., in clinical trials, for monitoring the status of a patient, for analyzing and assessing animal models, and in any scenario involving cancer treatment and prevention. Analyzing the expression profiles of polynucleotides of the present invention can be utilized as a parameter by which interventions are judged and measured. Treatment of a disorder can change the expression profile in some manner which is prognostic or indicative of the drug's effect on it. Changes in the profile can indicate, e.g., drug toxicity, return to a normal level, etc. Accordingly, the present invention also relates to methods of monitoring or assessing a therapeutic or preventative measure (e.g., chemotherapy, radiation, anti-neoplastic drugs, antibodies, etc.) in a subject having prostate cancer, or, susceptible to such a disorder, comprising, e.g., detecting the expression levels of one or more differentially-regulated genes of the present invention. A subject can be a cell-based assay system, non-human animal model, human patient, etc. Detecting can be accomplished as described for the methods above and below. By “therapeutic or preventative intervention,” it is meant, e.g., a drug administered to a patient, surgery, radiation, chemotherapy, and other measures taken to prevent, treat, or diagnose prostate cancer.
Expression can be assessed in any sample comprising any tissue or cell type, body fluid, etc., as discussed for other methods of the present invention, including cells from prostate can be used, or cells derived from prostate. By the phrase “cells derived from prostate,” it is meant that the derived cells originate from prostate, e.g., when metastasis from a primary tumor site has occurred, when a progenitor-type or pluripotent cell gives rise to other cells, etc.
The present invention also relates to methods of using binding partners for differentially-regulated genes, such as antibodies, to deliver active agents to the prostate for a variety of different purposes, including, e.g., for diagnostic, therapeutic (e.g., to treat cancer), and research purposes. Methods can involve delivering or administering an active agent to the prostate, comprising, e.g., administering to a subject in need thereof, an effective amount of an active agent coupled to a binding partner specific for a idfferentially-regulated gene polypeptide, wherein said binding partner is effective to deliver said active agent specifically to prostate.
Any type of active agent can be used in combination with the binding partner, including, therapeutic, cytotoxic, cytostatic, chemotherapeutic, anti-neoplastic, anti-proliferative, anti-biotic, etc., agents. A chemotherapeutic agent can be, e.g., DNA-interactive agent, alkylating agent, antimetabolite, tubulin-interactive agent, hormonal agent, hydroxyurea, Cisplatin, Cyclophosphamide, Altretamine, Bleomycin, Dactinomycin, Doxorubicin, Etoposide, Teniposide, paclitaxel, cytoxan, 2-methoxycarbonylaminobenzimidazole, Plicamycin, Methotrexate, Fluorouracil, Fluorodeoxyuridin, CB3717, Azacitidine, Floxuridine, Mercapyopurine, 6-Thioguanine, Pentostatin, Cytarabine, Fludarabine, etc. Agents can also be contrast agents useful in imaging technology, e.g., X-ray, CT, CAT, MRI, ultrasound, PET, SPECT, and scintographic.
An active agent can be associated in any manner with a binding partner which is effective to achieve its delivery specifically to the target. Specific delivery or targeting indicates that the agent is provided to the prostate, without being substantially provided to other tissues. This is useful especially where an agent is toxic, and specific targeting to the prostate enables the majority of the toxicity to be aimed at the prostate, with as small as possible effect on other tissues in the body. The association of the active agent and the binding partner (“coupling) can be direct, e.g., through chemical bonds between the binding partner and the agent, or, via a linking agent, or the association can be less direct, e.g., where the active agent is in a liposome, or other carrier, and the binding partner is associated with the liposome surface. In such case, the binding partner can be oriented in such a way that it is able to bind to the gene product on prostate cell surface. Methods for delivery of DNA via a cell-surface receptor is described, e.g., in U.S. Pat. No. 6,339,139.
Identifying Agent Methods
The present invention also relates to methods of identifying agents, and the agents themselves, which modulate differentially regulated genes and gene products of the present invention. These agents can be used to modulate the biological activity of the polypeptide encoded for the gene, or the gene, itself. Agents which regulate the gene or its product are useful in variety of different environments, including as medicinal agents to treat or prevent disorders associated with differentially regulated genes and as research reagents to modify the function of tissues and cell.
Methods of identifying agents generally comprise steps in which an agent is placed in contact with the gene, transcription product, translation product, or other target, and then a determination is performed to assess whether the agent “modulates” the target. The specific method utilized will depend upon a number of factors, including, e.g., the target (i.e., is it the gene or polypeptide encoded by it), the environment (e.g., in vitro or in vivo), the composition of the agent, etc.
For modulating the expression of differentially-regulated genes of the present invention, a method can comprise, in any effective order, one or more of the following steps, e.g., contacting a differentially-regulated gene (e.g., in a cell population) with a test agent under conditions effective for said test agent to modulate the expression of said gene, and determining whether said test agent modulates said gene. An agent can modulate expression of a differentially-regulated gene at any level, including transcription, translation, and/or perdurance of the nucleic acid (e.g., degradation, stability, etc.) in the cell. For modulating the biological activity of polypeptides coded for by differentially-regulated genes, a method can comprise, in any effective order, one or more of the following steps, e.g., contacting a polypeptide (e.g., in a cell, lysate, or isolated) with a test agent under conditions effective for said test agent to modulate the biological activity of said polypeptide, and determining whether said test agent modulates said biological activity.
Contacting a differentially-regulated gene or polypeptide with the test agent can be accomplished by any suitable method and/or means that places the agent in a position to functionally control expression or biological activity of said gene or polypeptide present in the sample. Functional control indicates that the agent can exert its physiological effect on the gene or polypeptide through whatever mechanism it works. The choice of the method and/or means can depend upon the nature of the agent and the condition and type of environment in which the gene or polypeptide is presented, e.g., lysate, isolated, or in a cell population (such as, in vivo, in vitro, organ explants, etc.). For instance, if the cell population is an in vitro cell culture, the agent can be contacted with the cells by adding it directly into the culture medium. If the agent cannot dissolve readily in an aqueous medium, it can be incorporated into liposomes, or another lipophilic carrier, and then administered to the cell culture. Contact can also be facilitated by incorporation of agent with carriers and delivery molecules and complexes, by injection, by infusion, etc.
After the agent has been administered in such a way that it can gain access to the gene or polypeptide, it can be determined whether the test agent modulates their expression or biological activity. Modulation can be of any type, quality, or quantity, e.g., increase, facilitate, enhance, up-regulate, stimulate, activate, amplify, augment, induce, decrease, down-regulate, diminish, lessen, reduce, etc. The modulatory quantity can also encompass any value, e.g., 1%, 5%, 10%, 50%, 75%, 1-fold, 2-fold, 5-fold, 10-fold, 100-fold, etc. To modulate gene expression means, e.g., that the test agent has an effect on its expression, e.g., to effect the amount of transcription, to effect RNA splicing, to effect translation of the RNA into polypeptide, to effect RNA or polypeptide stability, to effect polyadenylation or other processing of the RNA, to effect post-transcriptional or post-translational processing, etc. To modulate biological activity means, e.g., that a functional activity of the polypeptide is changed in comparison to its normal activity in the absence of the agent. This effect includes, increase, decrease, block, inhibit, enhance, etc.
A test agent can be of any molecular composition, e.g., chemical compounds, biomolecules, such as polypeptides, lipids, nucleic acids (e.g., antisense to a polynucleotide sequence selected from SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29), carbohydrates, antibodies, ribozymes, double-stranded RNA, aptamers, etc. For example, if a polypeptide to be modulated is a cell-surface molecule, a test agent can be an antibody that specifically recognizes it and, e.g., causes the polypeptide to be internalized, leading to its down regulation on the surface of the cell. Such an effect does not have to be permanent, but can require the presence of the antibody to continue the down-regulatory effect. Antibodies can also be used to modulate the biological activity a polypeptide in a lysate or other cell-free form. Antisense can also be used as test agents to modulate gene expression.
Markers
The polynucleotides of the present invention can be used with other markers, especially prostate and prostate cancer markers to identity, detect, stage, diagnosis, determine, prognosticate, treat, etc., tissue, diseases and conditions, etc, of the prostate. Markers can be polynucleotides, polypeptides, antibodies, ligands, specific binding partners, etc.
A number of genes and gene products have been identified which are associated with prostate cancer metastasis and/or progression, e.g., PSA, KAI1 (shows decreased expression in metastatic cells; Dong et al., Science , 268:884-6, 1995), D44 isoforms (differentially-regulated during carcinoma progression; Noordzij et al., Clin. Cancer Res ., 3:805-15, 1997), p53 (Effert et al., J Urol ., 150:257-61, 1993), Rb, CDKN2, E-cadherin, PTEN (Hamilton et al., Br. J. Cancer , 82:1671-6, 2000; Dong et al., Clin. Cancer Res ., 7:304-308, 2001), bcl-2, prostatic acid phosphatase (PAP), prostate specific membrane antigen (e.g., U.S. Pat. Nos. 5,538,866 and 6,107,090), Smad3 (e.g., Kang et al., Proc. Natl. Acad. Sci ., 98:3018-3023, 2001), TGF-beta, and other oncogenes and tumor suppressor genes. See, also, Myers and Grizzle, Eur. Urol ., 30:153-166, 1996, for other biomarkers associated with prostatic carcinoma, such as PCNA, p185-erbB-2, p180erbB-3, TAG-72, nm23-H1 and FASE. Such markers can be used in combination with the methods of the present invention to facilitate identifying, grading, staging, prognostication, etc, of conditions and diseases of the prostate.
Therapeutics
Selective polynucleotides, polypeptides, and specific-binding partners thereto, can be utilized in therapeutic applications, especially to treat prostate cancer. Useful methods include, but are not limited to, immunotherapy (e.g., using specific-binding partners to polypeptides), vaccination (e.g., using a selective polypeptide or a naked DNA encoding such polypeptide), protein or polypeptide replacement therapy, gene therapy (e.g., germ-line correction, antisense), etc.
Various immunotherapeutic approaches can be used. For instance, unlabeled antibody that specifically recognizes a tissue-specific antigen can be used to stimulate the body to destroy or attack the cancer, to cause down-regulation, to produce complement-mediated lysis, to inhibit cell growth, etc., of target cells which display the antigen, e.g., analogously to how c-erbB-2 antibodies are used to treat breast cancer. In addition, antibody can be labeled or conjugated to enhance its deleterious effect, e.g., with radionuclides and other energy emitting entitities, toxins, such as ricin, exotoxin A (ETA), and diphtheria, cytotoxic or cytostatic agents, immunomodulators, chemotherapeutic agents, etc. See, e.g., U.S. Pat. No. 6,107,090.
An antibody or other specific-binding partner can be conjugated to a second molecule, such as a cytotoxic agent, and used for targeting the second molecule to a tissue-antigen positive cell (Vitetta, E. S. et al., 1993, Immunotoxin therapy, in DeVita, Jr., V. T. et al., eds, Cancer: Principles and Practice of Oncology, 4th ed., J. B. Lippincott Co., Philadelphia, 2624-2636). Examples of cytotoxic agents include, but are not limited to, antimetabolites, alkylating agents, anthracyclines, antibiotics, anti-mitotic agents, radioisotopes and chemotherapeutic agents. Further examples of cytotoxic agents include, but are not limited to ricin, doxorubicin, daunorubicin, taxol, ethidium bromide, mitomycin, etoposide, tenoposide, vincristine, vinblastine, colchicine, dihydroxy anthracin dione, actinomycin D, 1-dehydrotestosterone, diptheria toxin, Pseudomonas exotoxin (PE) A, PE40, abrin, elongation factor-2 and glucocorticoid. Techniques for conjugating therapeutic agents to antibodies are well.
In addition to immunotherapy, polynucleotides and polypeptides can be used as targets for non-immunotherapeutic applications, e.g., using compounds which interfere with function, expression (e.g., antisense as a therapeutic agent), assembly, etc. RNA interference can be used in vivtro and in vivo to silence differentially-expressed genes when its expression contributes to a disease (but also for other purposes, e.g., to identify the gene's function to change a developmental pathway of a cell, etc.). See, e.g., Sharp and Zamore, Science , 287:2431-2433, 2001; Grishok et al., Science , 287:2494, 2001.
Delivery of therapeutic agents can be achieved according to any effective method, including, liposomes, viruses, plasmid vectors, bacterial delivery systems, orally, systemically, etc. Therapeutic agents of the present invention can be administered in any form by any effective route, including, e.g., oral, parenteral, enteral, intraperitoneal, topical, transdermal (e.g., using any standard patch), ophthalmic, nasally, local, non-oral, such as aerosal, inhalation, subcutaneous, intramuscular, buccal, sublingual, rectal, vaginal, intra-arterial, and intrathecal, etc. They can be administered alone, or in combination with any ingredient(s), active or inactive.
In addition to therapeutics, per se, the present invention also relates to methods of treating prostate cancer showing altered expression of differentially-regulated genes, such as SEQ ID NOS 1-30, comprising, e.g., administering to a subject in need thereof a therapeutic agent which is effective for regulating expression of said genes and/or which is effective in treating said disease. The term “treating” is used conventionally, e.g., the management or care of a subject for the purpose of combating, alleviating, reducing, relieving, improving the condition of, etc., of a disease or disorder. By the phrase “altered expression,” it is meant that the disease is associated with a mutation in the gene, or any modification to the gene (or corresponding product) which affects its normal function. Thus, expression of a differentially-regulated gene refers to, e.g., transcription, translation, splicing, stability of the mRNA or protein product, activity of the gene product, differential expression, etc.
Any agent which “treats” the disease can be used. Such an agent can be one which regulates the expression of the gene. Expression refers to the same acts already mentioned, e.g. transcription, translation, splicing, stability of the mRNA or protein product, activity of the gene product, differential expression, etc. For instance, if the condition was a result of a complete deficiency of the gene product, administration of gene product to a patient would be said to treat the disease and regulate the gene's expression. Many other possible situations are possible, e.g., where the gene is aberrantly expressed, and the therapeutic agent regulates the aberrant expression by restoring its normal expression pattern.
Antisense
Antisense polynucleotide (e.g., RNA) can also be prepared from a polynucleotide according to the present invention, preferably an anti-sense to a sequence of SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29. Antisense polynucleotide can be used in various ways, such as to regulate or modulate expression of the polypeptides they encode, e.g., inhibit their expression, for in situ hybridization, for therapeutic purposes, for making targeted mutations (in vivo, triplex, etc.) etc. For guidance on administering and designing anti-sense, see, e.g., U.S. Pat. Nos. 6,200,960, 6,200,807, 6,197,584, 6,190,869, 6,190,661, 6,187,587, 6,168,950, 6,153,595, 6,150,162, 6,133,246, 6,117,847, 6,096,722, 6,087,343, 6,040,296, 6,005,095, 5,998,383, 5,994,230, 5,891,725, 5,885,970, and 5,840,708. An antisense polynucleotides can be operably linked to an expression control sequence. A total length of about 35 bp can be used in cell culture with cationic liposomes to facilitate cellular uptake, but for in vivo use, preferably shorter oligonucleotides are administered, e.g. 25 nucleotides.
Antisense polynucleotides can comprise modified, nonnaturally-occurring nucleotides and linkages between the nucleotides (e.g., modification of the phosphate-sugar backbone; methyl phosphonate, phosphorothioate, or phosphorodithioate linkages; and 2′-O-methyl ribose sugar units), e.g., to enhance in vivo or in vitro stability, to confer nuclease resistance, to modulate uptake, to modulate cellular distribution and compartmentalization, etc. Any effective nucleotide or modification can be used, including those already mentioned, as known in the art, etc., e.g., disclosed in U.S. Pat. Nos. 6,133,438; 6,127,533; 6,124,445; 6,121,437; 5,218,103 (e.g., nucleoside thiophosphoramidites); 4,973,679; Sproat et al., “2′-O-Methyloligoribonucleotides: synthesis and applications,” Oligonucleotides and Analogs A Practical Approach, Eckstein (ed.), IRL Press, Oxford, 1991, 49-86; Iribarren et al., “2′O-Alkyl Oligoribonucleotides as Antisense Probes,” Proc. Natl. Acad. Sci. USA, 1990, 87, 7747-775 1; Cotton et al., “2′-O-methyl, 2′-O-ethyl oligoribonucleotides and phosphorothioate oligodeoxyribonucleotides as inhibitors of the in vitro U7 snRNP-dependent mRNA processing event,” Nucl. Acids Res., 1991, 19, 2629-2635.
Arrays
The present invention also relates to an ordered array of polynucleotide probes and specific-binding partners (e.g., antibodies) for detecting the expression of differentially-regulated genes in a sample, comprising, one or more polynucleotide probes or specific binding partners associated with a solid support, wherein each probe is specific for said genes, and the probes comprise a nucleotide sequence of SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29 which is specific for said gene, a nucleotide sequence having sequence identity to SEQ ID NOS 1, 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, and 29 which is specific for said gene or polynucleotide, or complements thereto, or a specific-binding partner which is specific for said genes.
The phrase “ordered array” indicates that the probes are arranged in an identifiable or position-addressable pattern, e.g., such as the arrays disclosed in U.S. Pat. Nos. 6,156,501, 6,077,673, 6,054,270, 5,723,320, 5,700,637, WO09919711, WO00023803. The probes are associated with the solid support in any effective way. For instance, the probes can be bound to the solid support, either by polymerizing the probes on the substrate, or by attaching a probe to the substrate. Association can be, covalent, electrostatic, noncovalent, hydrophobic, hydrophilic, noncovalent, coordination, adsorbed, absorbed, polar, etc. When fibers or hollow filaments are utilized for the array, the probes can fill the hollow orifice, be absorbed into the solid filament, be attached to the surface of the orifice, etc. Probes can be of any effective size, sequence identity, composition, etc., as already discussed.
Ordered arrays can further comprise polynucleotide probes or specific-binding partners which are specific for other genes, including genes specific for prostate or disorders associated with prostate.
Transgenic Animals
The present invention also relates to transgenic animals comprising differentially-regulated genes of the present invention. Such genes, as discussed in more detail below, include, but are not limited to, functionally-disrupted genes, mutated genes, ectopically or selectively-expressed genes, inducible or regulatable genes, etc. These transgenic animals can be produced according to any suitable technique or method, including homologous recombination, mutagenesis (e.g., ENU, Rathkolb et al., Exp. Physiol ., 85(6):635-644, 2000), and the tetracycline-regulated gene expression system (e.g., U.S. Pat. No. 6,242,667). The term “gene” as used herein includes any part of a gene, i.e., regulatory sequences, promoters, enhancers, exons, introns, coding sequences, etc. The nucleic acid present in the construct or transgene can be naturally-occurring wild-type, polymorphic, or mutated. When a mouse or other mammal is used, the appropriate homolog can be used in place of a human gene of the present invention.
Along these lines, polynucleotides of the present invention can be used to create transgenic animals, e.g. a non-human animal, comprising at least one cell whose genome comprises a functional disruption of a differentially-regulated gene. By the phrases “functional disruption” or “functionally disrupted,” it is meant that the gene does not express a biologically-active product. It can be substantially deficient in at least one functional activity coded for by the gene. Expression of a polypeptide can be substantially absent, i.e., essentially undetectable amounts are made. However, polypeptide can also be made, but which is deficient in activity, e.g., where only an amino-terminal portion of the gene product is produced.
The transgenic animal can comprise one or more cells. When substantially all its cells contain the engineered gene, it can be referred to as a transgenic animal “whose genome comprises” the engineered gene. This indicates that the endogenous gene loci of the animal has been modified and substantially all cells contain such modification.
Functional disruption of the gene can be accomplished in any effective way, including, e.g., introduction of a stop codon into any part of the coding sequence such that the resulting polypeptide is biologically inactive (e.g., because it lacks a catalytic domain, a ligand binding domain, etc.), introduction of a mutation into a promoter or other regulatory sequence that is effective to turn it off, or reduce transcription of the gene, insertion of an exogenous sequence into the gene which inactivates it (e.g., which disrupts the production of a biologically-active polypeptide or which disrupts the promoter or other transcriptional machinery), deletion of sequences from the a differentially-regulated gene, etc. Examples of transgenic animals having functionally disrupted genes are well known, e.g., as described in U.S. Pat. Nos. 6,239,326, 6,225,525, 6,207,878, 6,194,633, 6,187,992, 6,180,849, 6,177,610, 6,100,445, 6,087,555, 6,080,910, 6,069,297, 6,060,642, 6,028,244, 6,013,858, 5,981,830, 5,866,760, 5,859,314, 5,850,004, 5,817,912, 5,789,654, 5,777,195, and 5,569,824. A transgenic animal which comprises the functional disruption can also be referred to as a “knock-out” animal, since the biological activity of its a differentially-regulated gene has been “knocked-out.” Knock-outs can be homozygous or heterozygous.
For creating functional disrupted genes, and other gene mutations, homologous recombination technology is of special interest since it allows specific regions of the genome to be targeted. Using homologous recombination methods, genes can be specifically-inactivated, specific mutations can be introduced, and exogenous sequences can be introduced at specific sites. These methods are well known in the art, e.g., as described in the patents above. See, also, Robertson, Biol. Reproduc ., 44(2):238-245, 1991. Generally, the genetic engineering is performed in an embryonic stem (ES) cell, or other pluripotent cell line (e.g., adult stem cells, EG cells), and that genetically-modified cell (or nucleus) is used to create a whole organism. Nuclear transfer can be used in combination with homologous recombination technologies.
For example, a differentially-regulated gene locus can be disrupted in mouse ES cells using a positive-negative selection method (e.g., Mansour et al., Nature , 336:348-352, 1988). In this method, a targeting vector can be constructed which comprises a part of the gene to be targeted. A selectable marker, such as neomycin resistance genes, can be inserted into a a differentially-regulated gene exon present in the targeting vector, disrupting it. When the vector recombines with the ES cell genome, it disrupts the function of the gene. The presence in the cell of the vector can be determined by expression of neomycin resistance. See, e.g., U.S. Pat. No. 6,239,326. Cells having at least one functionally disrupted gene can be used to make chimeric and germline animals, e.g., animals having somatic and/or germ cells comprising the engineered gene. Homozygous knock-out animals can be obtained from breeding heterozygous knock-out animals. See, e.g., U.S. Pat. No. 6,225,525.
A transgenic animal, or animal cell, lacking one or more functional differentially-regulated genes can be useful in a variety of applications, including, as an animal model for cancer, for drug screening assays, as a source of tissues deficient in said gene activity, and any of the utilities mentioned in any issued U.S. Patent on transgenic animals, including, U.S. Pat. Nos. 6,239,326, 6,225,525, 6,207,878, 6,194,633, 6,187,992, 6,180,849, 6,177,610, 6,100,445, 6,087,555, 6,080,910, 6,069,297, 6,060,642, 6,028,244, 6,013,858, 5,981,830, 5,866,760, 5,859,314, 5,850,004, 5,817,912, 5,789,654, 5,777,195, and 5,569,824.
The present invention also relates to non-human, transgenic animal whose genome comprises recombinant a differentially-regulated gene nucleic acid operatively linked to an expression control sequence effective to express said coding sequence, e.g., in prostate. such a transgenic animal can also be referred to as a “knock-in” animal since an exogenous gene has been introduced, stably, into its genome.
A recombinant a differentially-regulated gene nucleic acid refers to a gene which has been introduced into a target host cell and optionally modified, such as cells derived from animals, plants, bacteria, yeast, etc. A recombinant a differentially-regulated gene includes completely synthetic nucleic acid sequences, semi-synthetic nucleic acid sequences, sequences derived from natural sources, and chimeras thereof. “Operable linkage” has the meaning used through the specification, i.e., placed in a functional relationship with another nucleic acid. When a gene is operably linked to an expression control sequence, as explained above, it indicates that the gene (e.g., coding sequence) is joined to the expression control sequence (e.g., promoter) in such a way that facilitates transcription and translation of the coding sequence. As described above, the phrase “genome” indicates that the genome of the cell has been modified. In this case, the recombinant a differentially-regulated gene has been stably integrated into the genome of the animal. The a differentially-regulated gene nucleic acid in operable linkage with the expression control sequence can also be referred to as a construct or transgene.
Any expression control sequence can be used depending on the purpose. For instance, if selective expression is desired, then expression control sequences which limit its expression can be selected. These include, e.g., tissue or cell-specific promoters, introns, enhancers, etc. For various methods of cell and tissue-specific expression, see, e.g., U.S. Pat. Nos. 6,215,040, 6,210,736, and 6,153,427. These also include the endogenous promoter, i.e., the coding sequence can be operably linked to its own promoter. Inducible and regulatable promoters can also be utilized.
The present invention also relates to a transgenic animal which contains a functionally disrupted and a transgene stably integrated into the animals genome. Such an animal can be constructed using combinations any of the above- and below-mentioned methods. Such animals have any of the aforementioned uses, including permitting the knock-out of the normal gene and its replacement with a mutated gene. Such a transgene can be integrated at the endogenous gene locus so that the functional disruption and “knock-in” are carried out in the same step.
In addition to the methods mentioned above, transgenic animals can be prepared according to known methods, including, e.g., by pronuclear injection of recombinant genes into pronuclei of 1-cell embryos, incorporating an artificial yeast chromosome into embryonic stem cells, gene targeting methods, embryonic stem cell methodology, cloning methods, nuclear transfer methods. See, also, e.g., U.S. Pat. Nos. 4,736,866; 4,873,191; 4,873,316; 5,082,779; 5,304,489; 5,174,986; 5,175,384; 5,175,385; 5,221,778; Gordon et al., Proc. Natl. Acad. Sci., 77:7380-7384, 1980; Palmiter et al., Cell, 41:343-345, 1985; Palmiter et al., Ann. Rev. Genet., 20:465-499, 1986; Askew et al., Mol. Cell. Bio., 13:4115-4124, 1993; Games et al. Nature, 373:523-527, 1995; Valancius and Smithies, Mol. Cell. Bio., 11:1402-1408, 1991; Stacey et al., Mol. Cell. Bio., 14:1009-1016, 1994; Hasty et al., Nature, 350:243-246, 1995; Rubinstein et al., Nucl. Acid Res., 21:2613-2617,1993; Cibelli et al., Science, 280:1256-1258, 1998. For guidance on recombinase excision systems, see, e.g., U.S. Pat. Nos. 5,626,159, 5,527,695, and 5,434,066. See also, Orban, P. C., et al., “Tissue- and Site-Specific DNA Recombination in Transgenic Mice,” Proc. Natl. Acad. Sci. USA, 89:6861-6865 (1992); O'Gorman, S., et al., “Recombinase-Mediated Gene Activation and Site-Specific Integration in Mammalian Cells,” Science, 251:1351-1355 (1991); Sauer, B., et al., “Cre-stimulated recombination at loxP-Containing DNA sequences placed into the mammalian genome,” Polynucleotides Research, 17(1):147-161 (1989); Gagneten, S. et al. (1997) Nucl. Acids Res. 25:3326-3331; Xiao and Weaver (1997) Nucl. Acids Res. 25:2985-2991; Agah, R. et al. (1997) J. Clin. Invest. 100:169-179; Barlow, C. et. al. (1997) Nucl. Acids Res. 25:2543-2545; Araki, K. et al. (1997) Nucl. Acids Res. 25:868-872; Mortensen, R. N. et al. (1992) Mol. Cell. Biol. 12:2391-2395 (G418 escalation method); Lakhlani, P. P. et al. (1997) Proc. Natl. Acad. Sci. USA 94:9950-9955 (“hit and run”); Westphal and Leder (1997) Curr. Biol. 7:530-533 (transposon-generated “knock-out” and “knock-in”); Templeton, N. S. et al. (1997) Gene Ther. 4:700-709 (methods for efficient gene targeting, allowing for a high frequency of homologous recombination events, e.g., without selectable markers); PCT International Publication WO 93/22443 (functionally-disrupted).
A polynucleotide according to the present invention can be introduced into any non-human animal, including a non-human mammal, mouse (Hogan et al., Manipulating the Mouse Embryo: A Laboratory Manual, Cold Spring Harbor Laboratory , Cold Spring Harbor, New York, 1986), pig (Hammer et al., Nature, 315:343-345, 1985), sheep (Hammer et al., Nature, 315:343-345, 1985), cattle, rat, or primate. See also, e.g., Church, 1987, Trends in Biotech. 5:13-19; Clark et al., Trends in Biotech. 5:20-24, 1987); and DePamphilis et al., BioTechniques, 6:662-680, 1988. Transgenic animals can be produced by the methods described in U.S. Pat. No. 5,994,618, and utilized for any of the utilities described therein.
Database
The present invention also relates to electronic forms of polynucleotides, polypeptides, etc., of the present invention, including computer-readable medium (e.g., magnetic, optical, etc., stored in any suitable format, such as flat files or hierarchical files) which comprise such sequences, or fragments thereof, e-commerce-related means, etc. Along these lines, the present invention relates to methods of retrieving gene sequences from a computer-readable medium, comprising, one or more of the following steps in any effective order, e.g., selecting a cell or gene expression profile, e.g., a profile that specifies that said gene is differentially expressed in prostate cancer, and retrieving said differentially expressed gene sequences, where the gene sequences consist of the genes represented by SEQ ID NOS 1-30.
A “gene expression profile” means the list of tissues, cells, etc., in which a defined gene is expressed (i.e, transcribed and/or translated). A “cell expression profile” means the genes which are expressed in the particular cell type. The profile can be a list of the tissues in which the gene is expressed, but can include additional information as well, including level of expression (e.g., a quantity as compared or normalized to a control gene), and information on temporal (e.g., at what point in the cell-cycle or developmental program) and spatial expression. By the phrase “selecting a gene or cell expression profile,” it is meant that a user decides what type of gene or cell expression pattern he is interested in retrieving, e.g., he may require that the gene is differentially expressed in a tissue, or he may require that the gene is not expressed in blood, but must be expressed in prostate cancer. Any pattern of expression preferences may be selected. The selecting can be performed by any effective method. In general, “selecting” refers to the process in which a user forms a query that is used to search a database of gene expression profiles. The step of retrieving involves searching for results in a database that correspond to the query set forth in the selecting step. Any suitable algorithm can be utilized to perform the search query, including algorithms that look for matches, or that perform optimization between query and data. The database is information that has been stored in an appropriate storage medium, having a suitable computer-readable format. Once results are retrieved, they can be displayed in any suitable format, such as HTML.
For instance, the user may be interested in identifying genes that are differentially expressed in a prostate cancer. He may not care whether small amounts of expression occur in other tissues, as long as such genes are not expressed in peripheral blood lymphocytes. A query is formed by the user to retrieve the set of genes from the database having the desired gene or cell expression profile. Once the query is inputted into the system, a search algorithm is used to interrogate the database, and retrieve results.
Advertising, Licensing, etc., Methods
The present invention also relates to methods of advertising, licensing, selling, purchasing, brokering, etc., genes, polynucleotides, specific-binding partners, antibodies, etc., of the present invention. Methods can comprises, e.g., displaying a differentially-regulated gene , a differentially-regulated gene polypeptide, or antibody specific for a differentially-regulated gene in a printed or computer-readable medium (e.g., on the Web or Internet), accepting an offer to purchase said gene, polypeptide, or antibody.
Other
A polynucleotide, probe, polypeptide, antibody, specific-binding partner, etc., according to the present invention can be isolated. The term “isolate” means that the material is in a form in which it is not found in its original environment or in nature, e.g., more concentrated, more purified, separated from component, etc. An isolated polynucleotide includes, e.g., a polynucleotide having the sequenced separated from the chromosomal DNA found in a living animal, e.g., as the complete gene, a transcript, or a cDNA. This polynucleotide can be part of a vector or inserted into a chromosome (by specific gene-targeting or by random integration at a position other than its normal position) and still be isolated in that it is not in a form that is found in its natural environment. A polynucleotide, polypeptide, etc., of the present invention can also be substantially purified. By substantially purified, it is meant that polynucleotide or polypeptide is separated and is essentially free from other polynucleotides or polypeptides, i.e., the polynucleotide or polypeptide is the primary and active constituent. A polynucleotide can also be a recombinant molecule. By “recombinant,” it is meant that the polynucleotide is an arrangement or form which does not occur in nature. For instance, a recombinant molecule comprising a promoter sequence would not encompass the naturally-occurring gene, but would include the promoter operably linked to a coding sequence not associated with it in nature, e.g., a reporter gene, or a truncation of the normal coding sequence.
The term “marker” is used herein to indicate a means for detecting or labeling a target. A marker can be a polynucleotide (usually referred to as a “probe”), polypeptide (e.g., an antibody conjugated to a detectable label), PNA, or any effective material.
The topic headings set forth above are meant as guidance where certain information can be found in the application, but are not intended to be the only source in the application where information on such topic can be found.
Reference Materials
For other aspects of the polynucleotides, reference is made to standard textbooks of molecular biology. See, e.g., Hames et al., Polynucleotide Hybridization , IL Press, 1985; Davis et al., Basic Methods in Molecular Biology , Elsevir Sciences Publishing, Inc., New York, 1986; Sambrook et al., Molecular Cloning , CSH Press, 1989; Howe, Gene Cloning and Manipulation , Cambridge University Press, 1995; Ausubel et al., Current Protocols in Molecular Biology , John Wiley & Sons, Inc., 1994-1998.
The preceding preferred specific embodiments are, therefore, to be construed as merely illustrative, and not limiting the remainder of the disclosure in any way whatsoever. The entire disclosure of all applications, patents and publications, cited above and in the figures are hereby incorporated by reference in their entirety.








TABLE 1



Clone ID
Protein-L*
Location
Domains Names



1. Pcp0749-2z
1564aa
Nuclear
1. ZnF_C3H1 domain: 36-63aa;




2. Caldesmon domain: 423-1027aa;




3. Coiled coil: 162-197aa;




4. Coiled coil: 645-789aa;




5. Coiled coil: 1339-1366aa.

2. Pcp0389Az
694aa
Extracellular
1. Coiled coil: 17-51aa;




2. Methyl-accepting chemotaxis-like domain (MA): 101-200aa.

3. Pcp0814z
279aa
Membrane
1. Transmembrane domain: 83-105aa;




2. Transmembrane domain: 120-142aa;




3. Transmembrane domain: 192-211aa;




4. MotA/TolQ/ExbB proton channel domain: 34-156aa;




5. Coiled coil: 226-253aa.

4. Pcp0623
2697aa
Nuclear
1. Caldesmon domain: 590-884aa.

5. Pcp0815
1041aa
Nuclear
1. ZF_C2H2: 371-393aa;




2. ZF_C2H2: 399-421aa;




3. ZF_C2H2: 621-651aa;




4. ZF_C2H2: 657-679aa;




5. ZF_C2H2: 689-711aa;




6. ZF_C2H2: 909-931aa;




7. ZF_C2H2: 938-961aa;




8. PP_M1 Phosphoprotein domain: 754-923aa.

6. Pcp0840z
243aa
Nuclear
1. ZnF_C2H2 domains: 12-37aa;




2. ZnF_C2H2 domains: 173-198aa;




3. ZnF_C2H2 domains: 208-230aa.

7. Pcp0424Az
789aa
Cytoplasm
1. Dynamin, large GTPase domain: 54-308aa. (GTP-binding);




2. Dynamin GTPase effector domain: 692-783aa.

7. Pcp0424Bz
763aa
Cytoplasm
1. Dynamin, large GTPase domain: 54-308aa. (GTP-binding);




2. Dynamin GTPase effector domain: 692783aa;

7. Pcp0424Cz
752aa
Cytoplasm
1. Dynamin, large GTPase domain: 54-308aa. (GTP-binding);




2. Dynamin GTPase effector domain: 692-783aa.

8. Pc0382
1584aa
Nuclear
1. SAM domain: 11-78aa;




2. Kinesin domain: 1079-1103aa.

9. Pcp0816
1013aa
Membrane
1. Signal peptide: 1-38aa;




2. EGF-like domain: 274-308aa;




3. Transmembrane domain: 908-930aa.

10. Pcp0480
171aa
Nuclear
1. Estrogen receptor: 1-169aa.

11. Pcp0842x
2221aa
Cytoplasm
1. SET7 domain: 630-842aa



L* stands for protein length in amino acids



























































TABLE 2



Clone ID
Locus
Associated diseases










1. Pcp0749-2z
13q14.11
1.
Rieger syndrome type 2 at 13q14;



2.
Low grade B-cell malignancy at 13q14.

2. Pcp0389Az
6q22.33
1.
IgA Nephropathy at 6q22-q23;



2.
Autosomal recessive craniometaphyseal dysplasia at 6q21-q22;



3.
Heterocellular hereditary persistence of fetal hemoglobin at 6q22.3-




q23.1;



4.
Oculodentodigital dysplasia at 6q22-q24;



5.
Susceptibility to severe hepatic fibrosis due to Schistosoma mansoni




infection at 6q22-q23.

3. Pcp0814z
12p13.3
1.
Chromosomal abnormalities associated with breast and




ovary cancer.

4. Pcp0623
5p13.2

5. Pcp0815
14q11.1
1.
Respiratory allergies (asthma) at 14q11.1

6. Pcp0840z
7p15.1
1.
JAZF1 gene at 7p15 [The gene has not yet been discovered except




EST (Hs.346818). It creates a fusion protein by t (7;17) (p15; q21




and causes all type endometrial stromal tumors].

7. Pcp0424Az
12p12.23
1.
Alzheimer disease familial type 5 at 12p11.23-q13.l2;



2.
Fibrosis of extraocular muscles congenital lat 12p11.2-q12;



3.
Hypertension with brachydactyly at 12p12.2-p11.2.

7. Pcp0424Bz
12p12.3

same as Bcu0424Az.

7. Pcp0424Cz
12p12.3

same as Bcu0424Az.

8. Pc0382
7q21.3
1.
Split-hand/foot malformation type-1 (SHFM1) at 7q21.2-q21.3;



2.
SHFM with sensorineural hearing loss (SHFM1D at 7q21.2-21.3.);



4.
Malignant hyperthermia susceptibility 3 at 7q21-q22;



5.
Myoclonic dystonia-11 at 7q21.

9. Pcp0816
1p13.1
1.
Vesicoureteral reflux (VUR) at 1p13;



2.
Trisomy and Monosomy at 1p13 cause cancers in prostate, ovary




and breast.

10. Pcp0480
6q25.1
1.
Estrogen receptor-1 at 6q25.1 (Alternative isoforms are related to




breast cancer);



2.
Schizophrenia-5 at 6q26-q13;



3.
Insulin-dependent diabetes mellitus-8 at 6q25-q27.

11. Pcp0842x
6q23.3
1.
Dilated cardiomyopathy 1J (CMD1J) at 6q23-q24;



2.
Dilated cardiomyopathy 1F (CMD1F) at 6q23;



3.
Oculodentodigital dysplasia (ODDD) at 6q22-q24;



4.
Susceptibility to severe hepatic fibrosis due to Schistosoma mansoni




infection at 6q22-q23;



5.
IgA nephropathy at 6q22-q23.


































































TABLE 3



Gene




Name
SEQ ID NO
Expression




PCP0749
1-4
UP


PCP0389
5-8
UP


PCP0814
9-10
DOWN


PCP0623
11-12
DOWN


PCP0815
13-14
UP


PCP0840
15-16
DOWN


PCP0424
17-18 (A); 19-20 (B);
UP



21-22 (C)


PC0382
23-24
UP


PCP0816
25-26
UP


PCP0480
27-28
UP
normal expression




restricted to muscle




and uterus

PCP0842
29-30
UP




































44


1
6726
DNA
Homo sapiens

CDS
(367)..(5061)


1
gagaggaaca gggcaaacct ctgacttccg gcggcatttt gaggcggtcc tcctagcggc 60
ctggtagtgt ttttgttgcc ttttcttaat ctacaatctc ttcgttattt ttcttcctgc 120
gacccagttt cgcttgaccc tggagaggcg gcgggcgggt tggttctgct tctcagccat 180
cccgggggct cctcgctagc caagagccgg ttcccgggag ccgcgcgcgc atcgctttct 240
cctcgtcgtc gtcctcctgg gtccaggcgc ggggacagag tcgcctcccc cgctcctcgg 300
agcggcggcg gcggtggtgc ctccggactg cacttgcgaa gggagcttgg ggaggaatag 360
tacaaa atg tca aaa att aga agg aag gtc aca gtg gaa aat acc aag 408
Met Ser Lys Ile Arg Arg Lys Val Thr Val Glu Asn Thr Lys
1 5 10
act ata tct gat agc aca tcc cga aga ccc agt gta ttt gag agg ctt 456
Thr Ile Ser Asp Ser Thr Ser Arg Arg Pro Ser Val Phe Glu Arg Leu
15 20 25 30
gga ccc agc act ggc agt aca gca gag aca cag tgc cgt aac tgg ctg 504
Gly Pro Ser Thr Gly Ser Thr Ala Glu Thr Gln Cys Arg Asn Trp Leu
35 40 45
aag act ggc aac tgc ctc tat gga aac aca tgt aga ttc gta cat ggc 552
Lys Thr Gly Asn Cys Leu Tyr Gly Asn Thr Cys Arg Phe Val His Gly
50 55 60
cct tca cct cgt ggt aaa ggt tat agc agc aat tat aga agg tca cca 600
Pro Ser Pro Arg Gly Lys Gly Tyr Ser Ser Asn Tyr Arg Arg Ser Pro
65 70 75
gaa aga cct aca ggg gat ctt aga gaa aga atg aag aac aag cgc caa 648
Glu Arg Pro Thr Gly Asp Leu Arg Glu Arg Met Lys Asn Lys Arg Gln
80 85 90
gac gtg gac act gag ccc cag aaa cga aat aca gag gag tca tcc tca 696
Asp Val Asp Thr Glu Pro Gln Lys Arg Asn Thr Glu Glu Ser Ser Ser
95 100 105 110
cct gtt agg aaa gaa tct tca aga ggg aga cat agg gaa aag gaa gac 744
Pro Val Arg Lys Glu Ser Ser Arg Gly Arg His Arg Glu Lys Glu Asp
115 120 125
ata aaa atc act aag gaa aga act cca gaa agt gaa gaa gaa aat gta 792
Ile Lys Ile Thr Lys Glu Arg Thr Pro Glu Ser Glu Glu Glu Asn Val
130 135 140
gaa tgg gaa act aat aga gat gat tct gac aat gga gat att aat tat 840
Glu Trp Glu Thr Asn Arg Asp Asp Ser Asp Asn Gly Asp Ile Asn Tyr
145 150 155
gat tat gtt cat gaa ttg tca ttg gaa atg aag cgt cag aag ata cag 888
Asp Tyr Val His Glu Leu Ser Leu Glu Met Lys Arg Gln Lys Ile Gln
160 165 170
agg gaa tta atg aag ctg gaa caa gaa aac atg gag aag aga gaa gaa 936
Arg Glu Leu Met Lys Leu Glu Gln Glu Asn Met Glu Lys Arg Glu Glu
175 180 185 190
att atc att aaa aag gag gtt tca cca gaa gtg gtt aga tca aaa ttg 984
Ile Ile Ile Lys Lys Glu Val Ser Pro Glu Val Val Arg Ser Lys Leu
195 200 205
tcc ccg tca cct tct cta aga aag tct agc aaa tct ccg aag cga aaa 1032
Ser Pro Ser Pro Ser Leu Arg Lys Ser Ser Lys Ser Pro Lys Arg Lys
210 215 220
tca agc ccg aag tcg tct tca gct agc aag aaa gat agg aag aca tct 1080
Ser Ser Pro Lys Ser Ser Ser Ala Ser Lys Lys Asp Arg Lys Thr Ser
225 230 235
gca gta tct tct ccc ctg ttg gac cag cag aga aat tca aaa acc aac 1128
Ala Val Ser Ser Pro Leu Leu Asp Gln Gln Arg Asn Ser Lys Thr Asn
240 245 250
caa agt aaa aag aaa gga cca cgt act cct agt cca ccc cct cct ata 1176
Gln Ser Lys Lys Lys Gly Pro Arg Thr Pro Ser Pro Pro Pro Pro Ile
255 260 265 270
cca gaa gat atc gct ctg ggg aaa aaa tac aaa gaa aaa tat aaa gta 1224
Pro Glu Asp Ile Ala Leu Gly Lys Lys Tyr Lys Glu Lys Tyr Lys Val
275 280 285
aaa gac agg ata gaa gaa aaa aca aga gat gga aag gac aga gga cga 1272
Lys Asp Arg Ile Glu Glu Lys Thr Arg Asp Gly Lys Asp Arg Gly Arg
290 295 300
gat ttt gaa cga caa aga gaa aag aga gac aag cca agg tct act tcc 1320
Asp Phe Glu Arg Gln Arg Glu Lys Arg Asp Lys Pro Arg Ser Thr Ser
305 310 315
cca gca gga cag cat cat tct cct ata tct tct aga cat cac tca tct 1368
Pro Ala Gly Gln His His Ser Pro Ile Ser Ser Arg His His Ser Ser
320 325 330
tcc tca caa tca gga tca tct att caa aga cat tct cct tct cct cgt 1416
Ser Ser Gln Ser Gly Ser Ser Ile Gln Arg His Ser Pro Ser Pro Arg
335 340 345 350
cga aaa aga act cct tca cca tct tat cag cgg aca cta act cca cct 1464
Arg Lys Arg Thr Pro Ser Pro Ser Tyr Gln Arg Thr Leu Thr Pro Pro
355 360 365
tta cga cgc tct gcc tct cct tat cct tca cat tct ttg tcg tct ccc 1512
Leu Arg Arg Ser Ala Ser Pro Tyr Pro Ser His Ser Leu Ser Ser Pro
370 375 380
cag aga aag cag agt cct cca aga cat cgc tct cca atg cga gag aaa 1560
Gln Arg Lys Gln Ser Pro Pro Arg His Arg Ser Pro Met Arg Glu Lys
385 390 395
ggg aga cat gat cat gaa cga act tca cag tct cat gat cga cgc cac 1608
Gly Arg His Asp His Glu Arg Thr Ser Gln Ser His Asp Arg Arg His
400 405 410
gaa agg agg gaa gat act agg ggc aaa cga gac aga gaa aag gac tca 1656
Glu Arg Arg Glu Asp Thr Arg Gly Lys Arg Asp Arg Glu Lys Asp Ser
415 420 425 430
aga gaa gaa cga gaa tat gaa cag gat cag agc tct tct aga gac cac 1704
Arg Glu Glu Arg Glu Tyr Glu Gln Asp Gln Ser Ser Ser Arg Asp His
435 440 445
aga gat gac aga gaa cct cga gat ggt cgg gat cgg aga gat gcc aga 1752
Arg Asp Asp Arg Glu Pro Arg Asp Gly Arg Asp Arg Arg Asp Ala Arg
450 455 460
gat act agg gac cga agg gaa cta aga gac tcc aga gac atg cgg gac 1800
Asp Thr Arg Asp Arg Arg Glu Leu Arg Asp Ser Arg Asp Met Arg Asp
465 470 475
tca agg gag atg aga gat tat agc aga gat acc aaa gag agc cgt gat 1848
Ser Arg Glu Met Arg Asp Tyr Ser Arg Asp Thr Lys Glu Ser Arg Asp
480 485 490
ccc aga gat tct cgg tcc act cgt gat gcc cat gac tac agg gac cgt 1896
Pro Arg Asp Ser Arg Ser Thr Arg Asp Ala His Asp Tyr Arg Asp Arg
495 500 505 510
gaa ggt cga gat act cat cga aag gag gat aca tat cca gaa gaa tcc 1944
Glu Gly Arg Asp Thr His Arg Lys Glu Asp Thr Tyr Pro Glu Glu Ser
515 520 525
cgg agt tat ggc cga aac cat ttg aga gaa gaa agt tct cgt acg gaa 1992
Arg Ser Tyr Gly Arg Asn His Leu Arg Glu Glu Ser Ser Arg Thr Glu
530 535 540
ata agg aat gag tcc aga aat gag tct cga agt gaa att aga aat gac 2040
Ile Arg Asn Glu Ser Arg Asn Glu Ser Arg Ser Glu Ile Arg Asn Asp
545 550 555
cga atg ggc cga agt agg ggg agg gtt cct gag tta cct gaa aag gga 2088
Arg Met Gly Arg Ser Arg Gly Arg Val Pro Glu Leu Pro Glu Lys Gly
560 565 570
agt cga ggc tca aga ggt tct caa att gat agt cac agt agt aat agc 2136
Ser Arg Gly Ser Arg Gly Ser Gln Ile Asp Ser His Ser Ser Asn Ser
575 580 585 590
aac tat cat gac agc tgg gaa act cga agt agc tat cct gaa aga gat 2184
Asn Tyr His Asp Ser Trp Glu Thr Arg Ser Ser Tyr Pro Glu Arg Asp
595 600 605
aga tat cct gaa aga gac aac aga gat caa gca agg gat tct tcc ttt 2232
Arg Tyr Pro Glu Arg Asp Asn Arg Asp Gln Ala Arg Asp Ser Ser Phe
610 615 620
gag aga aga cat gga gag cga gac cgt cgt gac aac aga gag aga gat 2280
Glu Arg Arg His Gly Glu Arg Asp Arg Arg Asp Asn Arg Glu Arg Asp
625 630 635
caa aga cca agc tca cca att cga cat cag gga agg aat gac gag ctt 2328
Gln Arg Pro Ser Ser Pro Ile Arg His Gln Gly Arg Asn Asp Glu Leu
640 645 650
gag cgt gat gaa aga aga gag gaa cga aga gta gac aga gtg gat gat 2376
Glu Arg Asp Glu Arg Arg Glu Glu Arg Arg Val Asp Arg Val Asp Asp
655 660 665 670
agg aga gat gaa agg gct aga gag aga gat cgg gaa cga gaa cga gac 2424
Arg Arg Asp Glu Arg Ala Arg Glu Arg Asp Arg Glu Arg Glu Arg Asp
675 680 685
agg gag cgg gag aga gag agg gaa cgt gaa cgg gat cgg gaa aga gaa 2472
Arg Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg Asp Arg Glu Arg Glu
690 695 700
aaa gag aga gaa cta gaa aga gag cgt gct agg gaa cgg gag aga gaa 2520
Lys Glu Arg Glu Leu Glu Arg Glu Arg Ala Arg Glu Arg Glu Arg Glu
705 710 715
aga gaa aaa gag aga gat cgt gaa agg gat aga gac cga gac cac gat 2568
Arg Glu Lys Glu Arg Asp Arg Glu Arg Asp Arg Asp Arg Asp His Asp
720 725 730
cga gag cgg gaa aga gag agg gaa cga gac agg gaa aaa gaa cgg gaa 2616
Arg Glu Arg Glu Arg Glu Arg Glu Arg Asp Arg Glu Lys Glu Arg Glu
735 740 745 750
cga gaa aga gaa gag aga gag agg gag aga gag cga gaa cgg gag aga 2664
Arg Glu Arg Glu Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg
755 760 765
gag cga gag cga gaa cgg gaa cga gaa aga gcg aga gaa agg gat aaa 2712
Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg Ala Arg Glu Arg Asp Lys
770 775 780
gaa cga gaa cgc caa agg gat tgg gaa gac aaa gac aaa gga cga gat 2760
Glu Arg Glu Arg Gln Arg Asp Trp Glu Asp Lys Asp Lys Gly Arg Asp
785 790 795
gac cgc aga gaa aag cga gaa gag atc cga gaa gat agg aat cca aga 2808
Asp Arg Arg Glu Lys Arg Glu Glu Ile Arg Glu Asp Arg Asn Pro Arg
800 805 810
gat gga cat gat gaa aga aaa tca aag aag cgc tat aga aat gaa ggg 2856
Asp Gly His Asp Glu Arg Lys Ser Lys Lys Arg Tyr Arg Asn Glu Gly
815 820 825 830
agt ccc agc cct aga cag tcc ccg aag cgc cgg cgt gaa cat tct ccg 2904
Ser Pro Ser Pro Arg Gln Ser Pro Lys Arg Arg Arg Glu His Ser Pro
835 840 845
gac agt gat gcc tac aac agt gga gat gat aaa aat gaa aaa cac aga 2952
Asp Ser Asp Ala Tyr Asn Ser Gly Asp Asp Lys Asn Glu Lys His Arg
850 855 860
ctc ttg agc caa gtt gta cga cct caa gaa tct cgt tct ctt agt ccc 3000
Leu Leu Ser Gln Val Val Arg Pro Gln Glu Ser Arg Ser Leu Ser Pro
865 870 875
tcg cac ctc aca gaa gac aga cag ggt aga tgg aaa gag gag gat cgt 3048
Ser His Leu Thr Glu Asp Arg Gln Gly Arg Trp Lys Glu Glu Asp Arg
880 885 890
aaa cca gaa agg aaa gag agt tca agg cgc tac gaa gaa cag gaa ctc 3096
Lys Pro Glu Arg Lys Glu Ser Ser Arg Arg Tyr Glu Glu Gln Glu Leu
895 900 905 910
aag gag aaa gtt tct tct gta gat aaa cag aga gaa cag aca gaa atc 3144
Lys Glu Lys Val Ser Ser Val Asp Lys Gln Arg Glu Gln Thr Glu Ile
915 920 925
ctg gaa agc tca aga atg cgt gca cag gac att ata gga cac cac cag 3192
Leu Glu Ser Ser Arg Met Arg Ala Gln Asp Ile Ile Gly His His Gln
930 935 940
tct gaa gat cga gag aca tct gat cga gct cat gat gaa aac aag aag 3240
Ser Glu Asp Arg Glu Thr Ser Asp Arg Ala His Asp Glu Asn Lys Lys
945 950 955
aaa gca aaa att caa aag aaa cca att aag aaa aag aaa gag gat gat 3288
Lys Ala Lys Ile Gln Lys Lys Pro Ile Lys Lys Lys Lys Glu Asp Asp
960 965 970
gtt gga ata gag agg ggt aac ata gag aca aca tct gaa gat ggt caa 3336
Val Gly Ile Glu Arg Gly Asn Ile Glu Thr Thr Ser Glu Asp Gly Gln
975 980 985 990
gta ttt tca cca aaa aaa gga cag aaa aag aaa agc att gaa aaa aaa 3384
Val Phe Ser Pro Lys Lys Gly Gln Lys Lys Lys Ser Ile Glu Lys Lys
995 1000 1005
cgt aaa aaa tcc aaa ggt gat tct gat att tct gat gaa gaa gca 3429
Arg Lys Lys Ser Lys Gly Asp Ser Asp Ile Ser Asp Glu Glu Ala
1010 1015 1020
gcc cag caa agt aag aag aaa aga ggc cca cgg act ccc cct ata 3474
Ala Gln Gln Ser Lys Lys Lys Arg Gly Pro Arg Thr Pro Pro Ile
1025 1030 1035
aca act aaa gag gaa ttg gtt gaa atg tgc aat ggt aag aat ggt 3519
Thr Thr Lys Glu Glu Leu Val Glu Met Cys Asn Gly Lys Asn Gly
1040 1045 1050
att cta gag gac tcc cag aaa aaa gaa gat aca gca ttc agt gac 3564
Ile Leu Glu Asp Ser Gln Lys Lys Glu Asp Thr Ala Phe Ser Asp
1055 1060 1065
tgg tct gat gag gat gtc cct gac cgt aca gag gtg aca gaa gca 3609
Trp Ser Asp Glu Asp Val Pro Asp Arg Thr Glu Val Thr Glu Ala
1070 1075 1080
gag cat act gcc acc gcc acg act cct ggt agt acc cct tct cct 3654
Glu His Thr Ala Thr Ala Thr Thr Pro Gly Ser Thr Pro Ser Pro
1085 1090 1095
cta tct tct ctt ctt cct cct cca ccg cct gtg gct act gcc act 3699
Leu Ser Ser Leu Leu Pro Pro Pro Pro Pro Val Ala Thr Ala Thr
1100 1105 1110
gct aca act gtg cct gca act ctt gct gcc act act gct gct gcc 3744
Ala Thr Thr Val Pro Ala Thr Leu Ala Ala Thr Thr Ala Ala Ala
1115 1120 1125
gcc acc tct ttc agc aca tct gcc atc act att tcc acc tct gcc 3789
Ala Thr Ser Phe Ser Thr Ser Ala Ile Thr Ile Ser Thr Ser Ala
1130 1135 1140
acc ccc acc aat acc acc aat aat act ttt gcc aat gaa gac tca 3834
Thr Pro Thr Asn Thr Thr Asn Asn Thr Phe Ala Asn Glu Asp Ser
1145 1150 1155
cac aga aaa tgc cac aga aca cga gta gaa aaa gta gag acg cct 3879
His Arg Lys Cys His Arg Thr Arg Val Glu Lys Val Glu Thr Pro
1160 1165 1170
cac gtg act ata gaa gat gca cag cat cgc aag cct atg gat caa 3924
His Val Thr Ile Glu Asp Ala Gln His Arg Lys Pro Met Asp Gln
1175 1180 1185
aag agg agc agc agc ctc ggg agc aat cgg agt aac cgt agt cat 3969
Lys Arg Ser Ser Ser Leu Gly Ser Asn Arg Ser Asn Arg Ser His
1190 1195 1200
acg tct ggt cgt ctt cgc tcc cca tcc aat gat tca gcc cat cga 4014
Thr Ser Gly Arg Leu Arg Ser Pro Ser Asn Asp Ser Ala His Arg
1205 1210 1215
agt gga gat gac caa agt ggt cga aag aga gta ctg cac agt ggc 4059
Ser Gly Asp Asp Gln Ser Gly Arg Lys Arg Val Leu His Ser Gly
1220 1225 1230
tca aga gat aga gaa aaa aca aaa agc ctg gaa atc aca gga gag 4104
Ser Arg Asp Arg Glu Lys Thr Lys Ser Leu Glu Ile Thr Gly Glu
1235 1240 1245
aga aaa tct agg att gat cag tta aag cgt gga gaa ccc agt cga 4149
Arg Lys Ser Arg Ile Asp Gln Leu Lys Arg Gly Glu Pro Ser Arg
1250 1255 1260
agt act tct tca gat cgc cag gat tca aga agc cat agt tca aga 4194
Ser Thr Ser Ser Asp Arg Gln Asp Ser Arg Ser His Ser Ser Arg
1265 1270 1275
aga agt tct cca gag tca gat cga cag gtc cat tca aga tct ggg 4239
Arg Ser Ser Pro Glu Ser Asp Arg Gln Val His Ser Arg Ser Gly
1280 1285 1290
tca ttt gat agc aga gac agg ctt caa gaa cga gat cga tat gaa 4284
Ser Phe Asp Ser Arg Asp Arg Leu Gln Glu Arg Asp Arg Tyr Glu
1295 1300 1305
cac gac aga gag cgc gag aga gag agg aga gat acg agg cag aga 4329
His Asp Arg Glu Arg Glu Arg Glu Arg Arg Asp Thr Arg Gln Arg
1310 1315 1320
gaa tgg gac cga gat gct gat aaa gat tgg cca cgc aac agg gat 4374
Glu Trp Asp Arg Asp Ala Asp Lys Asp Trp Pro Arg Asn Arg Asp
1325 1330 1335
cga gat aga ttg cga gaa cga gaa cga gag aga gaa cga gac aaa 4419
Arg Asp Arg Leu Arg Glu Arg Glu Arg Glu Arg Glu Arg Asp Lys
1340 1345 1350
agg aga gac ttg gat agg gaa aga gag aga cta att tct gat tct 4464
Arg Arg Asp Leu Asp Arg Glu Arg Glu Arg Leu Ile Ser Asp Ser
1355 1360 1365
gtt gaa agg gac agg gac aga gac aga gac aga act ttt gag agt 4509
Val Glu Arg Asp Arg Asp Arg Asp Arg Asp Arg Thr Phe Glu Ser
1370 1375 1380
tct caa ata gag tct gtg aaa cgc tgt gaa gca aaa ctg gaa ggt 4554
Ser Gln Ile Glu Ser Val Lys Arg Cys Glu Ala Lys Leu Glu Gly
1385 1390 1395
gaa cat gaa agg gat cta gaa agc act tcc cga gac tct cta gcc 4599
Glu His Glu Arg Asp Leu Glu Ser Thr Ser Arg Asp Ser Leu Ala
1400 1405 1410
ttg gat aaa gag aga atg gat aaa gat ctg gga tct gtg cag gga 4644
Leu Asp Lys Glu Arg Met Asp Lys Asp Leu Gly Ser Val Gln Gly
1415 1420 1425
ttt gaa gat aca aat aaa tcc gag aga act gag agt ctg gaa gca 4689
Phe Glu Asp Thr Asn Lys Ser Glu Arg Thr Glu Ser Leu Glu Ala
1430 1435 1440
gga gat gac gag tcc aag tta gat gat gca cat tca tta ggc tct 4734
Gly Asp Asp Glu Ser Lys Leu Asp Asp Ala His Ser Leu Gly Ser
1445 1450 1455
ggt gct gga gaa gga tac gag cca atc agt gat gac gaa cta gat 4779
Gly Ala Gly Glu Gly Tyr Glu Pro Ile Ser Asp Asp Glu Leu Asp
1460 1465 1470
gaa att ctg gca ggt gat gca gaa aag agg gag gac caa cag gat 4824
Glu Ile Leu Ala Gly Asp Ala Glu Lys Arg Glu Asp Gln Gln Asp
1475 1480 1485
gag gag aag atg cca gat ccc tta gat gtg ata gat gtg gat tgg 4869
Glu Glu Lys Met Pro Asp Pro Leu Asp Val Ile Asp Val Asp Trp
1490 1495 1500
tct ggt ctt atg cca aag cat cca aaa gaa cca cga gag cct ggg 4914
Ser Gly Leu Met Pro Lys His Pro Lys Glu Pro Arg Glu Pro Gly
1505 1510 1515
gct gca ctc tta aaa ttc aca cct gga gct gtt atg cta aga gtt 4959
Ala Ala Leu Leu Lys Phe Thr Pro Gly Ala Val Met Leu Arg Val
1520 1525 1530
ggg att tct aaa aag ttg gca ggt tct gaa ctc ttt gcc aaa gtc 5004
Gly Ile Ser Lys Lys Leu Ala Gly Ser Glu Leu Phe Ala Lys Val
1535 1540 1545
aaa gaa aca tgt cag aga ctt tta gaa aaa ccc aaa ggt agt ttc 5049
Lys Glu Thr Cys Gln Arg Leu Leu Glu Lys Pro Lys Gly Ser Phe
1550 1555 1560
att tta ctt taa ctatataatg tctgttaacc atttaagatg ccatctgaag 5101
Ile Leu Leu
gggattctga tctgttctta tgtagcactt aacactgtgt agaaactatt ttttgagaaa 5161
tcattttata atcattattt aaccctcatg gtcaaagttt ctctttaaaa tttattttga 5221
gaagaagagt tatcccacag aaaagttggg aaaagagtac aatgaccttt ttgtatgaaa 5281
attacttatt aacaggccag gcgtggtgtt gcatgtctgt agtcacagct actcagggag 5341
gttgaggcag caggattgct ggagcccagg aaattgaggc tgcagtgagc catgattgag 5401
ccaccacact ccaacctagg tgacagagca agaccctgtc tcaaaaaaaa aaaaacaaat 5461
taaccaataa gttctaatat caaagtgctc agtggtttgc ccttggctaa atgaagcaga 5521
gccaggaaaa acagactaca tatttttcat gtctaaagaa attgggtatt ttggcagccc 5581
tttcccctag acatctaccc aaatgcaggt gtgtaggttg agtctttaac aaagtgatta 5641
agagcttggt ctgtaaggcc ggatgatctg gatttcagta ggcacaccac ttactggcta 5701
ttacttaatc tgtgtgttag tgtcatcatc tgtaagtcag gaataatcat accaccaact 5761
tcctatggta attaggagca aatgagttat tacaggcaaa acacttagaa cagttcctgg 5821
catatagtaa tacccaataa atattaactg ctactttgaa aatatcctat cacgctgatt 5881
tttgacctca ctgcagcaat tttcagttat tccagattat ctagcttatg gattctggtg 5941
gtaggggttg tttggttttg gttttcactg tctctgtctc atctagtacc taccttagtt 6001
tattttgcaa cttactaata ctttattaat ggggagggac gagtagatgg taaaaagaag 6061
gaaaaggagg taaaaggtga aaggaacaac attaattaac aattttacgt catgtccctg 6121
gacataaaag tttagttagt attaaatttt tcactaatac aaaataaaaa aatattgttt 6181
tatgagtttt atgaattcat gcccttcctt tactctatta gcataagcag taaatttttt 6241
tattttaata tagcccaata aacctagagt atacatgtac aaaatacata taattgttaa 6301
cgtgtattaa ccgaaaaatg acccaagact tagttcttgc cctactgtat ctgccttgtt 6361
tggttggttc tgtgacctta agcaaataac tcctgtgagc ctcaatttta tttgtaaagt 6421
gatggaataa aacccctaaa atcttaccca cctctaaaga tatttgtttc tgtgaccttt 6481
tgctagtagc atttcaagtt aaaatctggt ttgattttgc tacccatgaa atacagttcg 6541
gcccttactt attgatgact taacctaaac agtgaaaata tgcactgtaa agggtggggt 6601
gatgtggctt aacaatcaga cttcttctat ttttgctgct atggtggttg tattagagaa 6661
ctgatgtatt atcttgaata aagactttgt cttgtttact gccctaaaaa aaaaaaaaaa 6721
aaaaa 6726


2
1564
PRT
Homo sapiens

2
Met Ser Lys Ile Arg Arg Lys Val Thr Val Glu Asn Thr Lys Thr Ile
1 5 10 15
Ser Asp Ser Thr Ser Arg Arg Pro Ser Val Phe Glu Arg Leu Gly Pro
20 25 30
Ser Thr Gly Ser Thr Ala Glu Thr Gln Cys Arg Asn Trp Leu Lys Thr
35 40 45
Gly Asn Cys Leu Tyr Gly Asn Thr Cys Arg Phe Val His Gly Pro Ser
50 55 60
Pro Arg Gly Lys Gly Tyr Ser Ser Asn Tyr Arg Arg Ser Pro Glu Arg
65 70 75 80
Pro Thr Gly Asp Leu Arg Glu Arg Met Lys Asn Lys Arg Gln Asp Val
85 90 95
Asp Thr Glu Pro Gln Lys Arg Asn Thr Glu Glu Ser Ser Ser Pro Val
100 105 110
Arg Lys Glu Ser Ser Arg Gly Arg His Arg Glu Lys Glu Asp Ile Lys
115 120 125
Ile Thr Lys Glu Arg Thr Pro Glu Ser Glu Glu Glu Asn Val Glu Trp
130 135 140
Glu Thr Asn Arg Asp Asp Ser Asp Asn Gly Asp Ile Asn Tyr Asp Tyr
145 150 155 160
Val His Glu Leu Ser Leu Glu Met Lys Arg Gln Lys Ile Gln Arg Glu
165 170 175
Leu Met Lys Leu Glu Gln Glu Asn Met Glu Lys Arg Glu Glu Ile Ile
180 185 190
Ile Lys Lys Glu Val Ser Pro Glu Val Val Arg Ser Lys Leu Ser Pro
195 200 205
Ser Pro Ser Leu Arg Lys Ser Ser Lys Ser Pro Lys Arg Lys Ser Ser
210 215 220
Pro Lys Ser Ser Ser Ala Ser Lys Lys Asp Arg Lys Thr Ser Ala Val
225 230 235 240
Ser Ser Pro Leu Leu Asp Gln Gln Arg Asn Ser Lys Thr Asn Gln Ser
245 250 255
Lys Lys Lys Gly Pro Arg Thr Pro Ser Pro Pro Pro Pro Ile Pro Glu
260 265 270
Asp Ile Ala Leu Gly Lys Lys Tyr Lys Glu Lys Tyr Lys Val Lys Asp
275 280 285
Arg Ile Glu Glu Lys Thr Arg Asp Gly Lys Asp Arg Gly Arg Asp Phe
290 295 300
Glu Arg Gln Arg Glu Lys Arg Asp Lys Pro Arg Ser Thr Ser Pro Ala
305 310 315 320
Gly Gln His His Ser Pro Ile Ser Ser Arg His His Ser Ser Ser Ser
325 330 335
Gln Ser Gly Ser Ser Ile Gln Arg His Ser Pro Ser Pro Arg Arg Lys
340 345 350
Arg Thr Pro Ser Pro Ser Tyr Gln Arg Thr Leu Thr Pro Pro Leu Arg
355 360 365
Arg Ser Ala Ser Pro Tyr Pro Ser His Ser Leu Ser Ser Pro Gln Arg
370 375 380
Lys Gln Ser Pro Pro Arg His Arg Ser Pro Met Arg Glu Lys Gly Arg
385 390 395 400
His Asp His Glu Arg Thr Ser Gln Ser His Asp Arg Arg His Glu Arg
405 410 415
Arg Glu Asp Thr Arg Gly Lys Arg Asp Arg Glu Lys Asp Ser Arg Glu
420 425 430
Glu Arg Glu Tyr Glu Gln Asp Gln Ser Ser Ser Arg Asp His Arg Asp
435 440 445
Asp Arg Glu Pro Arg Asp Gly Arg Asp Arg Arg Asp Ala Arg Asp Thr
450 455 460
Arg Asp Arg Arg Glu Leu Arg Asp Ser Arg Asp Met Arg Asp Ser Arg
465 470 475 480
Glu Met Arg Asp Tyr Ser Arg Asp Thr Lys Glu Ser Arg Asp Pro Arg
485 490 495
Asp Ser Arg Ser Thr Arg Asp Ala His Asp Tyr Arg Asp Arg Glu Gly
500 505 510
Arg Asp Thr His Arg Lys Glu Asp Thr Tyr Pro Glu Glu Ser Arg Ser
515 520 525
Tyr Gly Arg Asn His Leu Arg Glu Glu Ser Ser Arg Thr Glu Ile Arg
530 535 540
Asn Glu Ser Arg Asn Glu Ser Arg Ser Glu Ile Arg Asn Asp Arg Met
545 550 555 560
Gly Arg Ser Arg Gly Arg Val Pro Glu Leu Pro Glu Lys Gly Ser Arg
565 570 575
Gly Ser Arg Gly Ser Gln Ile Asp Ser His Ser Ser Asn Ser Asn Tyr
580 585 590
His Asp Ser Trp Glu Thr Arg Ser Ser Tyr Pro Glu Arg Asp Arg Tyr
595 600 605
Pro Glu Arg Asp Asn Arg Asp Gln Ala Arg Asp Ser Ser Phe Glu Arg
610 615 620
Arg His Gly Glu Arg Asp Arg Arg Asp Asn Arg Glu Arg Asp Gln Arg
625 630 635 640
Pro Ser Ser Pro Ile Arg His Gln Gly Arg Asn Asp Glu Leu Glu Arg
645 650 655
Asp Glu Arg Arg Glu Glu Arg Arg Val Asp Arg Val Asp Asp Arg Arg
660 665 670
Asp Glu Arg Ala Arg Glu Arg Asp Arg Glu Arg Glu Arg Asp Arg Glu
675 680 685
Arg Glu Arg Glu Arg Glu Arg Glu Arg Asp Arg Glu Arg Glu Lys Glu
690 695 700
Arg Glu Leu Glu Arg Glu Arg Ala Arg Glu Arg Glu Arg Glu Arg Glu
705 710 715 720
Lys Glu Arg Asp Arg Glu Arg Asp Arg Asp Arg Asp His Asp Arg Glu
725 730 735
Arg Glu Arg Glu Arg Glu Arg Asp Arg Glu Lys Glu Arg Glu Arg Glu
740 745 750
Arg Glu Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg
755 760 765
Glu Arg Glu Arg Glu Arg Glu Arg Ala Arg Glu Arg Asp Lys Glu Arg
770 775 780
Glu Arg Gln Arg Asp Trp Glu Asp Lys Asp Lys Gly Arg Asp Asp Arg
785 790 795 800
Arg Glu Lys Arg Glu Glu Ile Arg Glu Asp Arg Asn Pro Arg Asp Gly
805 810 815
His Asp Glu Arg Lys Ser Lys Lys Arg Tyr Arg Asn Glu Gly Ser Pro
820 825 830
Ser Pro Arg Gln Ser Pro Lys Arg Arg Arg Glu His Ser Pro Asp Ser
835 840 845
Asp Ala Tyr Asn Ser Gly Asp Asp Lys Asn Glu Lys His Arg Leu Leu
850 855 860
Ser Gln Val Val Arg Pro Gln Glu Ser Arg Ser Leu Ser Pro Ser His
865 870 875 880
Leu Thr Glu Asp Arg Gln Gly Arg Trp Lys Glu Glu Asp Arg Lys Pro
885 890 895
Glu Arg Lys Glu Ser Ser Arg Arg Tyr Glu Glu Gln Glu Leu Lys Glu
900 905 910
Lys Val Ser Ser Val Asp Lys Gln Arg Glu Gln Thr Glu Ile Leu Glu
915 920 925
Ser Ser Arg Met Arg Ala Gln Asp Ile Ile Gly His His Gln Ser Glu
930 935 940
Asp Arg Glu Thr Ser Asp Arg Ala His Asp Glu Asn Lys Lys Lys Ala
945 950 955 960
Lys Ile Gln Lys Lys Pro Ile Lys Lys Lys Lys Glu Asp Asp Val Gly
965 970 975
Ile Glu Arg Gly Asn Ile Glu Thr Thr Ser Glu Asp Gly Gln Val Phe
980 985 990
Ser Pro Lys Lys Gly Gln Lys Lys Lys Ser Ile Glu Lys Lys Arg Lys
995 1000 1005
Lys Ser Lys Gly Asp Ser Asp Ile Ser Asp Glu Glu Ala Ala Gln
1010 1015 1020
Gln Ser Lys Lys Lys Arg Gly Pro Arg Thr Pro Pro Ile Thr Thr
1025 1030 1035
Lys Glu Glu Leu Val Glu Met Cys Asn Gly Lys Asn Gly Ile Leu
1040 1045 1050
Glu Asp Ser Gln Lys Lys Glu Asp Thr Ala Phe Ser Asp Trp Ser
1055 1060 1065
Asp Glu Asp Val Pro Asp Arg Thr Glu Val Thr Glu Ala Glu His
1070 1075 1080
Thr Ala Thr Ala Thr Thr Pro Gly Ser Thr Pro Ser Pro Leu Ser
1085 1090 1095
Ser Leu Leu Pro Pro Pro Pro Pro Val Ala Thr Ala Thr Ala Thr
1100 1105 1110
Thr Val Pro Ala Thr Leu Ala Ala Thr Thr Ala Ala Ala Ala Thr
1115 1120 1125
Ser Phe Ser Thr Ser Ala Ile Thr Ile Ser Thr Ser Ala Thr Pro
1130 1135 1140
Thr Asn Thr Thr Asn Asn Thr Phe Ala Asn Glu Asp Ser His Arg
1145 1150 1155
Lys Cys His Arg Thr Arg Val Glu Lys Val Glu Thr Pro His Val
1160 1165 1170
Thr Ile Glu Asp Ala Gln His Arg Lys Pro Met Asp Gln Lys Arg
1175 1180 1185
Ser Ser Ser Leu Gly Ser Asn Arg Ser Asn Arg Ser His Thr Ser
1190 1195 1200
Gly Arg Leu Arg Ser Pro Ser Asn Asp Ser Ala His Arg Ser Gly
1205 1210 1215
Asp Asp Gln Ser Gly Arg Lys Arg Val Leu His Ser Gly Ser Arg
1220 1225 1230
Asp Arg Glu Lys Thr Lys Ser Leu Glu Ile Thr Gly Glu Arg Lys
1235 1240 1245
Ser Arg Ile Asp Gln Leu Lys Arg Gly Glu Pro Ser Arg Ser Thr
1250 1255 1260
Ser Ser Asp Arg Gln Asp Ser Arg Ser His Ser Ser Arg Arg Ser
1265 1270 1275
Ser Pro Glu Ser Asp Arg Gln Val His Ser Arg Ser Gly Ser Phe
1280 1285 1290
Asp Ser Arg Asp Arg Leu Gln Glu Arg Asp Arg Tyr Glu His Asp
1295 1300 1305
Arg Glu Arg Glu Arg Glu Arg Arg Asp Thr Arg Gln Arg Glu Trp
1310 1315 1320
Asp Arg Asp Ala Asp Lys Asp Trp Pro Arg Asn Arg Asp Arg Asp
1325 1330 1335
Arg Leu Arg Glu Arg Glu Arg Glu Arg Glu Arg Asp Lys Arg Arg
1340 1345 1350
Asp Leu Asp Arg Glu Arg Glu Arg Leu Ile Ser Asp Ser Val Glu
1355 1360 1365
Arg Asp Arg Asp Arg Asp Arg Asp Arg Thr Phe Glu Ser Ser Gln
1370 1375 1380
Ile Glu Ser Val Lys Arg Cys Glu Ala Lys Leu Glu Gly Glu His
1385 1390 1395
Glu Arg Asp Leu Glu Ser Thr Ser Arg Asp Ser Leu Ala Leu Asp
1400 1405 1410
Lys Glu Arg Met Asp Lys Asp Leu Gly Ser Val Gln Gly Phe Glu
1415 1420 1425
Asp Thr Asn Lys Ser Glu Arg Thr Glu Ser Leu Glu Ala Gly Asp
1430 1435 1440
Asp Glu Ser Lys Leu Asp Asp Ala His Ser Leu Gly Ser Gly Ala
1445 1450 1455
Gly Glu Gly Tyr Glu Pro Ile Ser Asp Asp Glu Leu Asp Glu Ile
1460 1465 1470
Leu Ala Gly Asp Ala Glu Lys Arg Glu Asp Gln Gln Asp Glu Glu
1475 1480 1485
Lys Met Pro Asp Pro Leu Asp Val Ile Asp Val Asp Trp Ser Gly
1490 1495 1500
Leu Met Pro Lys His Pro Lys Glu Pro Arg Glu Pro Gly Ala Ala
1505 1510 1515
Leu Leu Lys Phe Thr Pro Gly Ala Val Met Leu Arg Val Gly Ile
1520 1525 1530
Ser Lys Lys Leu Ala Gly Ser Glu Leu Phe Ala Lys Val Lys Glu
1535 1540 1545
Thr Cys Gln Arg Leu Leu Glu Lys Pro Lys Gly Ser Phe Ile Leu
1550 1555 1560
Leu


3
6429
DNA
Homo sapiens

CDS
(70)..(4764)


3
gagaggaaca gggcaaacct ctgacttccg gcggcatttt gaggcggtcc tcctagcggc 60
ctgtacaaa atg tca aaa att aga agg aag gtc aca gtg gaa aat acc aag 111
Met Ser Lys Ile Arg Arg Lys Val Thr Val Glu Asn Thr Lys
1 5 10
act ata tct gat agc aca tcc cga aga ccc agt gta ttt gag agg ctt 159
Thr Ile Ser Asp Ser Thr Ser Arg Arg Pro Ser Val Phe Glu Arg Leu
15 20 25 30
gga ccc agc act ggc agt aca gca gag aca cag tgc cgt aac tgg ctg 207
Gly Pro Ser Thr Gly Ser Thr Ala Glu Thr Gln Cys Arg Asn Trp Leu
35 40 45
aag act ggc aac tgc ctc tat gga aac aca tgt aga ttc gta cat ggc 255
Lys Thr Gly Asn Cys Leu Tyr Gly Asn Thr Cys Arg Phe Val His Gly
50 55 60
cct tca cct cgt ggt aaa ggt tat agc agc aat tat aga agg tca cca 303
Pro Ser Pro Arg Gly Lys Gly Tyr Ser Ser Asn Tyr Arg Arg Ser Pro
65 70 75
gaa aga cct aca ggg gat ctt aga gaa aga atg aag aac aag cgc caa 351
Glu Arg Pro Thr Gly Asp Leu Arg Glu Arg Met Lys Asn Lys Arg Gln
80 85 90
gac gtg gac act gag ccc cag aaa cga aat aca gag gag tca tcc tca 399
Asp Val Asp Thr Glu Pro Gln Lys Arg Asn Thr Glu Glu Ser Ser Ser
95 100 105 110
cct gtt agg aaa gaa tct tca aga ggg aga cat agg gaa aag gaa gac 447
Pro Val Arg Lys Glu Ser Ser Arg Gly Arg His Arg Glu Lys Glu Asp
115 120 125
ata aaa atc act aag gaa aga act cca gaa agt gaa gaa gaa aat gta 495
Ile Lys Ile Thr Lys Glu Arg Thr Pro Glu Ser Glu Glu Glu Asn Val
130 135 140
gaa tgg gaa act aat aga gat gat tct gac aat gga gat att aat tat 543
Glu Trp Glu Thr Asn Arg Asp Asp Ser Asp Asn Gly Asp Ile Asn Tyr
145 150 155
gat tat gtt cat gaa ttg tca ttg gaa atg aag cgt cag aag ata cag 591
Asp Tyr Val His Glu Leu Ser Leu Glu Met Lys Arg Gln Lys Ile Gln
160 165 170
agg gaa tta atg aag ctg gaa caa gaa aac atg gag aag aga gaa gaa 639
Arg Glu Leu Met Lys Leu Glu Gln Glu Asn Met Glu Lys Arg Glu Glu
175 180 185 190
att atc att aaa aag gag gtt tca cca gaa gtg gtt aga tca aaa ttg 687
Ile Ile Ile Lys Lys Glu Val Ser Pro Glu Val Val Arg Ser Lys Leu
195 200 205
tcc ccg tca cct tct cta aga aag tct agc aaa tct ccg aag cga aaa 735
Ser Pro Ser Pro Ser Leu Arg Lys Ser Ser Lys Ser Pro Lys Arg Lys
210 215 220
tca agc ccg aag tcg tct tca gct agc aag aaa gat agg aag aca tct 783
Ser Ser Pro Lys Ser Ser Ser Ala Ser Lys Lys Asp Arg Lys Thr Ser
225 230 235
gca gta tct tct ccc ctg ttg gac cag cag aga aat tca aaa acc aac 831
Ala Val Ser Ser Pro Leu Leu Asp Gln Gln Arg Asn Ser Lys Thr Asn
240 245 250
caa agt aaa aag aaa gga cca cgt act cct agt cca ccc cct cct ata 879
Gln Ser Lys Lys Lys Gly Pro Arg Thr Pro Ser Pro Pro Pro Pro Ile
255 260 265 270
cca gaa gat atc gct ctg ggg aaa aaa tac aaa gaa aaa tat aaa gta 927
Pro Glu Asp Ile Ala Leu Gly Lys Lys Tyr Lys Glu Lys Tyr Lys Val
275 280 285
aaa gac agg ata gaa gaa aaa aca aga gat gga aag gac aga gga cga 975
Lys Asp Arg Ile Glu Glu Lys Thr Arg Asp Gly Lys Asp Arg Gly Arg
290 295 300
gat ttt gaa cga caa aga gaa aag aga gac aag cca agg tct act tcc 1023
Asp Phe Glu Arg Gln Arg Glu Lys Arg Asp Lys Pro Arg Ser Thr Ser
305 310 315
cca gca gga cag cat cat tct cct ata tct tct aga cat cac tca tct 1071
Pro Ala Gly Gln His His Ser Pro Ile Ser Ser Arg His His Ser Ser
320 325 330
tcc tca caa tca gga tca tct att caa aga cat tct cct tct cct cgt 1119
Ser Ser Gln Ser Gly Ser Ser Ile Gln Arg His Ser Pro Ser Pro Arg
335 340 345 350
cga aaa aga act cct tca cca tct tat cag cgg aca cta act cca cct 1167
Arg Lys Arg Thr Pro Ser Pro Ser Tyr Gln Arg Thr Leu Thr Pro Pro
355 360 365
tta cga cgc tct gcc tct cct tat cct tca cat tct ttg tcg tct ccc 1215
Leu Arg Arg Ser Ala Ser Pro Tyr Pro Ser His Ser Leu Ser Ser Pro
370 375 380
cag aga aag cag agt cct cca aga cat cgc tct cca atg cga gag aaa 1263
Gln Arg Lys Gln Ser Pro Pro Arg His Arg Ser Pro Met Arg Glu Lys
385 390 395
ggg aga cat gat cat gaa cga act tca cag tct cat gat cga cgc cac 1311
Gly Arg His Asp His Glu Arg Thr Ser Gln Ser His Asp Arg Arg His
400 405 410
gaa agg agg gaa gat act agg ggc aaa cga gac aga gaa aag gac tca 1359
Glu Arg Arg Glu Asp Thr Arg Gly Lys Arg Asp Arg Glu Lys Asp Ser
415 420 425 430
aga gaa gaa cga gaa tat gaa cag gat cag agc tct tct aga gac cac 1407
Arg Glu Glu Arg Glu Tyr Glu Gln Asp Gln Ser Ser Ser Arg Asp His
435 440 445
aga gat gac aga gaa cct cga gat ggt cgg gat cgg aga gat gcc aga 1455
Arg Asp Asp Arg Glu Pro Arg Asp Gly Arg Asp Arg Arg Asp Ala Arg
450 455 460
gat act agg gac cga agg gaa cta aga gac tcc aga gac atg cgg gac 1503
Asp Thr Arg Asp Arg Arg Glu Leu Arg Asp Ser Arg Asp Met Arg Asp
465 470 475
tca agg gag atg aga gat tat agc aga gat acc aaa gag agc cgt gat 1551
Ser Arg Glu Met Arg Asp Tyr Ser Arg Asp Thr Lys Glu Ser Arg Asp
480 485 490
ccc aga gat tct cgg tcc act cgt gat gcc cat gac tac agg gac cgt 1599
Pro Arg Asp Ser Arg Ser Thr Arg Asp Ala His Asp Tyr Arg Asp Arg
495 500 505 510
gaa ggt cga gat act cat cga aag gag gat aca tat cca gaa gaa tcc 1647
Glu Gly Arg Asp Thr His Arg Lys Glu Asp Thr Tyr Pro Glu Glu Ser
515 520 525
cgg agt tat ggc cga aac cat ttg aga gaa gaa agt tct cgt acg gaa 1695
Arg Ser Tyr Gly Arg Asn His Leu Arg Glu Glu Ser Ser Arg Thr Glu
530 535 540
ata agg aat gag tcc aga aat gag tct cga agt gaa att aga aat gac 1743
Ile Arg Asn Glu Ser Arg Asn Glu Ser Arg Ser Glu Ile Arg Asn Asp
545 550 555
cga atg ggc cga agt agg ggg agg gtt cct gag tta cct gaa aag gga 1791
Arg Met Gly Arg Ser Arg Gly Arg Val Pro Glu Leu Pro Glu Lys Gly
560 565 570
agt cga ggc tca aga ggt tct caa att gat agt cac agt agt aat agc 1839
Ser Arg Gly Ser Arg Gly Ser Gln Ile Asp Ser His Ser Ser Asn Ser
575 580 585 590
aac tat cat gac agc tgg gaa act cga agt agc tat cct gaa aga gat 1887
Asn Tyr His Asp Ser Trp Glu Thr Arg Ser Ser Tyr Pro Glu Arg Asp
595 600 605
aga tat cct gaa aga gac aac aga gat caa gca agg gat tct tcc ttt 1935
Arg Tyr Pro Glu Arg Asp Asn Arg Asp Gln Ala Arg Asp Ser Ser Phe
610 615 620
gag aga aga cat gga gag cga gac cgt cgt gac aac aga gag aga gat 1983
Glu Arg Arg His Gly Glu Arg Asp Arg Arg Asp Asn Arg Glu Arg Asp
625 630 635
caa aga cca agc tca cca att cga cat cag gga agg aat gac gag ctt 2031
Gln Arg Pro Ser Ser Pro Ile Arg His Gln Gly Arg Asn Asp Glu Leu
640 645 650
gag cgt gat gaa aga aga gag gaa cga aga gta gac aga gtg gat gat 2079
Glu Arg Asp Glu Arg Arg Glu Glu Arg Arg Val Asp Arg Val Asp Asp
655 660 665 670
agg aga gat gaa agg gct aga gag aga gat cgg gaa cga gaa cga gac 2127
Arg Arg Asp Glu Arg Ala Arg Glu Arg Asp Arg Glu Arg Glu Arg Asp
675 680 685
agg gag cgg gag aga gag agg gaa cgt gaa cgg gat cgg gaa aga gaa 2175
Arg Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg Asp Arg Glu Arg Glu
690 695 700
aaa gag aga gaa cta gaa aga gag cgt gct agg gaa cgg gag aga gaa 2223
Lys Glu Arg Glu Leu Glu Arg Glu Arg Ala Arg Glu Arg Glu Arg Glu
705 710 715
aga gaa aaa gag aga gat cgt gaa agg gat aga gac cga gac cac gat 2271
Arg Glu Lys Glu Arg Asp Arg Glu Arg Asp Arg Asp Arg Asp His Asp
720 725 730
cga gag cgg gaa aga gag agg gaa cga gac agg gaa aaa gaa cgg gaa 2319
Arg Glu Arg Glu Arg Glu Arg Glu Arg Asp Arg Glu Lys Glu Arg Glu
735 740 745 750
cga gaa aga gaa gag aga gag agg gag aga gag cga gaa cgg gag aga 2367
Arg Glu Arg Glu Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg
755 760 765
gag cga gag cga gaa cgg gaa cga gaa aga gcg aga gaa agg gat aaa 2415
Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg Ala Arg Glu Arg Asp Lys
770 775 780
gaa cga gaa cgc caa agg gat tgg gaa gac aaa gac aaa gga cga gat 2463
Glu Arg Glu Arg Gln Arg Asp Trp Glu Asp Lys Asp Lys Gly Arg Asp
785 790 795
gac cgc aga gaa aag cga gaa gag atc cga gaa gat agg aat cca aga 2511
Asp Arg Arg Glu Lys Arg Glu Glu Ile Arg Glu Asp Arg Asn Pro Arg
800 805 810
gat gga cat gat gaa aga aaa tca aag aag cgc tat aga aat gaa ggg 2559
Asp Gly His Asp Glu Arg Lys Ser Lys Lys Arg Tyr Arg Asn Glu Gly
815 820 825 830
agt ccc agc cct aga cag tcc ccg aag cgc cgg cgt gaa cat tct ccg 2607
Ser Pro Ser Pro Arg Gln Ser Pro Lys Arg Arg Arg Glu His Ser Pro
835 840 845
gac agt gat gcc tac aac agt gga gat gat aaa aat gaa aaa cac aga 2655
Asp Ser Asp Ala Tyr Asn Ser Gly Asp Asp Lys Asn Glu Lys His Arg
850 855 860
ctc ttg agc caa gtt gta cga cct caa gaa tct cgt tct ctt agt ccc 2703
Leu Leu Ser Gln Val Val Arg Pro Gln Glu Ser Arg Ser Leu Ser Pro
865 870 875
tcg cac ctc aca gaa gac aga cag ggt aga tgg aaa gag gag gat cgt 2751
Ser His Leu Thr Glu Asp Arg Gln Gly Arg Trp Lys Glu Glu Asp Arg
880 885 890
aaa cca gaa agg aaa gag agt tca agg cgc tac gaa gaa cag gaa ctc 2799
Lys Pro Glu Arg Lys Glu Ser Ser Arg Arg Tyr Glu Glu Gln Glu Leu
895 900 905 910
aag gag aaa gtt tct tct gta gat aaa cag aga gaa cag aca gaa atc 2847
Lys Glu Lys Val Ser Ser Val Asp Lys Gln Arg Glu Gln Thr Glu Ile
915 920 925
ctg gaa agc tca aga atg cgt gca cag gac att ata gga cac cac cag 2895
Leu Glu Ser Ser Arg Met Arg Ala Gln Asp Ile Ile Gly His His Gln
930 935 940
tct gaa gat cga gag aca tct gat cga gct cat gat gaa aac aag aag 2943
Ser Glu Asp Arg Glu Thr Ser Asp Arg Ala His Asp Glu Asn Lys Lys
945 950 955
aaa gca aaa att caa aag aaa cca att aag aaa aag aaa gag gat gat 2991
Lys Ala Lys Ile Gln Lys Lys Pro Ile Lys Lys Lys Lys Glu Asp Asp
960 965 970
gtt gga ata gag agg ggt aac ata gag aca aca tct gaa gat ggt caa 3039
Val Gly Ile Glu Arg Gly Asn Ile Glu Thr Thr Ser Glu Asp Gly Gln
975 980 985 990
gta ttt tca cca aaa aaa gga cag aaa aag aaa agc att gaa aaa aaa 3087
Val Phe Ser Pro Lys Lys Gly Gln Lys Lys Lys Ser Ile Glu Lys Lys
995 1000 1005
cgt aaa aaa tcc aaa ggt gat tct gat att tct gat gaa gaa gca 3132
Arg Lys Lys Ser Lys Gly Asp Ser Asp Ile Ser Asp Glu Glu Ala
1010 1015 1020
gcc cag caa agt aag aag aaa aga ggc cca cgg act ccc cct ata 3177
Ala Gln Gln Ser Lys Lys Lys Arg Gly Pro Arg Thr Pro Pro Ile
1025 1030 1035
aca act aaa gag gaa ttg gtt gaa atg tgc aat ggt aag aat ggt 3222
Thr Thr Lys Glu Glu Leu Val Glu Met Cys Asn Gly Lys Asn Gly
1040 1045 1050
att cta gag gac tcc cag aaa aaa gaa gat aca gca ttc agt gac 3267
Ile Leu Glu Asp Ser Gln Lys Lys Glu Asp Thr Ala Phe Ser Asp
1055 1060 1065
tgg tct gat gag gat gtc cct gac cgt aca gag gtg aca gaa gca 3312
Trp Ser Asp Glu Asp Val Pro Asp Arg Thr Glu Val Thr Glu Ala
1070 1075 1080
gag cat act gcc acc gcc acg act cct ggt agt acc cct tct cct 3357
Glu His Thr Ala Thr Ala Thr Thr Pro Gly Ser Thr Pro Ser Pro
1085 1090 1095
cta tct tct ctt ctt cct cct cca ccg cct gtg gct act gcc act 3402
Leu Ser Ser Leu Leu Pro Pro Pro Pro Pro Val Ala Thr Ala Thr
1100 1105 1110
gct aca act gtg cct gca act ctt gct gcc act act gct gct gcc 3447
Ala Thr Thr Val Pro Ala Thr Leu Ala Ala Thr Thr Ala Ala Ala
1115 1120 1125
gcc acc tct ttc agc aca tct gcc atc act att tcc acc tct gcc 3492
Ala Thr Ser Phe Ser Thr Ser Ala Ile Thr Ile Ser Thr Ser Ala
1130 1135 1140
acc ccc acc aat acc acc aat aat act ttt gcc aat gaa gac tca 3537
Thr Pro Thr Asn Thr Thr Asn Asn Thr Phe Ala Asn Glu Asp Ser
1145 1150 1155
cac aga aaa tgc cac aga aca cga gta gaa aaa gta gag acg cct 3582
His Arg Lys Cys His Arg Thr Arg Val Glu Lys Val Glu Thr Pro
1160 1165 1170
cac gtg act ata gaa gat gca cag cat cgc aag cct atg gat caa 3627
His Val Thr Ile Glu Asp Ala Gln His Arg Lys Pro Met Asp Gln
1175 1180 1185
aag agg agc agc agc ctc ggg agc aat cgg agt aac cgt agt cat 3672
Lys Arg Ser Ser Ser Leu Gly Ser Asn Arg Ser Asn Arg Ser His
1190 1195 1200
acg tct ggt cgt ctt cgc tcc cca tcc aat gat tca gcc cat cga 3717
Thr Ser Gly Arg Leu Arg Ser Pro Ser Asn Asp Ser Ala His Arg
1205 1210 1215
agt gga gat gac caa agt ggt cga aag aga gta ctg cac agt ggc 3762
Ser Gly Asp Asp Gln Ser Gly Arg Lys Arg Val Leu His Ser Gly
1220 1225 1230
tca aga gat aga gaa aaa aca aaa agc ctg gaa atc aca gga gag 3807
Ser Arg Asp Arg Glu Lys Thr Lys Ser Leu Glu Ile Thr Gly Glu
1235 1240 1245
aga aaa tct agg att gat cag tta aag cgt gga gaa ccc agt cga 3852
Arg Lys Ser Arg Ile Asp Gln Leu Lys Arg Gly Glu Pro Ser Arg
1250 1255 1260
agt act tct tca gat cgc cag gat tca aga agc cat agt tca aga 3897
Ser Thr Ser Ser Asp Arg Gln Asp Ser Arg Ser His Ser Ser Arg
1265 1270 1275
aga agt tct cca gag tca gat cga cag gtc cat tca aga tct ggg 3942
Arg Ser Ser Pro Glu Ser Asp Arg Gln Val His Ser Arg Ser Gly
1280 1285 1290
tca ttt gat agc aga gac agg ctt caa gaa cga gat cga tat gaa 3987
Ser Phe Asp Ser Arg Asp Arg Leu Gln Glu Arg Asp Arg Tyr Glu
1295 1300 1305
cac gac aga gag cgc gag aga gag agg aga gat acg agg cag aga 4032
His Asp Arg Glu Arg Glu Arg Glu Arg Arg Asp Thr Arg Gln Arg
1310 1315 1320
gaa tgg gac cga gat gct gat aaa gat tgg cca cgc aac agg gat 4077
Glu Trp Asp Arg Asp Ala Asp Lys Asp Trp Pro Arg Asn Arg Asp
1325 1330 1335
cga gat aga ttg cga gaa cga gaa cga gag aga gaa cga gac aaa 4122
Arg Asp Arg Leu Arg Glu Arg Glu Arg Glu Arg Glu Arg Asp Lys
1340 1345 1350
agg aga gac ttg gat agg gaa aga gag aga cta att tct gat tct 4167
Arg Arg Asp Leu Asp Arg Glu Arg Glu Arg Leu Ile Ser Asp Ser
1355 1360 1365
gtt gaa agg gac agg gac aga gac aga gac aga act ttt gag agt 4212
Val Glu Arg Asp Arg Asp Arg Asp Arg Asp Arg Thr Phe Glu Ser
1370 1375 1380
tct caa ata gag tct gtg aaa cgc tgt gaa gca aaa ctg gaa ggt 4257
Ser Gln Ile Glu Ser Val Lys Arg Cys Glu Ala Lys Leu Glu Gly
1385 1390 1395
gaa cat gaa agg gat cta gaa agc act tcc cga gac tct cta gcc 4302
Glu His Glu Arg Asp Leu Glu Ser Thr Ser Arg Asp Ser Leu Ala
1400 1405 1410
ttg gat aaa gag aga atg gat aaa gat ctg gga tct gtg cag gga 4347
Leu Asp Lys Glu Arg Met Asp Lys Asp Leu Gly Ser Val Gln Gly
1415 1420 1425
ttt gaa gat aca aat aaa tcc gag aga act gag agt ctg gaa gca 4392
Phe Glu Asp Thr Asn Lys Ser Glu Arg Thr Glu Ser Leu Glu Ala
1430 1435 1440
gga gat gac gag tcc aag tta gat gat gca cat tca tta ggc tct 4437
Gly Asp Asp Glu Ser Lys Leu Asp Asp Ala His Ser Leu Gly Ser
1445 1450 1455
ggt gct gga gaa gga tac gag cca atc agt gat gac gaa cta gat 4482
Gly Ala Gly Glu Gly Tyr Glu Pro Ile Ser Asp Asp Glu Leu Asp
1460 1465 1470
gaa att ctg gca ggt gat gca gaa aag agg gag gac caa cag gat 4527
Glu Ile Leu Ala Gly Asp Ala Glu Lys Arg Glu Asp Gln Gln Asp
1475 1480 1485
gag gag aag atg cca gat ccc tta gat gtg ata gat gtg gat tgg 4572
Glu Glu Lys Met Pro Asp Pro Leu Asp Val Ile Asp Val Asp Trp
1490 1495 1500
tct ggt ctt atg cca aag cat cca aaa gaa cca cga gag cct ggg 4617
Ser Gly Leu Met Pro Lys His Pro Lys Glu Pro Arg Glu Pro Gly
1505 1510 1515
gct gca ctc tta aaa ttc aca cct gga gct gtt atg cta aga gtt 4662
Ala Ala Leu Leu Lys Phe Thr Pro Gly Ala Val Met Leu Arg Val
1520 1525 1530
ggg att tct aaa aag ttg gca ggt tct gaa ctc ttt gcc aaa gtc 4707
Gly Ile Ser Lys Lys Leu Ala Gly Ser Glu Leu Phe Ala Lys Val
1535 1540 1545
aaa gaa aca tgt cag aga ctt tta gaa aaa ccc aaa ggt agt ttc 4752
Lys Glu Thr Cys Gln Arg Leu Leu Glu Lys Pro Lys Gly Ser Phe
1550 1555 1560
att tta ctt taa ctatataatg tctgttaacc atttaagatg ccatctgaag 4804
Ile Leu Leu
gggattctga tctgttctta tgtagcactt aacactgtgt agaaactatt ttttgagaaa 4864
tcattttata atcattattt aaccctcatg gtcaaagttt ctctttaaaa tttattttga 4924
gaagaagagt tatcccacag aaaagttggg aaaagagtac aatgaccttt ttgtatgaaa 4984
attacttatt aacaggccag gcgtggtgtt gcatgtctgt agtcacagct actcagggag 5044
gttgaggcag caggattgct ggagcccagg aaattgaggc tgcagtgagc catgattgag 5104
ccaccacact ccaacctagg tgacagagca agaccctgtc tcaaaaaaaa aaaaacaaat 5164
taaccaataa gttctaatat caaagtgctc agtggtttgc ccttggctaa atgaagcaga 5224
gccaggaaaa acagactaca tatttttcat gtctaaagaa attgggtatt ttggcagccc 5284
tttcccctag acatctaccc aaatgcaggt gtgtaggttg agtctttaac aaagtgatta 5344
agagcttggt ctgtaaggcc ggatgatctg gatttcagta ggcacaccac ttactggcta 5404
ttacttaatc tgtgtgttag tgtcatcatc tgtaagtcag gaataatcat accaccaact 5464
tcctatggta attaggagca aatgagttat tacaggcaaa acacttagaa cagttcctgg 5524
catatagtaa tacccaataa atattaactg ctactttgaa aatatcctat cacgctgatt 5584
tttgacctca ctgcagcaat tttcagttat tccagattat ctagcttatg gattctggtg 5644
gtaggggttg tttggttttg gttttcactg tctctgtctc atctagtacc taccttagtt 5704
tattttgcaa cttactaata ctttattaat ggggagggac gagtagatgg taaaaagaag 5764
gaaaaggagg taaaaggtga aaggaacaac attaattaac aattttacgt catgtccctg 5824
gacataaaag tttagttagt attaaatttt tcactaatac aaaataaaaa aatattgttt 5884
tatgagtttt atgaattcat gcccttcctt tactctatta gcataagcag taaatttttt 5944
tattttaata tagcccaata aacctagagt atacatgtac aaaatacata taattgttaa 6004
cgtgtattaa ccgaaaaatg acccaagact tagttcttgc cctactgtat ctgccttgtt 6064
tggttggttc tgtgacctta agcaaataac tcctgtgagc ctcaatttta tttgtaaagt 6124
gatggaataa aacccctaaa atcttaccca cctctaaaga tatttgtttc tgtgaccttt 6184
tgctagtagc atttcaagtt aaaatctggt ttgattttgc tacccatgaa atacagttcg 6244
gcccttactt attgatgact taacctaaac agtgaaaata tgcactgtaa agggtggggt 6304
gatgtggctt aacaatcaga cttcttctat ttttgctgct atggtggttg tattagagaa 6364
ctgatgtatt atcttgaata aagactttgt cttgtttact gccctaaaaa aaaaaaaaaa 6424
aaaaa 6429


4
1564
PRT
Homo sapiens

4
Met Ser Lys Ile Arg Arg Lys Val Thr Val Glu Asn Thr Lys Thr Ile
1 5 10 15
Ser Asp Ser Thr Ser Arg Arg Pro Ser Val Phe Glu Arg Leu Gly Pro
20 25 30
Ser Thr Gly Ser Thr Ala Glu Thr Gln Cys Arg Asn Trp Leu Lys Thr
35 40 45
Gly Asn Cys Leu Tyr Gly Asn Thr Cys Arg Phe Val His Gly Pro Ser
50 55 60
Pro Arg Gly Lys Gly Tyr Ser Ser Asn Tyr Arg Arg Ser Pro Glu Arg
65 70 75 80
Pro Thr Gly Asp Leu Arg Glu Arg Met Lys Asn Lys Arg Gln Asp Val
85 90 95
Asp Thr Glu Pro Gln Lys Arg Asn Thr Glu Glu Ser Ser Ser Pro Val
100 105 110
Arg Lys Glu Ser Ser Arg Gly Arg His Arg Glu Lys Glu Asp Ile Lys
115 120 125
Ile Thr Lys Glu Arg Thr Pro Glu Ser Glu Glu Glu Asn Val Glu Trp
130 135 140
Glu Thr Asn Arg Asp Asp Ser Asp Asn Gly Asp Ile Asn Tyr Asp Tyr
145 150 155 160
Val His Glu Leu Ser Leu Glu Met Lys Arg Gln Lys Ile Gln Arg Glu
165 170 175
Leu Met Lys Leu Glu Gln Glu Asn Met Glu Lys Arg Glu Glu Ile Ile
180 185 190
Ile Lys Lys Glu Val Ser Pro Glu Val Val Arg Ser Lys Leu Ser Pro
195 200 205
Ser Pro Ser Leu Arg Lys Ser Ser Lys Ser Pro Lys Arg Lys Ser Ser
210 215 220
Pro Lys Ser Ser Ser Ala Ser Lys Lys Asp Arg Lys Thr Ser Ala Val
225 230 235 240
Ser Ser Pro Leu Leu Asp Gln Gln Arg Asn Ser Lys Thr Asn Gln Ser
245 250 255
Lys Lys Lys Gly Pro Arg Thr Pro Ser Pro Pro Pro Pro Ile Pro Glu
260 265 270
Asp Ile Ala Leu Gly Lys Lys Tyr Lys Glu Lys Tyr Lys Val Lys Asp
275 280 285
Arg Ile Glu Glu Lys Thr Arg Asp Gly Lys Asp Arg Gly Arg Asp Phe
290 295 300
Glu Arg Gln Arg Glu Lys Arg Asp Lys Pro Arg Ser Thr Ser Pro Ala
305 310 315 320
Gly Gln His His Ser Pro Ile Ser Ser Arg His His Ser Ser Ser Ser
325 330 335
Gln Ser Gly Ser Ser Ile Gln Arg His Ser Pro Ser Pro Arg Arg Lys
340 345 350
Arg Thr Pro Ser Pro Ser Tyr Gln Arg Thr Leu Thr Pro Pro Leu Arg
355 360 365
Arg Ser Ala Ser Pro Tyr Pro Ser His Ser Leu Ser Ser Pro Gln Arg
370 375 380
Lys Gln Ser Pro Pro Arg His Arg Ser Pro Met Arg Glu Lys Gly Arg
385 390 395 400
His Asp His Glu Arg Thr Ser Gln Ser His Asp Arg Arg His Glu Arg
405 410 415
Arg Glu Asp Thr Arg Gly Lys Arg Asp Arg Glu Lys Asp Ser Arg Glu
420 425 430
Glu Arg Glu Tyr Glu Gln Asp Gln Ser Ser Ser Arg Asp His Arg Asp
435 440 445
Asp Arg Glu Pro Arg Asp Gly Arg Asp Arg Arg Asp Ala Arg Asp Thr
450 455 460
Arg Asp Arg Arg Glu Leu Arg Asp Ser Arg Asp Met Arg Asp Ser Arg
465 470 475 480
Glu Met Arg Asp Tyr Ser Arg Asp Thr Lys Glu Ser Arg Asp Pro Arg
485 490 495
Asp Ser Arg Ser Thr Arg Asp Ala His Asp Tyr Arg Asp Arg Glu Gly
500 505 510
Arg Asp Thr His Arg Lys Glu Asp Thr Tyr Pro Glu Glu Ser Arg Ser
515 520 525
Tyr Gly Arg Asn His Leu Arg Glu Glu Ser Ser Arg Thr Glu Ile Arg
530 535 540
Asn Glu Ser Arg Asn Glu Ser Arg Ser Glu Ile Arg Asn Asp Arg Met
545 550 555 560
Gly Arg Ser Arg Gly Arg Val Pro Glu Leu Pro Glu Lys Gly Ser Arg
565 570 575
Gly Ser Arg Gly Ser Gln Ile Asp Ser His Ser Ser Asn Ser Asn Tyr
580 585 590
His Asp Ser Trp Glu Thr Arg Ser Ser Tyr Pro Glu Arg Asp Arg Tyr
595 600 605
Pro Glu Arg Asp Asn Arg Asp Gln Ala Arg Asp Ser Ser Phe Glu Arg
610 615 620
Arg His Gly Glu Arg Asp Arg Arg Asp Asn Arg Glu Arg Asp Gln Arg
625 630 635 640
Pro Ser Ser Pro Ile Arg His Gln Gly Arg Asn Asp Glu Leu Glu Arg
645 650 655
Asp Glu Arg Arg Glu Glu Arg Arg Val Asp Arg Val Asp Asp Arg Arg
660 665 670
Asp Glu Arg Ala Arg Glu Arg Asp Arg Glu Arg Glu Arg Asp Arg Glu
675 680 685
Arg Glu Arg Glu Arg Glu Arg Glu Arg Asp Arg Glu Arg Glu Lys Glu
690 695 700
Arg Glu Leu Glu Arg Glu Arg Ala Arg Glu Arg Glu Arg Glu Arg Glu
705 710 715 720
Lys Glu Arg Asp Arg Glu Arg Asp Arg Asp Arg Asp His Asp Arg Glu
725 730 735
Arg Glu Arg Glu Arg Glu Arg Asp Arg Glu Lys Glu Arg Glu Arg Glu
740 745 750
Arg Glu Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg Glu Arg
755 760 765
Glu Arg Glu Arg Glu Arg Glu Arg Ala Arg Glu Arg Asp Lys Glu Arg
770 775 780
Glu Arg Gln Arg Asp Trp Glu Asp Lys Asp Lys Gly Arg Asp Asp Arg
785 790 795 800
Arg Glu Lys Arg Glu Glu Ile Arg Glu Asp Arg Asn Pro Arg Asp Gly
805 810 815
His Asp Glu Arg Lys Ser Lys Lys Arg Tyr Arg Asn Glu Gly Ser Pro
820 825 830
Ser Pro Arg Gln Ser Pro Lys Arg Arg Arg Glu His Ser Pro Asp Ser
835 840 845
Asp Ala Tyr Asn Ser Gly Asp Asp Lys Asn Glu Lys His Arg Leu Leu
850 855 860
Ser Gln Val Val Arg Pro Gln Glu Ser Arg Ser Leu Ser Pro Ser His
865 870 875 880
Leu Thr Glu Asp Arg Gln Gly Arg Trp Lys Glu Glu Asp Arg Lys Pro
885 890 895
Glu Arg Lys Glu Ser Ser Arg Arg Tyr Glu Glu Gln Glu Leu Lys Glu
900 905 910
Lys Val Ser Ser Val Asp Lys Gln Arg Glu Gln Thr Glu Ile Leu Glu
915 920 925
Ser Ser Arg Met Arg Ala Gln Asp Ile Ile Gly His His Gln Ser Glu
930 935 940
Asp Arg Glu Thr Ser Asp Arg Ala His Asp Glu Asn Lys Lys Lys Ala
945 950 955 960
Lys Ile Gln Lys Lys Pro Ile Lys Lys Lys Lys Glu Asp Asp Val Gly
965 970 975
Ile Glu Arg Gly Asn Ile Glu Thr Thr Ser Glu Asp Gly Gln Val Phe
980 985 990
Ser Pro Lys Lys Gly Gln Lys Lys Lys Ser Ile Glu Lys Lys Arg Lys
995 1000 1005
Lys Ser Lys Gly Asp Ser Asp Ile Ser Asp Glu Glu Ala Ala Gln
1010 1015 1020
Gln Ser Lys Lys Lys Arg Gly Pro Arg Thr Pro Pro Ile Thr Thr
1025 1030 1035
Lys Glu Glu Leu Val Glu Met Cys Asn Gly Lys Asn Gly Ile Leu
1040 1045 1050
Glu Asp Ser Gln Lys Lys Glu Asp Thr Ala Phe Ser Asp Trp Ser
1055 1060 1065
Asp Glu Asp Val Pro Asp Arg Thr Glu Val Thr Glu Ala Glu His
1070 1075 1080
Thr Ala Thr Ala Thr Thr Pro Gly Ser Thr Pro Ser Pro Leu Ser
1085 1090 1095
Ser Leu Leu Pro Pro Pro Pro Pro Val Ala Thr Ala Thr Ala Thr
1100 1105 1110
Thr Val Pro Ala Thr Leu Ala Ala Thr Thr Ala Ala Ala Ala Thr
1115 1120 1125
Ser Phe Ser Thr Ser Ala Ile Thr Ile Ser Thr Ser Ala Thr Pro
1130 1135 1140
Thr Asn Thr Thr Asn Asn Thr Phe Ala Asn Glu Asp Ser His Arg
1145 1150 1155
Lys Cys His Arg Thr Arg Val Glu Lys Val Glu Thr Pro His Val
1160 1165 1170
Thr Ile Glu Asp Ala Gln His Arg Lys Pro Met Asp Gln Lys Arg
1175 1180 1185
Ser Ser Ser Leu Gly Ser Asn Arg Ser Asn Arg Ser His Thr Ser
1190 1195 1200
Gly Arg Leu Arg Ser Pro Ser Asn Asp Ser Ala His Arg Ser Gly
1205 1210 1215
Asp Asp Gln Ser Gly Arg Lys Arg Val Leu His Ser Gly Ser Arg
1220 1225 1230
Asp Arg Glu Lys Thr Lys Ser Leu Glu Ile Thr Gly Glu Arg Lys
1235 1240 1245
Ser Arg Ile Asp Gln Leu Lys Arg Gly Glu Pro Ser Arg Ser Thr
1250 1255 1260
Ser Ser Asp Arg Gln Asp Ser Arg Ser His Ser Ser Arg Arg Ser
1265 1270 1275
Ser Pro Glu Ser Asp Arg Gln Val His Ser Arg Ser Gly Ser Phe
1280 1285 1290
Asp Ser Arg Asp Arg Leu Gln Glu Arg Asp Arg Tyr Glu His Asp
1295 1300 1305
Arg Glu Arg Glu Arg Glu Arg Arg Asp Thr Arg Gln Arg Glu Trp
1310 1315 1320
Asp Arg Asp Ala Asp Lys Asp Trp Pro Arg Asn Arg Asp Arg Asp
1325 1330 1335
Arg Leu Arg Glu Arg Glu Arg Glu Arg Glu Arg Asp Lys Arg Arg
1340 1345 1350
Asp Leu Asp Arg Glu Arg Glu Arg Leu Ile Ser Asp Ser Val Glu
1355 1360 1365
Arg Asp Arg Asp Arg Asp Arg Asp Arg Thr Phe Glu Ser Ser Gln
1370 1375 1380
Ile Glu Ser Val Lys Arg Cys Glu Ala Lys Leu Glu Gly Glu His
1385 1390 1395
Glu Arg Asp Leu Glu Ser Thr Ser Arg Asp Ser Leu Ala Leu Asp
1400 1405 1410
Lys Glu Arg Met Asp Lys Asp Leu Gly Ser Val Gln Gly Phe Glu
1415 1420 1425
Asp Thr Asn Lys Ser Glu Arg Thr Glu Ser Leu Glu Ala Gly Asp
1430 1435 1440
Asp Glu Ser Lys Leu Asp Asp Ala His Ser Leu Gly Ser Gly Ala
1445 1450 1455
Gly Glu Gly Tyr Glu Pro Ile Ser Asp Asp Glu Leu Asp Glu Ile
1460 1465 1470
Leu Ala Gly Asp Ala Glu Lys Arg Glu Asp Gln Gln Asp Glu Glu
1475 1480 1485
Lys Met Pro Asp Pro Leu Asp Val Ile Asp Val Asp Trp Ser Gly
1490 1495 1500
Leu Met Pro Lys His Pro Lys Glu Pro Arg Glu Pro Gly Ala Ala
1505 1510 1515
Leu Leu Lys Phe Thr Pro Gly Ala Val Met Leu Arg Val Gly Ile
1520 1525 1530
Ser Lys Lys Leu Ala Gly Ser Glu Leu Phe Ala Lys Val Lys Glu
1535 1540 1545
Thr Cys Gln Arg Leu Leu Glu Lys Pro Lys Gly Ser Phe Ile Leu
1550 1555 1560
Leu


5
6164
DNA
Homo sapiens

CDS
(314)..(2398)


5
gtaaaacttt ggacaatact tattacttta ttgactgtgt tagtttcttc ttcttaagta 60
gactgttgtc atctcttttc ttttgagtcc aattttccta tagtttgttt atgtcaatgg 120
ctcgacaaaa tgataaaata tatttccaga aagcacatgg atttggaact ctctcttgtt 180
atgtttatat taggctttat tttaaaggca agtgagactg cttcaaataa aacaacttca 240
agcttccaag aaacagttaa gaggaggcag agaggagcag aaacacttct ttgctgacac 300
ttacactgtt gcc atg gac cta cat aag cag tgg gag aac aca gag act 349
Met Asp Leu His Lys Gln Trp Glu Asn Thr Glu Thr
1 5 10
aac tgg cat aag gaa aag atg gaa tta ctg gac cag ttt gac aat gaa 397
Asn Trp His Lys Glu Lys Met Glu Leu Leu Asp Gln Phe Asp Asn Glu
15 20 25
aga aag gaa tgg gaa agt caa tgg aag att atg cag aag aaa ata gaa 445
Arg Lys Glu Trp Glu Ser Gln Trp Lys Ile Met Gln Lys Lys Ile Glu
30 35 40
gag ctt tgc cgg gaa gta aag ctt tgg agg aaa atc aat atc aat gaa 493
Glu Leu Cys Arg Glu Val Lys Leu Trp Arg Lys Ile Asn Ile Asn Glu
45 50 55 60
agt gct aag atc att gat ctt tac cat gag aag acc att cca gag aaa 541
Ser Ala Lys Ile Ile Asp Leu Tyr His Glu Lys Thr Ile Pro Glu Lys
65 70 75
gtg ata gaa tct tcc cca aat tac ccc gat tta gga caa agt gaa ttt 589
Val Ile Glu Ser Ser Pro Asn Tyr Pro Asp Leu Gly Gln Ser Glu Phe
80 85 90
ata agg acg aat cac aaa gat ggt ctg aga aaa gaa aat aaa aga gag 637
Ile Arg Thr Asn His Lys Asp Gly Leu Arg Lys Glu Asn Lys Arg Glu
95 100 105
cag agc tta gtc agt gga gga aat caa atg tgt aag gaa caa aaa gca 685
Gln Ser Leu Val Ser Gly Gly Asn Gln Met Cys Lys Glu Gln Lys Ala
110 115 120
aca aaa aaa tca aaa gta ggg ttt ttg gat cct ttg gct aca gac aac 733
Thr Lys Lys Ser Lys Val Gly Phe Leu Asp Pro Leu Ala Thr Asp Asn
125 130 135 140
caa aag gaa tgt gag gcc tgg cct gac ctg agg act tct gag gaa gac 781
Gln Lys Glu Cys Glu Ala Trp Pro Asp Leu Arg Thr Ser Glu Glu Asp
145 150 155
agc aag agc tgt tct ggc gcc ctc agt aca gct ctt gaa gaa ctt gcg 829
Ser Lys Ser Cys Ser Gly Ala Leu Ser Thr Ala Leu Glu Glu Leu Ala
160 165 170
aag gtg agt gaa gaa tta tgc agc ttt caa gag gaa att cga aag cgg 877
Lys Val Ser Glu Glu Leu Cys Ser Phe Gln Glu Glu Ile Arg Lys Arg
175 180 185
tct aac cat aga agg atg aag tca gat tct ttt ctc cag gaa atg cca 925
Ser Asn His Arg Arg Met Lys Ser Asp Ser Phe Leu Gln Glu Met Pro
190 195 200
aat gta act aat ata cct cat ggg gac ccc atg atc aac aat gac cag 973
Asn Val Thr Asn Ile Pro His Gly Asp Pro Met Ile Asn Asn Asp Gln
205 210 215 220
tgc att ctt cca atc agt tta gaa aaa gaa aaa cag aaa aac agg aag 1021
Cys Ile Leu Pro Ile Ser Leu Glu Lys Glu Lys Gln Lys Asn Arg Lys
225 230 235
aat ctg agc tgt acc aat gtg ctc cag agc aat tct acg aaa aaa tgt 1069
Asn Leu Ser Cys Thr Asn Val Leu Gln Ser Asn Ser Thr Lys Lys Cys
240 245 250
gga att gat aca atc gat tta aaa aga aat gaa act cca cca gtt cct 1117
Gly Ile Asp Thr Ile Asp Leu Lys Arg Asn Glu Thr Pro Pro Val Pro
255 260 265
cct cca aga agc acc tct cga aat ttt ccc agc tcg gat tct gaa caa 1165
Pro Pro Arg Ser Thr Ser Arg Asn Phe Pro Ser Ser Asp Ser Glu Gln
270 275 280
gcc tat gaa aga tgg aag gaa agg tta gac cac aac agc tgg gtg ccc 1213
Ala Tyr Glu Arg Trp Lys Glu Arg Leu Asp His Asn Ser Trp Val Pro
285 290 295 300
cat gag ggt cga agt aaa agg aat tac aac cct cac ttc cct ttg aga 1261
His Glu Gly Arg Ser Lys Arg Asn Tyr Asn Pro His Phe Pro Leu Arg
305 310 315
caa caa gag atg tct atg ttg tat cca aat gaa ggg aaa act tcg aaa 1309
Gln Gln Glu Met Ser Met Leu Tyr Pro Asn Glu Gly Lys Thr Ser Lys
320 325 330
gat ggt atc atc ttt tcc tct ttg gta cca gaa gtc aaa ata gat agc 1357
Asp Gly Ile Ile Phe Ser Ser Leu Val Pro Glu Val Lys Ile Asp Ser
335 340 345
aag cct cca agt aat gaa gat gtt gga ctt agc atg tgg tca tgt gac 1405
Lys Pro Pro Ser Asn Glu Asp Val Gly Leu Ser Met Trp Ser Cys Asp
350 355 360
att ggg ata ggt gca aaa agg agc ccc tct act tcg tgg ttt cag aaa 1453
Ile Gly Ile Gly Ala Lys Arg Ser Pro Ser Thr Ser Trp Phe Gln Lys
365 370 375 380
acc tgc tct acc ccc agt aat cca aaa tat gaa atg gtg atc cca gat 1501
Thr Cys Ser Thr Pro Ser Asn Pro Lys Tyr Glu Met Val Ile Pro Asp
385 390 395
cac cct gct aaa tct cat cct gat ctt cat gta agt aat gac tgt agc 1549
His Pro Ala Lys Ser His Pro Asp Leu His Val Ser Asn Asp Cys Ser
400 405 410
tcc tca gta gca gag agc agt agc cca ctt aga aat ttc agt tgt ggc 1597
Ser Ser Val Ala Glu Ser Ser Ser Pro Leu Arg Asn Phe Ser Cys Gly
415 420 425
ttt gaa agg act aca agg aat gag aag ctg gca gca aag act gat gaa 1645
Phe Glu Arg Thr Thr Arg Asn Glu Lys Leu Ala Ala Lys Thr Asp Glu
430 435 440
ttt aac aga act gta ttt aga aca gat aga aat tgt cag gca ata cag 1693
Phe Asn Arg Thr Val Phe Arg Thr Asp Arg Asn Cys Gln Ala Ile Gln
445 450 455 460
caa aat cac agc tgc tca aaa tca tcg gag gat ctc aag ccc tgt gat 1741
Gln Asn His Ser Cys Ser Lys Ser Ser Glu Asp Leu Lys Pro Cys Asp
465 470 475
acc tca tct act cac aca ggt agc ata tca caa agt aac gat gtg tcc 1789
Thr Ser Ser Thr His Thr Gly Ser Ile Ser Gln Ser Asn Asp Val Ser
480 485 490
ggt att tgg aaa acc aat gcc cac atg cct gtg ccc atg gaa aat gtg 1837
Gly Ile Trp Lys Thr Asn Ala His Met Pro Val Pro Met Glu Asn Val
495 500 505
cct gat aat ccc acc aag aaa tcc aca aca ggc cta gta aga caa atg 1885
Pro Asp Asn Pro Thr Lys Lys Ser Thr Thr Gly Leu Val Arg Gln Met
510 515 520
cag gga cac cta agt cct cgc agt tat cga aat atg ctc cac gag cat 1933
Gln Gly His Leu Ser Pro Arg Ser Tyr Arg Asn Met Leu His Glu His
525 530 535 540
gac tgg aga ccg agt aat ttg tct ggc cgt ccg agg tca gct gat ccc 1981
Asp Trp Arg Pro Ser Asn Leu Ser Gly Arg Pro Arg Ser Ala Asp Pro
545 550 555
agg tca aat tat ggt gtt gtg gaa aag ctg ctg aaa acc tat gag aca 2029
Arg Ser Asn Tyr Gly Val Val Glu Lys Leu Leu Lys Thr Tyr Glu Thr
560 565 570
gca aca gag tct gca ttg caa aat tct aag tgc ttc cag gat aat tgg 2077
Ala Thr Glu Ser Ala Leu Gln Asn Ser Lys Cys Phe Gln Asp Asn Trp
575 580 585
acc aaa tgt aat tct gat gtc agt ggt ggt gcc aca tta agt cag cat 2125
Thr Lys Cys Asn Ser Asp Val Ser Gly Gly Ala Thr Leu Ser Gln His
590 595 600
tta gaa atg ctc caa atg gaa caa cag ttt cag caa aag aca gct gtg 2173
Leu Glu Met Leu Gln Met Glu Gln Gln Phe Gln Gln Lys Thr Ala Val
605 610 615 620
tgg ggg gga cag gaa gtg aag caa gga ata gat ccg aaa aag ata aca 2221
Trp Gly Gly Gln Glu Val Lys Gln Gly Ile Asp Pro Lys Lys Ile Thr
625 630 635
gag gaa tcc atg tca gtg aac gcc tca cat gga aaa gga ttt tcc cga 2269
Glu Glu Ser Met Ser Val Asn Ala Ser His Gly Lys Gly Phe Ser Arg
640 645 650
cct gct aga cca gca aat cgt cgt ctc ccc tcc aga tgg gca tcc aga 2317
Pro Ala Arg Pro Ala Asn Arg Arg Leu Pro Ser Arg Trp Ala Ser Arg
655 660 665
tct cca tct gca ccc cct gcc ttg cgg aga act acc cac aac tat acc 2365
Ser Pro Ser Ala Pro Pro Ala Leu Arg Arg Thr Thr His Asn Tyr Thr
670 675 680
att tct ctg cga tcc gaa gca ttg atg gtt taa gtctttggcc tggattgcta 2418
Ile Ser Leu Arg Ser Glu Ala Leu Met Val
685 690
tattacagaa gttctagtcc cacttgtcaa acagagcatt ctgagtgttt acaggcggac 2478
ctgttctctt ccgacaagca atttgaatct taactttcca tcagtcttca gtgtttttaa 2538
tctaaggaat aattatcttc ctgcattttg atttcttaga tcagaatttt ttaatgccat 2598
cctcattagt tttccaatac aatataagtt gaaacaatgt acaatattgt atattctttg 2658
ttgcaagtgg cagaaagtaa ggttatgtgc atggccatgt gtttgtaggt gcatgtgttg 2718
aaataggaag tatcctagta tgtatttaga tatgaaaaac ttatgtgcta gtgttgactt 2778
tgaaattata acatgtatac ctatatattc tttgtgttta tttaaaagtt ttgaaaatat 2838
gcagtactgt ttatattttg tatacctttt aataggtatc cacttaaggc atttgcagta 2898
caaatattaa ttgaccactt ccttggcccc cagctacaat gaaaaagaag aattatgcac 2958
acatctaaca ttggtagatt tctaaagaca actcataaat aatttcttaa cccatataag 3018
gataaaataa taccattgat attcttgttt attcttttta aataaaaatg tcacaagttt 3078
aatagatcag ccttgtaaag caagcataaa atgttcataa atgttttata tattatttgg 3138
tagtctagta tggctttaac tgaatatttg atcctcagag acagtatcat gagactgcat 3198
tataaatgac atgattaaat gatgaattta ttttgtcagc ctcagcaaca aacatttcct 3258
aaatgggatg caaaaagaaa ctgaatgatg ttgaatttta gtttttcttt aagttgtggt 3318
aagcttttag tttagctgct ttaacatgga gtcatacata cttagaggta agtcatttat 3378
tatttttttc ctttttctaa tcttttcctt aaaattaata gataacaaac taagttactt 3438
ttttactaac aaggaagatc aggaataata tttctttgaa agctgaaatt atacttctca 3498
cagtttgcta ccgaaaaaag gcttaaacta aaccttgaca tccacagtag catcaggaat 3558
agaaatgtgt attttggcta cagtttgcat acagtgaaca cataaaatct atattgaaaa 3618
ctgacagaaa tatgaatgtc gaggggcttg gaattctaaa tggaagattt tagaaggaac 3678
tttgctctct actgtcacta tataaaacca attatgttat gttattagat attaactcta 3738
tttaagcttt tcttttacta agaaattctt atgccaaatg tattccaaga gccatctcct 3798
tatgatgtat ttgaaccatt tagagaaatt cacttcattg taccccatga cctgaggtaa 3858
agaaaataat tttcaaattg cagacttcct tgaaaggctc aagactgtag catggtgatg 3918
tctagattca tactttactg taaggacagt ttcggtagtt aagtggaatt aaaggtctag 3978
agtgatttgt attggatggt aactaaggtc tatacatcta ctcttttaat tcttatttcc 4038
ttcaggaaga tccttttcca caggaagcta tcaaagaaaa gtaaactaga caccaagtaa 4098
tatcactctc ataatatgct ttccagctag aggggagaaa acaccaggaa agaggaaccc 4158
tgggtcataa aatgacggac ctgttaggaa aatgctgttg tgtgacaatg gagagcctgc 4218
ccaaggactg tgcaacctat ctgttcctct ccaccagtgt atcccaagta gtctggtatg 4278
atctgtggtt ccttagaata ttgaggatct ctttaaaaaa tgaaatttct gatctcaccc 4338
catattacta aagcaaaatt tccaggggta gggactggga ctccagaacc attaataaaa 4398
caaaacaaaa caaagcaaaa tattgatgat caggcagatt tgaaaacagt gacattgctt 4458
gatctctgaa tggatggatg cccttgggtg gtcacttttc ttcctaggac ttgcctttgt 4518
tatctgtaaa ttagaatggc tatactttca gacttcacaa ttttaagcca cttttttcta 4578
ttaacagttg aatgaaccag tgggacacat tttaacgtct tcttatgttg actaaaatta 4638
tagttagagc tgagaaaaaa aaaatagcat ctagtccaac tccttgattg taaaactgaa 4698
aaactaaggt tatttgaatg ttctgttttc tctttttaaa tattttataa cttttaaatg 4758
gaaaaaccta ttaggtaaat ggaaataatc cttgaaaata gtttttgatg ttttgtgatt 4818
tttaactggt aaatttctac tttaggtggg cattttcttc cctagaatat gccctttatt 4878
atgctatcat tgctagattt aaagggactt gtaagcattt ctggaaatat ttgatttaaa 4938
aacatatatt aatagatgtt ttccctagca gacttttgga gcaaaaatat tattttagtt 4998
cagcagagga ttactgatat tatgggctga tctcagaaag gaataaggat gaggcagaga 5058
ggagtacttg agtttgtgtg tgtgtgtgtg tgtgtgtgtt tgtgtcagtg tcacataagt 5118
tctccatatt gccttatgtc ccaaagccaa atataaaaat ataaatgatg ctttgtataa 5178
ttcattttat caaaaattac ccataacttt catttgtttt tatatcgaca atgaagatga 5238
tcatatttca ttttgcagat gtggccataa aatattattt acttctatat aggtgatttt 5298
accaggttta gttatcctga gaaaacatct ggacttaaga gtttctgctt ccctacaaag 5358
atctttaaag ttatttttag gcacatttgt gacaaacaac tacttgatat tgaaatctcc 5418
ttcagccatt agaagctatc aaataaagta ggtgtaaaaa caactgtctg tggcatttgt 5478
atacatcgag aacatttttc tttccctcat tttctgcagt gaactccagt aaagctaagt 5538
gtcttatgaa atctaaactc atatatgtac acagttcact ctagcttctt ccaaaatatc 5598
tctaggtagt acaactgaag ccaaacctgc ctgacttcct gctcctggcc acccaaaact 5658
ccatatggct tctcgtacac tgacatcctc tctctaccca tttaactgct aattgagtct 5718
gataaaagtc ttctttgaaa aaagttttta cttctaagat ttgcatttac atcataaaat 5778
taaaccattt tcaggaaaat cagatttttt tattacagta ctatttgctt taaattcggc 5838
atgtttttct taagtagcaa gtacatgtat cggaacttag aactggtggg cgcggtggct 5898
cttgcctgta atcccagcac tttgggaggc caaggtgggg ggatcacgag gtcaggagat 5958
ggagaccatc ctggtttcat cacggtgaaa ccccctctct gctaaaaata caaaaaatta 6018
gccaggcatt gtggtggtca cctgtagtcc cagctgctcg ggaggctgag gcaggagaat 6078
ggcatgaacc cgggaggcag agcttgcagt gagcagagat cgcgccactg cactccagcc 6138
tgggtgacag agtgagactc tgtctc 6164


6
694
PRT
Homo sapiens

6
Met Asp Leu His Lys Gln Trp Glu Asn Thr Glu Thr Asn Trp His Lys
1 5 10 15
Glu Lys Met Glu Leu Leu Asp Gln Phe Asp Asn Glu Arg Lys Glu Trp
20 25 30
Glu Ser Gln Trp Lys Ile Met Gln Lys Lys Ile Glu Glu Leu Cys Arg
35 40 45
Glu Val Lys Leu Trp Arg Lys Ile Asn Ile Asn Glu Ser Ala Lys Ile
50 55 60
Ile Asp Leu Tyr His Glu Lys Thr Ile Pro Glu Lys Val Ile Glu Ser
65 70 75 80
Ser Pro Asn Tyr Pro Asp Leu Gly Gln Ser Glu Phe Ile Arg Thr Asn
85 90 95
His Lys Asp Gly Leu Arg Lys Glu Asn Lys Arg Glu Gln Ser Leu Val
100 105 110
Ser Gly Gly Asn Gln Met Cys Lys Glu Gln Lys Ala Thr Lys Lys Ser
115 120 125
Lys Val Gly Phe Leu Asp Pro Leu Ala Thr Asp Asn Gln Lys Glu Cys
130 135 140
Glu Ala Trp Pro Asp Leu Arg Thr Ser Glu Glu Asp Ser Lys Ser Cys
145 150 155 160
Ser Gly Ala Leu Ser Thr Ala Leu Glu Glu Leu Ala Lys Val Ser Glu
165 170 175
Glu Leu Cys Ser Phe Gln Glu Glu Ile Arg Lys Arg Ser Asn His Arg
180 185 190
Arg Met Lys Ser Asp Ser Phe Leu Gln Glu Met Pro Asn Val Thr Asn
195 200 205
Ile Pro His Gly Asp Pro Met Ile Asn Asn Asp Gln Cys Ile Leu Pro
210 215 220
Ile Ser Leu Glu Lys Glu Lys Gln Lys Asn Arg Lys Asn Leu Ser Cys
225 230 235 240
Thr Asn Val Leu Gln Ser Asn Ser Thr Lys Lys Cys Gly Ile Asp Thr
245 250 255
Ile Asp Leu Lys Arg Asn Glu Thr Pro Pro Val Pro Pro Pro Arg Ser
260 265 270
Thr Ser Arg Asn Phe Pro Ser Ser Asp Ser Glu Gln Ala Tyr Glu Arg
275 280 285
Trp Lys Glu Arg Leu Asp His Asn Ser Trp Val Pro His Glu Gly Arg
290 295 300
Ser Lys Arg Asn Tyr Asn Pro His Phe Pro Leu Arg Gln Gln Glu Met
305 310 315 320
Ser Met Leu Tyr Pro Asn Glu Gly Lys Thr Ser Lys Asp Gly Ile Ile
325 330 335
Phe Ser Ser Leu Val Pro Glu Val Lys Ile Asp Ser Lys Pro Pro Ser
340 345 350
Asn Glu Asp Val Gly Leu Ser Met Trp Ser Cys Asp Ile Gly Ile Gly
355 360 365
Ala Lys Arg Ser Pro Ser Thr Ser Trp Phe Gln Lys Thr Cys Ser Thr
370 375 380
Pro Ser Asn Pro Lys Tyr Glu Met Val Ile Pro Asp His Pro Ala Lys
385 390 395 400
Ser His Pro Asp Leu His Val Ser Asn Asp Cys Ser Ser Ser Val Ala
405 410 415
Glu Ser Ser Ser Pro Leu Arg Asn Phe Ser Cys Gly Phe Glu Arg Thr
420 425 430
Thr Arg Asn Glu Lys Leu Ala Ala Lys Thr Asp Glu Phe Asn Arg Thr
435 440 445
Val Phe Arg Thr Asp Arg Asn Cys Gln Ala Ile Gln Gln Asn His Ser
450 455 460
Cys Ser Lys Ser Ser Glu Asp Leu Lys Pro Cys Asp Thr Ser Ser Thr
465 470 475 480
His Thr Gly Ser Ile Ser Gln Ser Asn Asp Val Ser Gly Ile Trp Lys
485 490 495
Thr Asn Ala His Met Pro Val Pro Met Glu Asn Val Pro Asp Asn Pro
500 505 510
Thr Lys Lys Ser Thr Thr Gly Leu Val Arg Gln Met Gln Gly His Leu
515 520 525
Ser Pro Arg Ser Tyr Arg Asn Met Leu His Glu His Asp Trp Arg Pro
530 535 540
Ser Asn Leu Ser Gly Arg Pro Arg Ser Ala Asp Pro Arg Ser Asn Tyr
545 550 555 560
Gly Val Val Glu Lys Leu Leu Lys Thr Tyr Glu Thr Ala Thr Glu Ser
565 570 575
Ala Leu Gln Asn Ser Lys Cys Phe Gln Asp Asn Trp Thr Lys Cys Asn
580 585 590
Ser Asp Val Ser Gly Gly Ala Thr Leu Ser Gln His Leu Glu Met Leu
595 600 605
Gln Met Glu Gln Gln Phe Gln Gln Lys Thr Ala Val Trp Gly Gly Gln
610 615 620
Glu Val Lys Gln Gly Ile Asp Pro Lys Lys Ile Thr Glu Glu Ser Met
625 630 635 640
Ser Val Asn Ala Ser His Gly Lys Gly Phe Ser Arg Pro Ala Arg Pro
645 650 655
Ala Asn Arg Arg Leu Pro Ser Arg Trp Ala Ser Arg Ser Pro Ser Ala
660 665 670
Pro Pro Ala Leu Arg Arg Thr Thr His Asn Tyr Thr Ile Ser Leu Arg
675 680 685
Ser Glu Ala Leu Met Val
690


7
7014
DNA
Homo sapiens

CDS
(1164)..(3248)


7
agcagaacaa gcgcatcacg gcggagctca acaagtacaa gtacaagtcc ggcggccacg 60
acagcgcgcg gcaccacgac aacgccaaga ccgaggccct gcaggaggag ctgaaggcgg 120
cgcgcctgca gatcaacgag ctcagcggca aggtcatgca gctgcagtac gagaaccgcg 180
tgcttatgtc caacatgcag cgctacgacc tggcctcgca cctgggcatc cgcggcagcc 240
cccgcgacag cgacgccgag agcgacgcgg gcaagaagga gagcgacgac gactcgcggc 300
ctccgcaccg caagcgcgaa gggcccatcg gcggcgagag cgactcggag gaggtgcgca 360
acatccgctg cctcacgccc actcgctcct tctacccggc gcccgggccc tggcccaaga 420
gcttctccga tcggcagcag atgaaggaca tccgctcgga ggccgagcgc ctgggcaaga 480
ccatcgaccg gctcatcgcc gacacgagca ccatcatcac cgaggcgcgc atctacgtgg 540
ccaacgggga cctgttcgga ctcatggacg aggaggacga cggcagccgc atccgggagc 600
acgagctgct ctaccgcatc aacgctcaga tgaaggcctt ccgcaaggag ctgcagacct 660
tcatcgaccg cctcgaggtg cccaagtctg cggacgaccg cggcgccgag gagcccattt 720
ccgtgagtca gatgttccag cctatcattt tacttattct cattcttgta ttattttcat 780
cactttctta cacaacaata tttaaacttg tcttcctttt tacactgttt tttgtactgt 840
aaatctttca tcatttacca ttcattgtag tattttcagt ttgtttattt tgttcaccct 900
tcaagacaag aagtaaaaga agtataattt ctgtagtaac caatgctata aaaacactga 960
agactgctta tttctttaaa aagatacaac tcatcttacc aagaccaaat tcaataagaa 1020
gcccaaacac taaaatattt caggctttat tttaaaggca agtgagactg cttcaaataa 1080
aacaacttca agcttccaag aaacagttaa gaggaggcag agaggagcag aaacacttct 1140
ttgctgacac ttacactgtt gcc atg gac cta cat aag cag tgg gag aac aca 1193
Met Asp Leu His Lys Gln Trp Glu Asn Thr
1 5 10
gag act aac tgg cat aag gaa aag atg gaa tta ctg gac cag ttt gac 1241
Glu Thr Asn Trp His Lys Glu Lys Met Glu Leu Leu Asp Gln Phe Asp
15 20 25
aat gaa aga aag gaa tgg gaa agt caa tgg aag att atg cag aag aaa 1289
Asn Glu Arg Lys Glu Trp Glu Ser Gln Trp Lys Ile Met Gln Lys Lys
30 35 40
ata gaa gag ctt tgc cgg gaa gta aag ctt tgg agg aaa atc aat atc 1337
Ile Glu Glu Leu Cys Arg Glu Val Lys Leu Trp Arg Lys Ile Asn Ile
45 50 55
aat gaa agt gct aag atc att gat ctt tac cat gag aag acc att cca 1385
Asn Glu Ser Ala Lys Ile Ile Asp Leu Tyr His Glu Lys Thr Ile Pro
60 65 70
gag aaa gtg ata gaa tct tcc cca aat tac ccc gat tta gga caa agt 1433
Glu Lys Val Ile Glu Ser Ser Pro Asn Tyr Pro Asp Leu Gly Gln Ser
75 80 85 90
gaa ttt ata agg acg aat cac aaa gat ggt ctg aga aaa gaa aat aaa 1481
Glu Phe Ile Arg Thr Asn His Lys Asp Gly Leu Arg Lys Glu Asn Lys
95 100 105
aga gag cag agc tta gtc agt gga gga aat caa atg tgt aag gaa caa 1529
Arg Glu Gln Ser Leu Val Ser Gly Gly Asn Gln Met Cys Lys Glu Gln
110 115 120
aaa gca aca aaa aaa tca aaa gta ggg ttt ttg gat cct ttg gct aca 1577
Lys Ala Thr Lys Lys Ser Lys Val Gly Phe Leu Asp Pro Leu Ala Thr
125 130 135
gac aac caa aag gaa tgt gag gcc tgg cct gac ctg agg act tct gag 1625
Asp Asn Gln Lys Glu Cys Glu Ala Trp Pro Asp Leu Arg Thr Ser Glu
140 145 150
gaa gac agc aag agc tgt tct ggc gcc ctc agt aca gct ctt gaa gaa 1673
Glu Asp Ser Lys Ser Cys Ser Gly Ala Leu Ser Thr Ala Leu Glu Glu
155 160 165 170
ctt gcg aag gtg agt gaa gaa tta tgc agc ttt caa gag gaa att cga 1721
Leu Ala Lys Val Ser Glu Glu Leu Cys Ser Phe Gln Glu Glu Ile Arg
175 180 185
aag cgg tct aac cat aga agg atg aag tca gat tct ttt ctc cag gaa 1769
Lys Arg Ser Asn His Arg Arg Met Lys Ser Asp Ser Phe Leu Gln Glu
190 195 200
atg cca aat gta act aat ata cct cat ggg gac ccc atg atc aac aat 1817
Met Pro Asn Val Thr Asn Ile Pro His Gly Asp Pro Met Ile Asn Asn
205 210 215
gac cag tgc att ctt cca atc agt tta gaa aaa gaa aaa cag aaa aac 1865
Asp Gln Cys Ile Leu Pro Ile Ser Leu Glu Lys Glu Lys Gln Lys Asn
220 225 230
agg aag aat ctg agc tgt acc aat gtg ctc cag agc aat tct acg aaa 1913
Arg Lys Asn Leu Ser Cys Thr Asn Val Leu Gln Ser Asn Ser Thr Lys
235 240 245 250
aaa tgt gga att gat aca atc gat tta aaa aga aat gaa act cca cca 1961
Lys Cys Gly Ile Asp Thr Ile Asp Leu Lys Arg Asn Glu Thr Pro Pro
255 260 265
gtt cct cct cca aga agc acc tct cga aat ttt ccc agc tcg gat tct 2009
Val Pro Pro Pro Arg Ser Thr Ser Arg Asn Phe Pro Ser Ser Asp Ser
270 275 280
gaa caa gcc tat gaa aga tgg aag gaa agg tta gac cac aac agc tgg 2057
Glu Gln Ala Tyr Glu Arg Trp Lys Glu Arg Leu Asp His Asn Ser Trp
285 290 295
gtg ccc cat gag ggt cga agt aaa agg aat tac aac cct cac ttc cct 2105
Val Pro His Glu Gly Arg Ser Lys Arg Asn Tyr Asn Pro His Phe Pro
300 305 310
ttg aga caa caa gag atg tct atg ttg tat cca aat gaa ggg aaa act 2153
Leu Arg Gln Gln Glu Met Ser Met Leu Tyr Pro Asn Glu Gly Lys Thr
315 320 325 330
tcg aaa gat ggt atc atc ttt tcc tct ttg gta cca gaa gtc aaa ata 2201
Ser Lys Asp Gly Ile Ile Phe Ser Ser Leu Val Pro Glu Val Lys Ile
335 340 345
gat agc aag cct cca agt aat gaa gat gtt gga ctt agc atg tgg tca 2249
Asp Ser Lys Pro Pro Ser Asn Glu Asp Val Gly Leu Ser Met Trp Ser
350 355 360
tgt gac att ggg ata ggt gca aaa agg agc ccc tct act tcg tgg ttt 2297
Cys Asp Ile Gly Ile Gly Ala Lys Arg Ser Pro Ser Thr Ser Trp Phe
365 370 375
cag aaa acc tgc tct acc ccc agt aat cca aaa tat gaa atg gtg atc 2345
Gln Lys Thr Cys Ser Thr Pro Ser Asn Pro Lys Tyr Glu Met Val Ile
380 385 390
cca gat cac cct gct aaa tct cat cct gat ctt cat gta agt aat gac 2393
Pro Asp His Pro Ala Lys Ser His Pro Asp Leu His Val Ser Asn Asp
395 400 405 410
tgt agc tcc tca gta gca gag agc agt agc cca ctt aga aat ttc agt 2441
Cys Ser Ser Ser Val Ala Glu Ser Ser Ser Pro Leu Arg Asn Phe Ser
415 420 425
tgt ggc ttt gaa agg act aca agg aat gag aag ctg gca gca aag act 2489
Cys Gly Phe Glu Arg Thr Thr Arg Asn Glu Lys Leu Ala Ala Lys Thr
430 435 440
gat gaa ttt aac aga act gta ttt aga aca gat aga aat tgt cag gca 2537
Asp Glu Phe Asn Arg Thr Val Phe Arg Thr Asp Arg Asn Cys Gln Ala
445 450 455
ata cag caa aat cac agc tgc tca aaa tca tcg gag gat ctc aag ccc 2585
Ile Gln Gln Asn His Ser Cys Ser Lys Ser Ser Glu Asp Leu Lys Pro
460 465 470
tgt gat acc tca tct act cac aca ggt agc ata tca caa agt aac gat 2633
Cys Asp Thr Ser Ser Thr His Thr Gly Ser Ile Ser Gln Ser Asn Asp
475 480 485 490
gtg tcc ggt att tgg aaa acc aat gcc cac atg cct gtg ccc atg gaa 2681
Val Ser Gly Ile Trp Lys Thr Asn Ala His Met Pro Val Pro Met Glu
495 500 505
aat gtg cct gat aat ccc acc aag aaa tcc aca aca ggc cta gta aga 2729
Asn Val Pro Asp Asn Pro Thr Lys Lys Ser Thr Thr Gly Leu Val Arg
510 515 520
caa atg cag gga cac cta agt cct cgc agt tat cga aat atg ctc cac 2777
Gln Met Gln Gly His Leu Ser Pro Arg Ser Tyr Arg Asn Met Leu His
525 530 535
gag cat gac tgg aga ccg agt aat ttg tct ggc cgt ccg agg tca gct 2825
Glu His Asp Trp Arg Pro Ser Asn Leu Ser Gly Arg Pro Arg Ser Ala
540 545 550
gat ccc agg tca aat tat ggt gtt gtg gaa aag ctg ctg aaa acc tat 2873
Asp Pro Arg Ser Asn Tyr Gly Val Val Glu Lys Leu Leu Lys Thr Tyr
555 560 565 570
gag aca gca aca gag tct gca ttg caa aat tct aag tgc ttc cag gat 2921
Glu Thr Ala Thr Glu Ser Ala Leu Gln Asn Ser Lys Cys Phe Gln Asp
575 580 585
aat tgg acc aaa tgt aat tct gat gtc agt ggt ggt gcc aca tta agt 2969
Asn Trp Thr Lys Cys Asn Ser Asp Val Ser Gly Gly Ala Thr Leu Ser
590 595 600
cag cat tta gaa atg ctc caa atg gaa caa cag ttt cag caa aag aca 3017
Gln His Leu Glu Met Leu Gln Met Glu Gln Gln Phe Gln Gln Lys Thr
605 610 615
gct gtg tgg ggg gga cag gaa gtg aag caa gga ata gat ccg aaa aag 3065
Ala Val Trp Gly Gly Gln Glu Val Lys Gln Gly Ile Asp Pro Lys Lys
620 625 630
ata aca gag gaa tcc atg tca gtg aac gcc tca cat gga aaa gga ttt 3113
Ile Thr Glu Glu Ser Met Ser Val Asn Ala Ser His Gly Lys Gly Phe
635 640 645 650
tcc cga cct gct aga cca gca aat cgt cgt ctc ccc tcc aga tgg gca 3161
Ser Arg Pro Ala Arg Pro Ala Asn Arg Arg Leu Pro Ser Arg Trp Ala
655 660 665
tcc aga tct cca tct gca ccc cct gcc ttg cgg aga act acc cac aac 3209
Ser Arg Ser Pro Ser Ala Pro Pro Ala Leu Arg Arg Thr Thr His Asn
670 675 680
tat acc att tct ctg cga tcc gaa gca ttg atg gtt taa gtctttggcc 3258
Tyr Thr Ile Ser Leu Arg Ser Glu Ala Leu Met Val
685 690
tggattgcta tattacagaa gttctagtcc cacttgtcaa acagagcatt ctgagtgttt 3318
acaggcggac ctgttctctt ccgacaagca atttgaatct taactttcca tcagtcttca 3378
gtgtttttaa tctaaggaat aattatcttc ctgcattttg atttcttaga tcagaatttt 3438
ttaatgccat cctcattagt tttccaatac aatataagtt gaaacaatgt acaatattgt 3498
atattctttg ttgcaagtgg cagaaagtaa ggttatgtgc atggccatgt gtttgtaggt 3558
gcatgtgttg aaataggaag tatcctagta tgtatttaga tatgaaaaac ttatgtgcta 3618
gtgttgactt tgaaattata acatgtatac ctatatattc tttgtgttta tttaaaagtt 3678
ttgaaaatat gcagtactgt ttatattttg tatacctttt aataggtatc cacttaaggc 3738
atttgcagta caaatattaa ttgaccactt ccttggcccc cagctacaat gaaaaagaag 3798
aattatgcac acatctaaca ttggtagatt tctaaagaca actcataaat aatttcttaa 3858
cccatataag gataaaataa taccattgat attcttgttt attcttttta aataaaaatg 3918
tcacaagttt aatagatcag ccttgtaaag caagcataaa atgttcataa atgttttata 3978
tattatttgg tagtctagta tggctttaac tgaatatttg atcctcagag acagtatcat 4038
gagactgcat tataaatgac atgattaaat gatgaattta ttttgtcagc ctcagcaaca 4098
aacatttcct aaatgggatg caaaaagaaa ctgaatgatg ttgaatttta gtttttcttt 4158
aagttgtggt aagcttttag tttagctgct ttaacatgga gtcatacata cttagaggta 4218
agtcatttat tatttttttc ctttttctaa tcttttcctt aaaattaata gataacaaac 4278
taagttactt ttttactaac aaggaagatc aggaataata tttctttgaa agctgaaatt 4338
atacttctca cagtttgcta ccgaaaaaag gcttaaacta aaccttgaca tccacagtag 4398
catcaggaat agaaatgtgt attttggcta cagtttgcat acagtgaaca cataaaatct 4458
atattgaaaa ctgacagaaa tatgaatgtc gaggggcttg gaattctaaa tggaagattt 4518
tagaaggaac tttgctctct actgtcacta tataaaacca attatgttat gttattagat 4578
attaactcta tttaagcttt tcttttacta agaaattctt atgccaaatg tattccaaga 4638
gccatctcct tatgatgtat ttgaaccatt tagagaaatt cacttcattg taccccatga 4698
cctgaggtaa agaaaataat tttcaaattg cagacttcct tgaaaggctc aagactgtag 4758
catggtgatg tctagattca tactttactg taaggacagt ttcggtagtt aagtggaatt 4818
aaaggtctag agtgatttgt attggatggt aactaaggtc tatacatcta ctcttttaat 4878
tcttatttcc ttcaggaaga tccttttcca caggaagcta tcaaagaaaa gtaaactaga 4938
caccaagtaa tatcactctc ataatatgct ttccagctag aggggagaaa acaccaggaa 4998
agaggaaccc tgggtcataa aatgacggac ctgttaggaa aatgctgttg tgtgacaatg 5058
gagagcctgc ccaaggactg tgcaacctat ctgttcctct ccaccagtgt atcccaagta 5118
gtctggtatg atctgtggtt ccttagaata ttgaggatct ctttaaaaaa tgaaatttct 5178
gatctcaccc catattacta aagcaaaatt tccaggggta gggactggga ctccagaacc 5238
attaataaaa caaaacaaaa caaagcaaaa tattgatgat caggcagatt tgaaaacagt 5298
gacattgctt gatctctgaa tggatggatg cccttgggtg gtcacttttc ttcctaggac 5358
ttgcctttgt tatctgtaaa ttagaatggc tatactttca gacttcacaa ttttaagcca 5418
cttttttcta ttaacagttg aatgaaccag tgggacacat tttaacgtct tcttatgttg 5478
actaaaatta tagttagagc tgagaaaaaa aaaatagcat ctagtccaac tccttgattg 5538
taaaactgaa aaactaaggt tatttgaatg ttctgttttc tctttttaaa tattttataa 5598
cttttaaatg gaaaaaccta ttaggtaaat ggaaataatc cttgaaaata gtttttgatg 5658
ttttgtgatt tttaactggt aaatttctac tttaggtggg cattttcttc cctagaatat 5718
gccctttatt atgctatcat tgctagattt aaagggactt gtaagcattt ctggaaatat 5778
ttgatttaaa aacatatatt aatagatgtt ttccctagca gacttttgga gcaaaaatat 5838
tattttagtt cagcagagga ttactgatat tatgggctga tctcagaaag gaataaggat 5898
gaggcagaga ggagtacttg agtttgtgtg tgtgtgtgtg tgtgtgtgtt tgtgtcagtg 5958
tcacataagt tctccatatt gccttatgtc ccaaagccaa atataaaaat ataaatgatg 6018
ctttgtataa ttcattttat caaaaattac ccataacttt catttgtttt tatatcgaca 6078
atgaagatga tcatatttca ttttgcagat gtggccataa aatattattt acttctatat 6138
aggtgatttt accaggttta gttatcctga gaaaacatct ggacttaaga gtttctgctt 6198
ccctacaaag atctttaaag ttatttttag gcacatttgt gacaaacaac tacttgatat 6258
tgaaatctcc ttcagccatt agaagctatc aaataaagta ggtgtaaaaa caactgtctg 6318
tggcatttgt atacatcgag aacatttttc tttccctcat tttctgcagt gaactccagt 6378
aaagctaagt gtcttatgaa atctaaactc atatatgtac acagttcact ctagcttctt 6438
ccaaaatatc tctaggtagt acaactgaag ccaaacctgc ctgacttcct gctcctggcc 6498
acccaaaact ccatatggct tctcgtacac tgacatcctc tctctaccca tttaactgct 6558
aattgagtct gataaaagtc ttctttgaaa aaagttttta cttctaagat ttgcatttac 6618
atcataaaat taaaccattt tcaggaaaat cagatttttt tattacagta ctatttgctt 6678
taaattcggc atgtttttct taagtagcaa gtacatgtat cggaacttag aactggtggg 6738
cgcggtggct cttgcctgta atcccagcac tttgggaggc caaggtgggg ggatcacgag 6798
gtcaggagat ggagaccatc ctggtttcat cacggtgaaa ccccctctct gctaaaaata 6858
caaaaaatta gccaggcatt gtggtggtca cctgtagtcc cagctgctcg ggaggctgag 6918
gcaggagaat ggcatgaacc cgggaggcag agcttgcagt gagcagagat cgcgccactg 6978
cactccagcc tgggtgacag agtgagactc tgtctc 7014


8
694
PRT
Homo sapiens

8
Met Asp Leu His Lys Gln Trp Glu Asn Thr Glu Thr Asn Trp His Lys
1 5 10 15
Glu Lys Met Glu Leu Leu Asp Gln Phe Asp Asn Glu Arg Lys Glu Trp
20 25 30
Glu Ser Gln Trp Lys Ile Met Gln Lys Lys Ile Glu Glu Leu Cys Arg
35 40 45
Glu Val Lys Leu Trp Arg Lys Ile Asn Ile Asn Glu Ser Ala Lys Ile
50 55 60
Ile Asp Leu Tyr His Glu Lys Thr Ile Pro Glu Lys Val Ile Glu Ser
65 70 75 80
Ser Pro Asn Tyr Pro Asp Leu Gly Gln Ser Glu Phe Ile Arg Thr Asn
85 90 95
His Lys Asp Gly Leu Arg Lys Glu Asn Lys Arg Glu Gln Ser Leu Val
100 105 110
Ser Gly Gly Asn Gln Met Cys Lys Glu Gln Lys Ala Thr Lys Lys Ser
115 120 125
Lys Val Gly Phe Leu Asp Pro Leu Ala Thr Asp Asn Gln Lys Glu Cys
130 135 140
Glu Ala Trp Pro Asp Leu Arg Thr Ser Glu Glu Asp Ser Lys Ser Cys
145 150 155 160
Ser Gly Ala Leu Ser Thr Ala Leu Glu Glu Leu Ala Lys Val Ser Glu
165 170 175
Glu Leu Cys Ser Phe Gln Glu Glu Ile Arg Lys Arg Ser Asn His Arg
180 185 190
Arg Met Lys Ser Asp Ser Phe Leu Gln Glu Met Pro Asn Val Thr Asn
195 200 205
Ile Pro His Gly Asp Pro Met Ile Asn Asn Asp Gln Cys Ile Leu Pro
210 215 220
Ile Ser Leu Glu Lys Glu Lys Gln Lys Asn Arg Lys Asn Leu Ser Cys
225 230 235 240
Thr Asn Val Leu Gln Ser Asn Ser Thr Lys Lys Cys Gly Ile Asp Thr
245 250 255
Ile Asp Leu Lys Arg Asn Glu Thr Pro Pro Val Pro Pro Pro Arg Ser
260 265 270
Thr Ser Arg Asn Phe Pro Ser Ser Asp Ser Glu Gln Ala Tyr Glu Arg
275 280 285
Trp Lys Glu Arg Leu Asp His Asn Ser Trp Val Pro His Glu Gly Arg
290 295 300
Ser Lys Arg Asn Tyr Asn Pro His Phe Pro Leu Arg Gln Gln Glu Met
305 310 315 320
Ser Met Leu Tyr Pro Asn Glu Gly Lys Thr Ser Lys Asp Gly Ile Ile
325 330 335
Phe Ser Ser Leu Val Pro Glu Val Lys Ile Asp Ser Lys Pro Pro Ser
340 345 350
Asn Glu Asp Val Gly Leu Ser Met Trp Ser Cys Asp Ile Gly Ile Gly
355 360 365
Ala Lys Arg Ser Pro Ser Thr Ser Trp Phe Gln Lys Thr Cys Ser Thr
370 375 380
Pro Ser Asn Pro Lys Tyr Glu Met Val Ile Pro Asp His Pro Ala Lys
385 390 395 400
Ser His Pro Asp Leu His Val Ser Asn Asp Cys Ser Ser Ser Val Ala
405 410 415
Glu Ser Ser Ser Pro Leu Arg Asn Phe Ser Cys Gly Phe Glu Arg Thr
420 425 430
Thr Arg Asn Glu Lys Leu Ala Ala Lys Thr Asp Glu Phe Asn Arg Thr
435 440 445
Val Phe Arg Thr Asp Arg Asn Cys Gln Ala Ile Gln Gln Asn His Ser
450 455 460
Cys Ser Lys Ser Ser Glu Asp Leu Lys Pro Cys Asp Thr Ser Ser Thr
465 470 475 480
His Thr Gly Ser Ile Ser Gln Ser Asn Asp Val Ser Gly Ile Trp Lys
485 490 495
Thr Asn Ala His Met Pro Val Pro Met Glu Asn Val Pro Asp Asn Pro
500 505 510
Thr Lys Lys Ser Thr Thr Gly Leu Val Arg Gln Met Gln Gly His Leu
515 520 525
Ser Pro Arg Ser Tyr Arg Asn Met Leu His Glu His Asp Trp Arg Pro
530 535 540
Ser Asn Leu Ser Gly Arg Pro Arg Ser Ala Asp Pro Arg Ser Asn Tyr
545 550 555 560
Gly Val Val Glu Lys Leu Leu Lys Thr Tyr Glu Thr Ala Thr Glu Ser
565 570 575
Ala Leu Gln Asn Ser Lys Cys Phe Gln Asp Asn Trp Thr Lys Cys Asn
580 585 590
Ser Asp Val Ser Gly Gly Ala Thr Leu Ser Gln His Leu Glu Met Leu
595 600 605
Gln Met Glu Gln Gln Phe Gln Gln Lys Thr Ala Val Trp Gly Gly Gln
610 615 620
Glu Val Lys Gln Gly Ile Asp Pro Lys Lys Ile Thr Glu Glu Ser Met
625 630 635 640
Ser Val Asn Ala Ser His Gly Lys Gly Phe Ser Arg Pro Ala Arg Pro
645 650 655
Ala Asn Arg Arg Leu Pro Ser Arg Trp Ala Ser Arg Ser Pro Ser Ala
660 665 670
Pro Pro Ala Leu Arg Arg Thr Thr His Asn Tyr Thr Ile Ser Leu Arg
675 680 685
Ser Glu Ala Leu Met Val
690


9
4891
DNA
Homo sapiens

CDS
(202)..(1041)


9
gtgtgacgaa acctgcttcg gcggcccgag gtgggggttt tgagtcggtt agtggaggca 60
gtgggagcag gatgggcgga gcttctgttc caaaaatttc ccctaagtgc ggttgacagt 120
gtgcaggcag gcgggggtgc gcggggcggt cagcgatctg cagcttcgcg gggacagaga 180
tgtaacccaa ctcgttcacg g atg ttc cgc gcg ccg tgt cac cgg ctg cgg 231
Met Phe Arg Ala Pro Cys His Arg Leu Arg
1 5 10
gcc agg ggt act cgg aag gcg cgg gca gga gcc tgg cga gga tgc acc 279
Ala Arg Gly Thr Arg Lys Ala Arg Ala Gly Ala Trp Arg Gly Cys Thr
15 20 25
ttc ccc tgc ctt gga aag gga atg gag agg ccg gcg gcc cgg gag ccg 327
Phe Pro Cys Leu Gly Lys Gly Met Glu Arg Pro Ala Ala Arg Glu Pro
30 35 40
cat ggg ccc gac gcg ctg cgg cgc ttc cag gga ctg ctg ctg gac cgc 375
His Gly Pro Asp Ala Leu Arg Arg Phe Gln Gly Leu Leu Leu Asp Arg
45 50 55
cga ggc cgg ctg cac cgc cag gtg ctg cgc ctg cgc gag gtg gcc cgg 423
Arg Gly Arg Leu His Arg Gln Val Leu Arg Leu Arg Glu Val Ala Arg
60 65 70
cgc ctg gag cgc ctg cgc agg cgc tcc ctc gta gcc aac gtg gcc ggc 471
Arg Leu Glu Arg Leu Arg Arg Arg Ser Leu Val Ala Asn Val Ala Gly
75 80 85 90
agc tcg ctg agc gca acg ggc gcc ctc gcc gcc atc gtg ggg ctc tcg 519
Ser Ser Leu Ser Ala Thr Gly Ala Leu Ala Ala Ile Val Gly Leu Ser
95 100 105
ctc agc ccg gtc acc ctg ggg acc tcg ctg ctg gtg tcg gcc gtg ggg 567
Leu Ser Pro Val Thr Leu Gly Thr Ser Leu Leu Val Ser Ala Val Gly
110 115 120
ctg ggg gtg gcc aca gcc gga ggg gcc gtc acc atc acg tcc gat ctc 615
Leu Gly Val Ala Thr Ala Gly Gly Ala Val Thr Ile Thr Ser Asp Leu
125 130 135
tcg ctg atc ttc tgc aac tcc cgg gag ctg cgg agg gtg cag gag atc 663
Ser Leu Ile Phe Cys Asn Ser Arg Glu Leu Arg Arg Val Gln Glu Ile
140 145 150
gcg gcc acc tgc cag gac cag atg cga gag atc ctg agc tgc ctc gag 711
Ala Ala Thr Cys Gln Asp Gln Met Arg Glu Ile Leu Ser Cys Leu Glu
155 160 165 170
ttt ttc tgc cgc tgg cag ggc tgc ggg gac cgc cag ctg ctg cag tgc 759
Phe Phe Cys Arg Trp Gln Gly Cys Gly Asp Arg Gln Leu Leu Gln Cys
175 180 185
ggg agg aac gcc tcc atc gcc ctg tac aat tct gtc tac ttc atc gtc 807
Gly Arg Asn Ala Ser Ile Ala Leu Tyr Asn Ser Val Tyr Phe Ile Val
190 195 200
ttc ttt ggc tca cgt ggc ttc ctc atc ccc agg cgg gcg gag ggg gac 855
Phe Phe Gly Ser Arg Gly Phe Leu Ile Pro Arg Arg Ala Glu Gly Asp
205 210 215
acc aag gtt agc cag gcc gtg ctg aag gcc aag att cag aaa ctg gcc 903
Thr Lys Val Ser Gln Ala Val Leu Lys Ala Lys Ile Gln Lys Leu Ala
220 225 230
gag agc ctg gag tcc tgc acc ggg gct ctg gac gaa ctc agc gag cag 951
Glu Ser Leu Glu Ser Cys Thr Gly Ala Leu Asp Glu Leu Ser Glu Gln
235 240 245 250
ctg gag tct cgg gtt cag ctc tgc acc aag tcc agt cgt ggc cac gac 999
Leu Glu Ser Arg Val Gln Leu Cys Thr Lys Ser Ser Arg Gly His Asp
255 260 265
ctc aag atc tct gct gac cag cgt gca ggg ctg ttt ttc tga 1041
Leu Lys Ile Ser Ala Asp Gln Arg Ala Gly Leu Phe Phe
270 275
gaacatcctt tccccctaat gaccgaggcc agcaaatcat cctcatggga tgctccagaa 1101
tttgtagctc ccttaggaaa acaccaagct gggttaggag ccgaaggcaa aggatgagaa 1161
aaactgtttt tgaagtgggc aggtccccaa agcccttctt ttcccatcac tgtgacatct 1221
gcctgggctt gagtgctacg gacttttcag tcttcctagt ggaaaaatgt gacccaaaaa 1281
ctccttttcc tttatcaaaa actttctgtc taaacacagc tgggcaggca ctcctgtttt 1341
aaagttattt cggggtccct gaccctgccc tggtggcttg gcctgagact ggagagagtg 1401
ccatcctctg ggtcctctcc aagtcctact agtctttgaa gtcctcaaaa tgtgcgtgag 1461
gaaggcattt gcctctattc cagaatttct gatacaaaga actccagaat ccagagcaaa 1521
tcagcccttc tctgaacgtt gtaggatggt tcagaaccca gagaggaccc tggtgctgat 1581
atctcctcct cttccctttc ccctcagctt acttactccc agatgcggcc tgggtatgaa 1641
gtaggccttt cctgagtggc tcccaatcca gtcctccaag tactcagagg ggaagcccgt 1701
gaagccgtca tctaagtcct gctccctcac atgaagctga gggccagata gatggagcga 1761
ctgccaactt catttcccga catcattgtg ttcagaagag agtgatgggt tttgagttag 1821
acagtcctgg gcttgagaca ggctttgtca ctactgtgtg agtgtagcca cctaatctct 1881
ctgagactgt gtaaaacaaa gatgataaaa tctcaccctg ttgtgagata ttaaatgagc 1941
caaagtgcct agcatgatgg tgctggctca tatagtgtag tccctggaat ggcaaattaa 2001
catcacccag gaacttgtta gaaaggcaaa ttcttggaca caaccctcct gatttatgga 2061
atcagaaact ctggctgtgg ggcccagcaa cctgagttta aacaatttct ctgggtggtt 2121
ctgcggcaca ctaaggtttg aaaatcacta caacaaatgc taacttctaa tccccttgat 2181
gagctttcac gaagtctcac ggcttctcta gggactccat ggtcttcaga gtcgttcaca 2241
gatgaccaag gacagactgt gtcccagaag ccaaaatgag agagagagag agagcacgcg 2301
tacgtgcacc ctggggcagt gtctcaccgt atgaataagg gatgtaacac taaaagccca 2361
ttagggggca gtgtttcccg cctgttgtag aaactggtac agaaaggatc ctatatgaag 2421
ttcctgaaac tgacctttgt ctattattac cttctctgaa aagtgccagt ccatgtattt 2481
tttatttatt ttaagtttgt aatttaattt ttaattattg tttagtgttt gcatttaatt 2541
ttatttaatc accacattta gaaaataata agagcaagtt tctaaatggg agactgctga 2601
ggctctttgc aagagatgag attaagtttg agtttctaag gcagggcatg agctggaaat 2661
agcattgctt tccttgattg tctctctcct tcagggagat tctttttctc tagtgtttta 2721
agtgatcctt tgaagtaagt gtggagagtc ttgaatggca agaccaggag ctgagtttaa 2781
gcttgtaatg gaagcttgca ttgtgggata tataactgag gaagcatatt tatcctgaag 2841
gtattttgcc agaaggtatc acttgacctg gaaaaggaat ctatttagtt caggaaagat 2901
aaaaagttta gaggtatgtg aaggaagcac ttagaacttg caagcctgat gtcctatcaa 2961
gttatgtctt ctgggtgaca gacaaaatag cttgtcttat ggtggtgatg tgttgcattt 3021
tcactttggg gtctgtaaga aactgtcagt gaaaatatgt acaattcctt caatttccat 3081
tcttaacaac tgtaatgttg aaaaataagt tgaaaagtct ttgggaccat acatgcaaaa 3141
acggtgcctc tgttacttaa ttatttaata ttctataaat gtacccaatc tgtccgcacc 3201
cttcccagtg atggggcagt atgtctgagg aagtataatt tcagtactgg ggtcggggag 3261
aggaggtgat gtttctacat ttttattttt tctataaatt gcaattggtc tgtatgctgg 3321
tttattttga aatttatatt ggtttctttt caagctggtg tcatctccta gactgtttca 3381
cccagatgct agcatttttt ttttttttga gacagagtct cactctgtca cctaggctgg 3441
agttgcagtg gtttgatctc ggctcactgc aacctccgac tcctgggttc aagcaattct 3501
tctgcctcag cctcctgagt agctgggatt acagatgtgc accagcacac ccggctaatt 3561
ttttgtattt ttagtagaga cagggtttcg ccatgttggc caggctggtc ttgaactcct 3621
ggccttatgt gatccgccca ccttggcttc ccaaagtgct gggattacag gcatgagcca 3681
cctcgcctgg ccagatgcta gcattttaga tcaaacaatt cattttagat gaattgtttt 3741
gtttcacaat cattttaaat cattttagaa tgtacttcac attattagtt gtgttatggc 3801
ataaaggtac aaccattccc taactccatc ttttattaat gcttaagttt aaattatatt 3861
cttccaatgc ctaagctatt ccctagaatt aaactgggca cttttggaag cagcaacagt 3921
aacagcagca gcaaactttt cctctcatat tttgggtgta tcaaaagttc tagacttttg 3981
aagttatgat ttcagtggcc cactttattt ctaaggaaga gtgtctactt tggaacgata 4041
ctttgcacat agtaggaact caagaaatac atttgaataa ttataattaa ctgtttagct 4101
atcttaatga gaatttgttg acaacaaaag atcatccatc gccttatgtg tgagtaagat 4161
tggagcctct atcaagattt agtcaagttc agttagattg attctagaaa caaatattta 4221
tttctttctt ttacggggat gtgaataagg cttttcctta aggccttcat tctttaaaca 4281
aacaggttga aatggtatgt tgtaaaagag aagacgggag agaggtattt agatgataag 4341
tgtacttcac aaaaatgcca aagtttgaaa aataggtatg tttgttctaa atgtttaagt 4401
gcttctctgt taggttctgg ggcttgcaat catttgaatt gttctgtttc acaataaagg 4461
agattcactg ggttctgcat tttcaggatt caatagaact gctccattaa aaaaataatc 4521
cttagcaagc attcgaatcc taactgcttt gatgcacttg ccctcgggca cctgtcattt 4581
ccaatatggt aggtgtcaaa gtcaaaagta tttactggga gaaaaaagag aggagtggtt 4641
gtagaagtct ccctaaatca gacatgtcaa gcaatcagcc aacgtggtgt atttctcatt 4701
caatatttta gtgtgaattg agacactgag ataaagacat cgtgcagaga taaatgggga 4761
tacagttaaa tgtagcaact cttgagttca ttttttccca ctgtagcaaa attaatgctt 4821
tctctttatt gaaataaatt gctcattcct ccaaaaaaaa aaaaaaaaaa aaaaaaaaaa 4881
aaaaaaaagg 4891


10
279
PRT
Homo sapiens

10
Met Phe Arg Ala Pro Cys His Arg Leu Arg Ala Arg Gly Thr Arg Lys
1 5 10 15
Ala Arg Ala Gly Ala Trp Arg Gly Cys Thr Phe Pro Cys Leu Gly Lys
20 25 30
Gly Met Glu Arg Pro Ala Ala Arg Glu Pro His Gly Pro Asp Ala Leu
35 40 45
Arg Arg Phe Gln Gly Leu Leu Leu Asp Arg Arg Gly Arg Leu His Arg
50 55 60
Gln Val Leu Arg Leu Arg Glu Val Ala Arg Arg Leu Glu Arg Leu Arg
65 70 75 80
Arg Arg Ser Leu Val Ala Asn Val Ala Gly Ser Ser Leu Ser Ala Thr
85 90 95
Gly Ala Leu Ala Ala Ile Val Gly Leu Ser Leu Ser Pro Val Thr Leu
100 105 110
Gly Thr Ser Leu Leu Val Ser Ala Val Gly Leu Gly Val Ala Thr Ala
115 120 125
Gly Gly Ala Val Thr Ile Thr Ser Asp Leu Ser Leu Ile Phe Cys Asn
130 135 140
Ser Arg Glu Leu Arg Arg Val Gln Glu Ile Ala Ala Thr Cys Gln Asp
145 150 155 160
Gln Met Arg Glu Ile Leu Ser Cys Leu Glu Phe Phe Cys Arg Trp Gln
165 170 175
Gly Cys Gly Asp Arg Gln Leu Leu Gln Cys Gly Arg Asn Ala Ser Ile
180 185 190
Ala Leu Tyr Asn Ser Val Tyr Phe Ile Val Phe Phe Gly Ser Arg Gly
195 200 205
Phe Leu Ile Pro Arg Arg Ala Glu Gly Asp Thr Lys Val Ser Gln Ala
210 215 220
Val Leu Lys Ala Lys Ile Gln Lys Leu Ala Glu Ser Leu Glu Ser Cys
225 230 235 240
Thr Gly Ala Leu Asp Glu Leu Ser Glu Gln Leu Glu Ser Arg Val Gln
245 250 255
Leu Cys Thr Lys Ser Ser Arg Gly His Asp Leu Lys Ile Ser Ala Asp
260 265 270
Gln Arg Ala Gly Leu Phe Phe
275


11
8733
DNA
Homo sapiens

CDS
(473)..(8566)


11
agagacggaa cgagagagag acacacacag ggctccttcc ccccgccctc ccccccctcc 60
ctccgtcggt accgactcac ccgacaccac caagccgcag ggagggacgc ccccgccgac 120
aggagaattg gttcccgggt ccgcggcgat gcccccccgg tagctcgggc ccgtggtcgg 180
gtgtttgtga gtgtttctat gtgggagaag gaggaggagg aggaagaaga agcaacgatt 240
tgtcttctcg gctggtctcc ccccggctct acatgttccc cgcactgagg agacggaaga 300
ggagccgtag ccaccccccc tcccggcccg gattatagtc tctcgccaca gcggcctcgg 360
cctccccttg gattcagacg ccgattcgcc cagtgtttgg gaaatgggaa gtaatgacag 420
ctggcacctg aactaagtac ttttataggc aacaccattc cagaaattca gg atg aat 478
Met Asn
1
ggg gat atg ccc cat gtc ccc att act act ctt gcg ggg att gct agt 526
Gly Asp Met Pro His Val Pro Ile Thr Thr Leu Ala Gly Ile Ala Ser
5 10 15
ctc aca gac ctc ctg aac cag ctg cct ctt cca tct cct tta cct gct 574
Leu Thr Asp Leu Leu Asn Gln Leu Pro Leu Pro Ser Pro Leu Pro Ala
20 25 30
aca act aca aag agc ctt ctc ttt aat gca cga ata gca gaa gag gtg 622
Thr Thr Thr Lys Ser Leu Leu Phe Asn Ala Arg Ile Ala Glu Glu Val
35 40 45 50
aac tgc ctt ttg gct tgt agg gat gac aat ttg gtt tca cag ctt gtc 670
Asn Cys Leu Leu Ala Cys Arg Asp Asp Asn Leu Val Ser Gln Leu Val
55 60 65
cat agc ctc aac cag gta tca aca gat cac ata gag ttg aaa gat aac 718
His Ser Leu Asn Gln Val Ser Thr Asp His Ile Glu Leu Lys Asp Asn
70 75 80
ctt ggc agt gat gac cca gaa ggt gac ata cca gtc ttg ttg cag gcc 766
Leu Gly Ser Asp Asp Pro Glu Gly Asp Ile Pro Val Leu Leu Gln Ala
85 90 95
gtc ctg gca agg agt cct aat gtt ttc agg gag aaa agc atg cag aac 814
Val Leu Ala Arg Ser Pro Asn Val Phe Arg Glu Lys Ser Met Gln Asn
100 105 110
aga tat gta caa agt gga atg atg atg tct cag tat aaa ctt tct cag 862
Arg Tyr Val Gln Ser Gly Met Met Met Ser Gln Tyr Lys Leu Ser Gln
115 120 125 130
aat tcc atg cac agt agt cct gca tct tcc aat tat caa caa acc act 910
Asn Ser Met His Ser Ser Pro Ala Ser Ser Asn Tyr Gln Gln Thr Thr
135 140 145
atc tca cat agc ccc tcc agc cgg ttt gtg cca cca cag aca agc tct 958
Ile Ser His Ser Pro Ser Ser Arg Phe Val Pro Pro Gln Thr Ser Ser
150 155 160
ggg aac aga ttt atg cca cag caa aat agc cca gtg cct agt cca tac 1006
Gly Asn Arg Phe Met Pro Gln Gln Asn Ser Pro Val Pro Ser Pro Tyr
165 170 175
gcc cca caa agc cct gca gga tac atg cca tat tcc cat cct tca agt 1054
Ala Pro Gln Ser Pro Ala Gly Tyr Met Pro Tyr Ser His Pro Ser Ser
180 185 190
tac aca aca cat cca cag atg caa caa gca tcg gta tca agt ccc att 1102
Tyr Thr Thr His Pro Gln Met Gln Gln Ala Ser Val Ser Ser Pro Ile
195 200 205 210
gtt gca ggt ggt ttg aga aac ata cat gat aat aaa gtt tct ggt ccg 1150
Val Ala Gly Gly Leu Arg Asn Ile His Asp Asn Lys Val Ser Gly Pro
215 220 225
ttg tct ggc aat tca gct aat cat cat gct gat aat cct aga cat ggt 1198
Leu Ser Gly Asn Ser Ala Asn His His Ala Asp Asn Pro Arg His Gly
230 235 240
tca agt gag gac tac cta cac atg gtg cac agg cta agt agt gac gat 1246
Ser Ser Glu Asp Tyr Leu His Met Val His Arg Leu Ser Ser Asp Asp
245 250 255
gga gat tct tca aca atg agg aat gct gca tct ttt ccc ttg aga tct 1294
Gly Asp Ser Ser Thr Met Arg Asn Ala Ala Ser Phe Pro Leu Arg Ser
260 265 270
cca cag cca gta tgc tcc cct gct gga agt gaa gga act cct aaa ggc 1342
Pro Gln Pro Val Cys Ser Pro Ala Gly Ser Glu Gly Thr Pro Lys Gly
275 280 285 290
tca aga cca cct tta atc cta caa tct cag tct cta cct tgt tca tca 1390
Ser Arg Pro Pro Leu Ile Leu Gln Ser Gln Ser Leu Pro Cys Ser Ser
295 300 305
cct cga gat gtt cca cca gat atc ttg cta gat tct cca gaa aga aaa 1438
Pro Arg Asp Val Pro Pro Asp Ile Leu Leu Asp Ser Pro Glu Arg Lys
310 315 320
caa aag aag cag aag aaa atg aaa tta ggc aag gat gaa aaa gag cag 1486
Gln Lys Lys Gln Lys Lys Met Lys Leu Gly Lys Asp Glu Lys Glu Gln
325 330 335
agt gag aaa gcg gca atg tat gat ata att agt tct cca tcc aag gac 1534
Ser Glu Lys Ala Ala Met Tyr Asp Ile Ile Ser Ser Pro Ser Lys Asp
340 345 350
tct act aaa ctt aca tta aga ctt tct cgt gta agg tct tca gac atg 1582
Ser Thr Lys Leu Thr Leu Arg Leu Ser Arg Val Arg Ser Ser Asp Met
355 360 365 370
gac cag caa gag gat atg att tct ggt gtg gaa aat agc aat gtt tca 1630
Asp Gln Gln Glu Asp Met Ile Ser Gly Val Glu Asn Ser Asn Val Ser
375 380 385
gaa aat gat att cct ttt aat gtg cag tac cca gga cag act tca aaa 1678
Glu Asn Asp Ile Pro Phe Asn Val Gln Tyr Pro Gly Gln Thr Ser Lys
390 395 400
aca ccc att act cca caa gat ata aac cgc cca cta aat gct gct caa 1726
Thr Pro Ile Thr Pro Gln Asp Ile Asn Arg Pro Leu Asn Ala Ala Gln
405 410 415
tgt ttg tcg cag caa gaa caa aca gca ttc ctt cca gca aat caa gtg 1774
Cys Leu Ser Gln Gln Glu Gln Thr Ala Phe Leu Pro Ala Asn Gln Val
420 425 430
cct gtt tta caa cag aac act tca gtt gct gca aaa caa ccc cag act 1822
Pro Val Leu Gln Gln Asn Thr Ser Val Ala Ala Lys Gln Pro Gln Thr
435 440 445 450
tct gtg gta cag aat caa caa cag ata tca caa cag gga cct ata tat 1870
Ser Val Val Gln Asn Gln Gln Gln Ile Ser Gln Gln Gly Pro Ile Tyr
455 460 465
gat gaa gtg gaa ttg gat gca ttg gct gaa att gag cga ata gag aga 1918
Asp Glu Val Glu Leu Asp Ala Leu Ala Glu Ile Glu Arg Ile Glu Arg
470 475 480
gaa tca gct att gaa agg gag cgc ttc tca aaa gaa gtt caa gat aaa 1966
Glu Ser Ala Ile Glu Arg Glu Arg Phe Ser Lys Glu Val Gln Asp Lys
485 490 495
gat aag cct ttg aaa aaa aga aaa caa gat tct tac cca cag gag gct 2014
Asp Lys Pro Leu Lys Lys Arg Lys Gln Asp Ser Tyr Pro Gln Glu Ala
500 505 510
ggg ggt gct aca gga ggt aat aga cca gct tct cag gag acg ggt tct 2062
Gly Gly Ala Thr Gly Gly Asn Arg Pro Ala Ser Gln Glu Thr Gly Ser
515 520 525 530
acg gga aat ggg tca agg cca gca tta atg gtt agc att gat ctt cat 2110
Thr Gly Asn Gly Ser Arg Pro Ala Leu Met Val Ser Ile Asp Leu His
535 540 545
cag gca gga aga gtg gac tct cag gct tct ata act cag gat tca gac 2158
Gln Ala Gly Arg Val Asp Ser Gln Ala Ser Ile Thr Gln Asp Ser Asp
550 555 560
tcc ata aaa aag cct gaa gaa atc aaa caa tgt aat gat gca cct gtt 2206
Ser Ile Lys Lys Pro Glu Glu Ile Lys Gln Cys Asn Asp Ala Pro Val
565 570 575
tct gtt ctt cag gaa gat att gtt gga agt ctt aaa tct aca cca gaa 2254
Ser Val Leu Gln Glu Asp Ile Val Gly Ser Leu Lys Ser Thr Pro Glu
580 585 590
aac cat cct gag aca cct aaa aaa aag tct gat cct gag ctt tca aag 2302
Asn His Pro Glu Thr Pro Lys Lys Lys Ser Asp Pro Glu Leu Ser Lys
595 600 605 610
agt gaa atg aaa caa agt gaa agt aga tta gca gaa tct aaa cca aat 2350
Ser Glu Met Lys Gln Ser Glu Ser Arg Leu Ala Glu Ser Lys Pro Asn
615 620 625
gaa aac cga ttg gtg gag aca aaa tca agt gaa aat aag tta gaa act 2398
Glu Asn Arg Leu Val Glu Thr Lys Ser Ser Glu Asn Lys Leu Glu Thr
630 635 640
aaa gtt gag acc caa aca gaa gaa ctt aaa cag aat gag agc aga aca 2446
Lys Val Glu Thr Gln Thr Glu Glu Leu Lys Gln Asn Glu Ser Arg Thr
645 650 655
act gaa tgc aaa caa aac gag agc acc ata gtt gag cct aaa caa aat 2494
Thr Glu Cys Lys Gln Asn Glu Ser Thr Ile Val Glu Pro Lys Gln Asn
660 665 670
gaa aat aga ctg tct gac aca aaa cca aat gac aac aaa caa aat aat 2542
Glu Asn Arg Leu Ser Asp Thr Lys Pro Asn Asp Asn Lys Gln Asn Asn
675 680 685 690
ggc aga tca gaa aca aca aaa tca agg cct gaa acc cca aag caa aag 2590
Gly Arg Ser Glu Thr Thr Lys Ser Arg Pro Glu Thr Pro Lys Gln Lys
695 700 705
ggt gaa agc cgg cct gag act cca aaa caa aag agt gat ggg cat cct 2638
Gly Glu Ser Arg Pro Glu Thr Pro Lys Gln Lys Ser Asp Gly His Pro
710 715 720
gaa acc cca aaa cag aag ggt gat gga agg cct gaa act cca aag caa 2686
Glu Thr Pro Lys Gln Lys Gly Asp Gly Arg Pro Glu Thr Pro Lys Gln
725 730 735
aaa ggt gag agc cgc cct gaa act cca aag caa aaa aat gaa ggg cga 2734
Lys Gly Glu Ser Arg Pro Glu Thr Pro Lys Gln Lys Asn Glu Gly Arg
740 745 750
cct gaa aca cca aaa cac agg cat gac aat agg agg gat tct gga aag 2782
Pro Glu Thr Pro Lys His Arg His Asp Asn Arg Arg Asp Ser Gly Lys
755 760 765 770
cca tct aca gag aaa aaa cct gaa gtg tct aaa cat aaa caa gat act 2830
Pro Ser Thr Glu Lys Lys Pro Glu Val Ser Lys His Lys Gln Asp Thr
775 780 785
aaa tct gac tca cct cgg tta aaa tca gaa cga gct gaa gcc tta aag 2878
Lys Ser Asp Ser Pro Arg Leu Lys Ser Glu Arg Ala Glu Ala Leu Lys
790 795 800
cag aga cct gat ggg cga tct gtt tct gag tca cta aga cgt gac cat 2926
Gln Arg Pro Asp Gly Arg Ser Val Ser Glu Ser Leu Arg Arg Asp His
805 810 815
gat aat aaa caa aaa tca gat gac agg ggt gaa tca gag cga cat cga 2974
Asp Asn Lys Gln Lys Ser Asp Asp Arg Gly Glu Ser Glu Arg His Arg
820 825 830
ggg gat cag tct agg gtt cga aga cca gaa aca ttg aga tcc tct agt 3022
Gly Asp Gln Ser Arg Val Arg Arg Pro Glu Thr Leu Arg Ser Ser Ser
835 840 845 850
aga aat gaa cat ggc att aaa tct gat agt tca aaa act gat aaa cta 3070
Arg Asn Glu His Gly Ile Lys Ser Asp Ser Ser Lys Thr Asp Lys Leu
855 860 865
gaa cga aaa cac agg cat gaa tca ggg gac tca agg gaa aga cca tct 3118
Glu Arg Lys His Arg His Glu Ser Gly Asp Ser Arg Glu Arg Pro Ser
870 875 880
tct ggg gaa caa aaa tca aga cct gac agt cct cgt gtt aaa caa gga 3166
Ser Gly Glu Gln Lys Ser Arg Pro Asp Ser Pro Arg Val Lys Gln Gly
885 890 895
gat tct aat aaa tca aga tct gat aaa ctt ggt ttt aaa tca cca act 3214
Asp Ser Asn Lys Ser Arg Ser Asp Lys Leu Gly Phe Lys Ser Pro Thr
900 905 910
agt aaa gat gac aaa agg aca gag ggt aac aag agt aaa gta gac act 3262
Ser Lys Asp Asp Lys Arg Thr Glu Gly Asn Lys Ser Lys Val Asp Thr
915 920 925 930
aat aaa gca cac cct gac aat aag gca gaa ttt cca agt tat ttg ttg 3310
Asn Lys Ala His Pro Asp Asn Lys Ala Glu Phe Pro Ser Tyr Leu Leu
935 940 945
ggg ggc agg tct ggt gcg ttg aaa aat ttt gtc att ccg aaa atc aag 3358
Gly Gly Arg Ser Gly Ala Leu Lys Asn Phe Val Ile Pro Lys Ile Lys
950 955 960
agg gat aaa gat ggc aat gtt act cag gag aca aag aaa atg gaa atg 3406
Arg Asp Lys Asp Gly Asn Val Thr Gln Glu Thr Lys Lys Met Glu Met
965 970 975
aaa gga gag ccg aaa gac aaa gta gaa aaa ata gga tta gtt gaa gat 3454
Lys Gly Glu Pro Lys Asp Lys Val Glu Lys Ile Gly Leu Val Glu Asp
980 985 990
cta aat aaa gga gct aag cct gta gtt gtg cta caa aaa ctg tct 3499
Leu Asn Lys Gly Ala Lys Pro Val Val Val Leu Gln Lys Leu Ser
995 1000 1005
ttg gat gat gtt cag aaa ctt att aaa gat aga gag gac aaa tca 3544
Leu Asp Asp Val Gln Lys Leu Ile Lys Asp Arg Glu Asp Lys Ser
1010 1015 1020
aga agt tcc ctt aaa cct atc aag aat aaa cca tca aag tca aat 3589
Arg Ser Ser Leu Lys Pro Ile Lys Asn Lys Pro Ser Lys Ser Asn
1025 1030 1035
aaa ggt agt ata gat caa tca gtg tta aaa gaa tta ccc cct gaa 3634
Lys Gly Ser Ile Asp Gln Ser Val Leu Lys Glu Leu Pro Pro Glu
1040 1045 1050
ctc ctg gca gaa att gag tcc acc atg cca ctt tgt gaa cgt gtg 3679
Leu Leu Ala Glu Ile Glu Ser Thr Met Pro Leu Cys Glu Arg Val
1055 1060 1065
aaa atg aac aaa cgc aag cgt agc aca gtt aat gaa aag cca aaa 3724
Lys Met Asn Lys Arg Lys Arg Ser Thr Val Asn Glu Lys Pro Lys
1070 1075 1080
tat gct gaa atc agt tca gat gaa gat aat gat agt gat gaa gct 3769
Tyr Ala Glu Ile Ser Ser Asp Glu Asp Asn Asp Ser Asp Glu Ala
1085 1090 1095
ttt gaa tcc tct agg aaa cga cat aaa aaa gat gat gat aaa gct 3814
Phe Glu Ser Ser Arg Lys Arg His Lys Lys Asp Asp Asp Lys Ala
1100 1105 1110
tgg gaa tat gaa gag cgt gac aga aga agc tct ggg gat cat agg 3859
Trp Glu Tyr Glu Glu Arg Asp Arg Arg Ser Ser Gly Asp His Arg
1115 1120 1125
aga agt ggc cac tct cat gaa gga aga agg agt tca ggt ggt ggt 3904
Arg Ser Gly His Ser His Glu Gly Arg Arg Ser Ser Gly Gly Gly
1130 1135 1140
cgt tat cga aac cga agt ccg tca gat tct gac atg gaa gat tat 3949
Arg Tyr Arg Asn Arg Ser Pro Ser Asp Ser Asp Met Glu Asp Tyr
1145 1150 1155
tct cct cct ccc agc ctt agt gag gtt gct agg aaa atg aag aaa 3994
Ser Pro Pro Pro Ser Leu Ser Glu Val Ala Arg Lys Met Lys Lys
1160 1165 1170
aaa gaa aaa cag aag aaa agg aaa gca tat gaa cca aaa cta aca 4039
Lys Glu Lys Gln Lys Lys Arg Lys Ala Tyr Glu Pro Lys Leu Thr
1175 1180 1185
cct gaa gaa atg atg gac tct tca act ttt aag aga ttc aca gcc 4084
Pro Glu Glu Met Met Asp Ser Ser Thr Phe Lys Arg Phe Thr Ala
1190 1195 1200
tca ata gag aat att ttg gat aat ttg gaa gat atg gat ttt act 4129
Ser Ile Glu Asn Ile Leu Asp Asn Leu Glu Asp Met Asp Phe Thr
1205 1210 1215
gcg ttt ggt gat gat gat gaa att cct cag gaa ctg ctc tta gga 4174
Ala Phe Gly Asp Asp Asp Glu Ile Pro Gln Glu Leu Leu Leu Gly
1220 1225 1230
aaa cat cag ctt aat gaa ctt ggc agt gaa tct gct aaa ata aaa 4219
Lys His Gln Leu Asn Glu Leu Gly Ser Glu Ser Ala Lys Ile Lys
1235 1240 1245
gca atg ggt ata atg gat aag ctt tca act gac aaa act gtg aaa 4264
Ala Met Gly Ile Met Asp Lys Leu Ser Thr Asp Lys Thr Val Lys
1250 1255 1260
gtc tta aat atc ttg gag aag aat att cag gat ggg tca aag ctt 4309
Val Leu Asn Ile Leu Glu Lys Asn Ile Gln Asp Gly Ser Lys Leu
1265 1270 1275
tcc act ttg tta aat cat aat aac gat act gaa gaa gaa gaa agg 4354
Ser Thr Leu Leu Asn His Asn Asn Asp Thr Glu Glu Glu Glu Arg
1280 1285 1290
tta tgg aga gac ctt att atg gag aga gtt aca aaa tca gcg gat 4399
Leu Trp Arg Asp Leu Ile Met Glu Arg Val Thr Lys Ser Ala Asp
1295 1300 1305
gct tgt ctt aca act atc aac att atg aca tcc cct aac atg cca 4444
Ala Cys Leu Thr Thr Ile Asn Ile Met Thr Ser Pro Asn Met Pro
1310 1315 1320
aaa gct gtg tac att gag gat gta att gaa aga gtt ata cag tac 4489
Lys Ala Val Tyr Ile Glu Asp Val Ile Glu Arg Val Ile Gln Tyr
1325 1330 1335
act aaa ttt cat ttg cag aat aca ctt tat cct cag tat gat cct 4534
Thr Lys Phe His Leu Gln Asn Thr Leu Tyr Pro Gln Tyr Asp Pro
1340 1345 1350
gtt tac aga tta gat cct cat gga gga ggc tta tta agt tca aaa 4579
Val Tyr Arg Leu Asp Pro His Gly Gly Gly Leu Leu Ser Ser Lys
1355 1360 1365
gca aaa cgg gct aaa tgt tct acc cat aag cag aga gta ata gta 4624
Ala Lys Arg Ala Lys Cys Ser Thr His Lys Gln Arg Val Ile Val
1370 1375 1380
atg ctt tat aac aaa gtt tgt gac att gtt agc agc tta tca gaa 4669
Met Leu Tyr Asn Lys Val Cys Asp Ile Val Ser Ser Leu Ser Glu
1385 1390 1395
ttg cta gag ata caa ctt ctt aca gac aca aca att ctt cag gtt 4714
Leu Leu Glu Ile Gln Leu Leu Thr Asp Thr Thr Ile Leu Gln Val
1400 1405 1410
tca tct atg gga ata aca cca ttt ttt gtg gaa aat gtc agt gaa 4759
Ser Ser Met Gly Ile Thr Pro Phe Phe Val Glu Asn Val Ser Glu
1415 1420 1425
cta cag ttg tgt gcc att aag tta gtc act gca gta ttc tca aga 4804
Leu Gln Leu Cys Ala Ile Lys Leu Val Thr Ala Val Phe Ser Arg
1430 1435 1440
tat gaa aaa cat agg cag tta att ttg gaa gaa att ttt act tca 4849
Tyr Glu Lys His Arg Gln Leu Ile Leu Glu Glu Ile Phe Thr Ser
1445 1450 1455
ctt gca aga tta cca acc agc aag agg agt tta agg aac ttc agg 4894
Leu Ala Arg Leu Pro Thr Ser Lys Arg Ser Leu Arg Asn Phe Arg
1460 1465 1470
tta aac agt agt gat atg gat gga gaa cct atg tat att cag atg 4939
Leu Asn Ser Ser Asp Met Asp Gly Glu Pro Met Tyr Ile Gln Met
1475 1480 1485
gtt aca gca ctg gtt tta caa ctt att cag tgt gtg gta cac tta 4984
Val Thr Ala Leu Val Leu Gln Leu Ile Gln Cys Val Val His Leu
1490 1495 1500
cca tca tca gag aag gac tct aat gca gaa gaa gat tca aat aaa 5029
Pro Ser Ser Glu Lys Asp Ser Asn Ala Glu Glu Asp Ser Asn Lys
1505 1510 1515
aaa att gac cag gat gtt gtc att act aac tct tat gaa aca gct 5074
Lys Ile Asp Gln Asp Val Val Ile Thr Asn Ser Tyr Glu Thr Ala
1520 1525 1530
atg cga aca gcc caa aac ttc ctc tcc atc ttc ctt aaa aaa tgt 5119
Met Arg Thr Ala Gln Asn Phe Leu Ser Ile Phe Leu Lys Lys Cys
1535 1540 1545
ggt agt aag caa ggt gaa gaa gat tac aga cca ctg ttt gaa aat 5164
Gly Ser Lys Gln Gly Glu Glu Asp Tyr Arg Pro Leu Phe Glu Asn
1550 1555 1560
ttt gtt caa gac ctt ctt tca aca gtc aat aag cct gaa tgg cca 5209
Phe Val Gln Asp Leu Leu Ser Thr Val Asn Lys Pro Glu Trp Pro
1565 1570 1575
gct gct gaa cta ctc ctt agt ttg tta ggg aga ctg ttg gtt cat 5254
Ala Ala Glu Leu Leu Leu Ser Leu Leu Gly Arg Leu Leu Val His
1580 1585 1590
cag ttc agt aac aag tca aca gag atg gct tta aga gtg gca tct 5299
Gln Phe Ser Asn Lys Ser Thr Glu Met Ala Leu Arg Val Ala Ser
1595 1600 1605
ctt gat tac ctt gga act gtt gct gca cgg cta aga aaa gat gct 5344
Leu Asp Tyr Leu Gly Thr Val Ala Ala Arg Leu Arg Lys Asp Ala
1610 1615 1620
gtt aca agc aaa atg gat caa gga tct ata gaa cgc att tta aaa 5389
Val Thr Ser Lys Met Asp Gln Gly Ser Ile Glu Arg Ile Leu Lys
1625 1630 1635
cag gtt tca gga ggg gaa gat gaa atc caa caa tta caa aaa gca 5434
Gln Val Ser Gly Gly Glu Asp Glu Ile Gln Gln Leu Gln Lys Ala
1640 1645 1650
ttg ctt gat tac ttg gat gaa aac act gag act gat cct tca cta 5479
Leu Leu Asp Tyr Leu Asp Glu Asn Thr Glu Thr Asp Pro Ser Leu
1655 1660 1665
gtg ttt tct cgt aaa ttc tat ata gcc cag tgg ttt cga gac aca 5524
Val Phe Ser Arg Lys Phe Tyr Ile Ala Gln Trp Phe Arg Asp Thr
1670 1675 1680
act ctg gaa aca gaa aaa gca atg aaa tca caa aaa gat gaa gaa 5569
Thr Leu Glu Thr Glu Lys Ala Met Lys Ser Gln Lys Asp Glu Glu
1685 1690 1695
tca tct gaa gga aca cat cat gca aag gaa att gag aca act ggc 5614
Ser Ser Glu Gly Thr His His Ala Lys Glu Ile Glu Thr Thr Gly
1700 1705 1710
caa att atg cat cga gct gaa aac cga aaa aag ttt ctt aga agc 5659
Gln Ile Met His Arg Ala Glu Asn Arg Lys Lys Phe Leu Arg Ser
1715 1720 1725
att atc aaa acc aca cct tct cag ttt agc aca tta aag atg aac 5704
Ile Ile Lys Thr Thr Pro Ser Gln Phe Ser Thr Leu Lys Met Asn
1730 1735 1740
tct gat act gtg gac tat gat gat gct tgc ttg att gtt cga tac 5749
Ser Asp Thr Val Asp Tyr Asp Asp Ala Cys Leu Ile Val Arg Tyr
1745 1750 1755
ttg gcc tcc atg agg ccg ttt gcc cag agc ttt gat att tat ttg 5794
Leu Ala Ser Met Arg Pro Phe Ala Gln Ser Phe Asp Ile Tyr Leu
1760 1765 1770
aca cag atc cta cga gtt ctt ggt gaa aat gca att gct gtt cga 5839
Thr Gln Ile Leu Arg Val Leu Gly Glu Asn Ala Ile Ala Val Arg
1775 1780 1785
aca aaa gcc atg aag tgt ttg tct gag gtt gtt gct gta gac ccc 5884
Thr Lys Ala Met Lys Cys Leu Ser Glu Val Val Ala Val Asp Pro
1790 1795 1800
agt att cta gca agg ctt gat atg caa cga ggt gtt cat gga cga 5929
Ser Ile Leu Ala Arg Leu Asp Met Gln Arg Gly Val His Gly Arg
1805 1810 1815
ttg atg gat aat tcg act agt gtc cga gaa gca gca gta gaa tta 5974
Leu Met Asp Asn Ser Thr Ser Val Arg Glu Ala Ala Val Glu Leu
1820 1825 1830
cta ggt cga ttt gtc ctt tgt cga cct cag ctt gct gaa cag tat 6019
Leu Gly Arg Phe Val Leu Cys Arg Pro Gln Leu Ala Glu Gln Tyr
1835 1840 1845
tat gat atg ctg att gaa aga ata ttg gat act ggt atc agt gtc 6064
Tyr Asp Met Leu Ile Glu Arg Ile Leu Asp Thr Gly Ile Ser Val
1850 1855 1860
agg aaa aga gta ata aag att ctc aga gac att tgt att gaa caa 6109
Arg Lys Arg Val Ile Lys Ile Leu Arg Asp Ile Cys Ile Glu Gln
1865 1870 1875
cca aca ttt cca aaa atc aca gaa atg tgt gta aaa atg att cgc 6154
Pro Thr Phe Pro Lys Ile Thr Glu Met Cys Val Lys Met Ile Arg
1880 1885 1890
aga gtc aat gat gaa gag ggc att aag aaa tta gta aat gaa aca 6199
Arg Val Asn Asp Glu Glu Gly Ile Lys Lys Leu Val Asn Glu Thr
1895 1900 1905
ttc cag aaa ctc tgg ttt act cca act cca cac aat gac aaa gaa 6244
Phe Gln Lys Leu Trp Phe Thr Pro Thr Pro His Asn Asp Lys Glu
1910 1915 1920
gca atg aca agg aaa att tta aac att acc gat gtg gtt gca gca 6289
Ala Met Thr Arg Lys Ile Leu Asn Ile Thr Asp Val Val Ala Ala
1925 1930 1935
tgc aga gat act gga tat gac tgg ttt gag caa ctg ctt caa aac 6334
Cys Arg Asp Thr Gly Tyr Asp Trp Phe Glu Gln Leu Leu Gln Asn
1940 1945 1950
ttg ttg aag tcc gaa gag gat tcc tca tat aaa cct gtg aag aaa 6379
Leu Leu Lys Ser Glu Glu Asp Ser Ser Tyr Lys Pro Val Lys Lys
1955 1960 1965
gct tgt act caa ctt gtt gat aac cta gtt gag cac att ctt aaa 6424
Ala Cys Thr Gln Leu Val Asp Asn Leu Val Glu His Ile Leu Lys
1970 1975 1980
tat gag gaa tct cta gct gac tct gac aat aaa ggt gtg aat tct 6469
Tyr Glu Glu Ser Leu Ala Asp Ser Asp Asn Lys Gly Val Asn Ser
1985 1990 1995
gga aga ttg gta gct tgc ata acc act ttg ttc tta ttc agc aaa 6514
Gly Arg Leu Val Ala Cys Ile Thr Thr Leu Phe Leu Phe Ser Lys
2000 2005 2010
ata aga ccc cag ctc atg gtt aaa cat gca atg act atg caa cca 6559
Ile Arg Pro Gln Leu Met Val Lys His Ala Met Thr Met Gln Pro
2015 2020 2025
tac ctt acc act aaa tgt agt acg caa aat gat ttc atg gtt atc 6604
Tyr Leu Thr Thr Lys Cys Ser Thr Gln Asn Asp Phe Met Val Ile
2030 2035 2040
tgc aat gtt gca aaa atc cta gag cta gtt gta cca ctg atg gag 6649
Cys Asn Val Ala Lys Ile Leu Glu Leu Val Val Pro Leu Met Glu
2045 2050 2055
cat cca agt gaa act ttt ctt gcc act att gag gaa gat cta atg 6694
His Pro Ser Glu Thr Phe Leu Ala Thr Ile Glu Glu Asp Leu Met
2060 2065 2070
aag ctc atc atc aaa tat ggc atg act gta gtg caa cat tgt gtg 6739
Lys Leu Ile Ile Lys Tyr Gly Met Thr Val Val Gln His Cys Val
2075 2080 2085
agc tgt ctt gga gct gtt gta aat aaa gtg aca caa aat ttt aaa 6784
Ser Cys Leu Gly Ala Val Val Asn Lys Val Thr Gln Asn Phe Lys
2090 2095 2100
ttt gtg tgg gct tgt ttc aat aga tac tat ggt gcc att tca aaa 6829
Phe Val Trp Ala Cys Phe Asn Arg Tyr Tyr Gly Ala Ile Ser Lys
2105 2110 2115
tta aaa agt caa cac caa gag gac cca aat aac act tca ctt cta 6874
Leu Lys Ser Gln His Gln Glu Asp Pro Asn Asn Thr Ser Leu Leu
2120 2125 2130
aca aac aaa cca gca ctt ctt aga tcc ctt ttc acc gtt gga gca 6919
Thr Asn Lys Pro Ala Leu Leu Arg Ser Leu Phe Thr Val Gly Ala
2135 2140 2145
cta tgt cgg cat ttt gat ttt gat ctg gaa gat ttt aaa ggc aac 6964
Leu Cys Arg His Phe Asp Phe Asp Leu Glu Asp Phe Lys Gly Asn
2150 2155 2160
agc aag gtt aac ata aaa gat aaa gta ctt gaa cta ttg atg tat 7009
Ser Lys Val Asn Ile Lys Asp Lys Val Leu Glu Leu Leu Met Tyr
2165 2170 2175
ttt aca aaa cac tca gat gaa gaa gta caa aca aaa gct atc att 7054
Phe Thr Lys His Ser Asp Glu Glu Val Gln Thr Lys Ala Ile Ile
2180 2185 2190
ggt cta gga ttt gcc ttt att cag cat cca agt cta atg ttc gag 7099
Gly Leu Gly Phe Ala Phe Ile Gln His Pro Ser Leu Met Phe Glu
2195 2200 2205
caa gaa gtg aag aat cta tat aat aat att tta tct gat aag aac 7144
Gln Glu Val Lys Asn Leu Tyr Asn Asn Ile Leu Ser Asp Lys Asn
2210 2215 2220
tcc tca gtc aat tta aaa ata caa gtg tta aaa aac ctc cag acc 7189
Ser Ser Val Asn Leu Lys Ile Gln Val Leu Lys Asn Leu Gln Thr
2225 2230 2235
tac cta caa gaa gaa gat aca cgt atg cag cag gca gat aga gac 7234
Tyr Leu Gln Glu Glu Asp Thr Arg Met Gln Gln Ala Asp Arg Asp
2240 2245 2250
tgg aag aaa gtt gca aaa cag gaa gac tta aaa gaa atg ggt gat 7279
Trp Lys Lys Val Ala Lys Gln Glu Asp Leu Lys Glu Met Gly Asp
2255 2260 2265
gtt tcc tca ggg atg agt agt tcc atc atg cag ctt tat ctc aaa 7324
Val Ser Ser Gly Met Ser Ser Ser Ile Met Gln Leu Tyr Leu Lys
2270 2275 2280
cag gtg ctt gag gca ttt ttt cac acc cag tca agt gta cgc cac 7369
Gln Val Leu Glu Ala Phe Phe His Thr Gln Ser Ser Val Arg His
2285 2290 2295
ttt gcc cta aat gtc att gca ttg act cta aat caa ggt ctt att 7414
Phe Ala Leu Asn Val Ile Ala Leu Thr Leu Asn Gln Gly Leu Ile
2300 2305 2310
cat cca gtt cag tgt gtg cca tat tta att gct atg ggc aca gac 7459
His Pro Val Gln Cys Val Pro Tyr Leu Ile Ala Met Gly Thr Asp
2315 2320 2325
cca gaa cct gct atg cgg aac aag gct gat cag caa ctt gtg gaa 7504
Pro Glu Pro Ala Met Arg Asn Lys Ala Asp Gln Gln Leu Val Glu
2330 2335 2340
ata gac aaa aaa tat gct gga ttc att cat atg aaa gca gtg gct 7549
Ile Asp Lys Lys Tyr Ala Gly Phe Ile His Met Lys Ala Val Ala
2345 2350 2355
ggt atg aag atg tct tac cag gta caa cag gca atc aac aca tgc 7594
Gly Met Lys Met Ser Tyr Gln Val Gln Gln Ala Ile Asn Thr Cys
2360 2365 2370
cta aaa gat cct gta agg ggt ttc aga caa gac gag tcc tct agc 7639
Leu Lys Asp Pro Val Arg Gly Phe Arg Gln Asp Glu Ser Ser Ser
2375 2380 2385
gct ttg tgt tca cac ctt tac tcc atg atc cgt gga aac cgc caa 7684
Ala Leu Cys Ser His Leu Tyr Ser Met Ile Arg Gly Asn Arg Gln
2390 2395 2400
cac aga cga gcc ttt ctt att tct tta ctc aac ctc ttt gat gac 7729
His Arg Arg Ala Phe Leu Ile Ser Leu Leu Asn Leu Phe Asp Asp
2405 2410 2415
aca gca aaa aca gac gtg act atg ctc ttg tat ata gca gac aat 7774
Thr Ala Lys Thr Asp Val Thr Met Leu Leu Tyr Ile Ala Asp Asn
2420 2425 2430
cta gcc tgt ttt cca tac cag aca cag gaa gag ccg ttg ttt ata 7819
Leu Ala Cys Phe Pro Tyr Gln Thr Gln Glu Glu Pro Leu Phe Ile
2435 2440 2445
atg cat cat ata gac att aca ctc tca gtt tct ggt agt aac cta 7864
Met His His Ile Asp Ile Thr Leu Ser Val Ser Gly Ser Asn Leu
2450 2455 2460
ctg cag tca ttc aag gag tct atg gta aag gac aaa agg aaa gag 7909
Leu Gln Ser Phe Lys Glu Ser Met Val Lys Asp Lys Arg Lys Glu
2465 2470 2475
aga aaa tca tca cct agt aag gaa aat gag tca agc gac agt gaa 7954
Arg Lys Ser Ser Pro Ser Lys Glu Asn Glu Ser Ser Asp Ser Glu
2480 2485 2490
gaa gaa gtt tcc agg cct cgg aag tca cgg aaa cgt gta gat tca 7999
Glu Glu Val Ser Arg Pro Arg Lys Ser Arg Lys Arg Val Asp Ser
2495 2500 2505
gat tca gat tca gat tca gaa gac gat ata aat tca gtg atg aaa 8044
Asp Ser Asp Ser Asp Ser Glu Asp Asp Ile Asn Ser Val Met Lys
2510 2515 2520
tgt ttg cca gaa aat tca gct cct tta atc gaa ttt gca aat gtg 8089
Cys Leu Pro Glu Asn Ser Ala Pro Leu Ile Glu Phe Ala Asn Val
2525 2530 2535
tcc cag ggt att tta tta ctt ctc atg tta aaa caa cat ttg aag 8134
Ser Gln Gly Ile Leu Leu Leu Leu Met Leu Lys Gln His Leu Lys
2540 2545 2550
aat ctt tgt gga ttt tct gat agt aaa att cag aag tac tct cca 8179
Asn Leu Cys Gly Phe Ser Asp Ser Lys Ile Gln Lys Tyr Ser Pro
2555 2560 2565
tct gaa tct gca aaa gta tat gat aaa gcg ata aac cga aaa aca 8224
Ser Glu Ser Ala Lys Val Tyr Asp Lys Ala Ile Asn Arg Lys Thr
2570 2575 2580
gga gtt cat ttt cat cca aaa caa aca ctg gac ttc ctg cgg agt 8269
Gly Val His Phe His Pro Lys Gln Thr Leu Asp Phe Leu Arg Ser
2585 2590 2595
gac atg gct aat tcc aaa atc aca gaa gag gtg aaa agg agt ata 8314
Asp Met Ala Asn Ser Lys Ile Thr Glu Glu Val Lys Arg Ser Ile
2600 2605 2610
gta aaa cag tat cta gat ttc aaa ctt ctc atg gaa cat ctg gac 8359
Val Lys Gln Tyr Leu Asp Phe Lys Leu Leu Met Glu His Leu Asp
2615 2620 2625
cct gat gaa gaa gaa gaa gaa ggg gag gtt tca gct agc aca aat 8404
Pro Asp Glu Glu Glu Glu Glu Gly Glu Val Ser Ala Ser Thr Asn
2630 2635 2640
gct cgg aac aaa gca att acc tca ctg ctt gga gga ggc agc cct 8449
Ala Arg Asn Lys Ala Ile Thr Ser Leu Leu Gly Gly Gly Ser Pro
2645 2650 2655
aaa aat aat aca gca gca gag aca gaa gat gat gaa agt gat ggg 8494
Lys Asn Asn Thr Ala Ala Glu Thr Glu Asp Asp Glu Ser Asp Gly
2660 2665 2670
gag gat aga gga gga ggc act tca ggg gtg agg cgg agg agg agt 8539
Glu Asp Arg Gly Gly Gly Thr Ser Gly Val Arg Arg Arg Arg Ser
2675 2680 2685
caa cgt att tcg cag cgt att acg taa aatgattttt atgtgcttat 8586
Gln Arg Ile Ser Gln Arg Ile Thr
2690 2695
atatgtcagt ctattaaatg tacaccaagt aatgtaatac ttaaaagaga aaacattttg 8646
tagatagaga ttctctactt acccgtttat acatcctttt gtagaaagtt taacataaaa 8706
gacaataaaa aaacagaaat gagattt 8733


12
2697
PRT
Homo sapiens

12
Met Asn Gly Asp Met Pro His Val Pro Ile Thr Thr Leu Ala Gly Ile
1 5 10 15
Ala Ser Leu Thr Asp Leu Leu Asn Gln Leu Pro Leu Pro Ser Pro Leu
20 25 30
Pro Ala Thr Thr Thr Lys Ser Leu Leu Phe Asn Ala Arg Ile Ala Glu
35 40 45
Glu Val Asn Cys Leu Leu Ala Cys Arg Asp Asp Asn Leu Val Ser Gln
50 55 60
Leu Val His Ser Leu Asn Gln Val Ser Thr Asp His Ile Glu Leu Lys
65 70 75 80
Asp Asn Leu Gly Ser Asp Asp Pro Glu Gly Asp Ile Pro Val Leu Leu
85 90 95
Gln Ala Val Leu Ala Arg Ser Pro Asn Val Phe Arg Glu Lys Ser Met
100 105 110
Gln Asn Arg Tyr Val Gln Ser Gly Met Met Met Ser Gln Tyr Lys Leu
115 120 125
Ser Gln Asn Ser Met His Ser Ser Pro Ala Ser Ser Asn Tyr Gln Gln
130 135 140
Thr Thr Ile Ser His Ser Pro Ser Ser Arg Phe Val Pro Pro Gln Thr
145 150 155 160
Ser Ser Gly Asn Arg Phe Met Pro Gln Gln Asn Ser Pro Val Pro Ser
165 170 175
Pro Tyr Ala Pro Gln Ser Pro Ala Gly Tyr Met Pro Tyr Ser His Pro
180 185 190
Ser Ser Tyr Thr Thr His Pro Gln Met Gln Gln Ala Ser Val Ser Ser
195 200 205
Pro Ile Val Ala Gly Gly Leu Arg Asn Ile His Asp Asn Lys Val Ser
210 215 220
Gly Pro Leu Ser Gly Asn Ser Ala Asn His His Ala Asp Asn Pro Arg
225 230 235 240
His Gly Ser Ser Glu Asp Tyr Leu His Met Val His Arg Leu Ser Ser
245 250 255
Asp Asp Gly Asp Ser Ser Thr Met Arg Asn Ala Ala Ser Phe Pro Leu
260 265 270
Arg Ser Pro Gln Pro Val Cys Ser Pro Ala Gly Ser Glu Gly Thr Pro
275 280 285
Lys Gly Ser Arg Pro Pro Leu Ile Leu Gln Ser Gln Ser Leu Pro Cys
290 295 300
Ser Ser Pro Arg Asp Val Pro Pro Asp Ile Leu Leu Asp Ser Pro Glu
305 310 315 320
Arg Lys Gln Lys Lys Gln Lys Lys Met Lys Leu Gly Lys Asp Glu Lys
325 330 335
Glu Gln Ser Glu Lys Ala Ala Met Tyr Asp Ile Ile Ser Ser Pro Ser
340 345 350
Lys Asp Ser Thr Lys Leu Thr Leu Arg Leu Ser Arg Val Arg Ser Ser
355 360 365
Asp Met Asp Gln Gln Glu Asp Met Ile Ser Gly Val Glu Asn Ser Asn
370 375 380
Val Ser Glu Asn Asp Ile Pro Phe Asn Val Gln Tyr Pro Gly Gln Thr
385 390 395 400
Ser Lys Thr Pro Ile Thr Pro Gln Asp Ile Asn Arg Pro Leu Asn Ala
405 410 415
Ala Gln Cys Leu Ser Gln Gln Glu Gln Thr Ala Phe Leu Pro Ala Asn
420 425 430
Gln Val Pro Val Leu Gln Gln Asn Thr Ser Val Ala Ala Lys Gln Pro
435 440 445
Gln Thr Ser Val Val Gln Asn Gln Gln Gln Ile Ser Gln Gln Gly Pro
450 455 460
Ile Tyr Asp Glu Val Glu Leu Asp Ala Leu Ala Glu Ile Glu Arg Ile
465 470 475 480
Glu Arg Glu Ser Ala Ile Glu Arg Glu Arg Phe Ser Lys Glu Val Gln
485 490 495
Asp Lys Asp Lys Pro Leu Lys Lys Arg Lys Gln Asp Ser Tyr Pro Gln
500 505 510
Glu Ala Gly Gly Ala Thr Gly Gly Asn Arg Pro Ala Ser Gln Glu Thr
515 520 525
Gly Ser Thr Gly Asn Gly Ser Arg Pro Ala Leu Met Val Ser Ile Asp
530 535 540
Leu His Gln Ala Gly Arg Val Asp Ser Gln Ala Ser Ile Thr Gln Asp
545 550 555 560
Ser Asp Ser Ile Lys Lys Pro Glu Glu Ile Lys Gln Cys Asn Asp Ala
565 570 575
Pro Val Ser Val Leu Gln Glu Asp Ile Val Gly Ser Leu Lys Ser Thr
580 585 590
Pro Glu Asn His Pro Glu Thr Pro Lys Lys Lys Ser Asp Pro Glu Leu
595 600 605
Ser Lys Ser Glu Met Lys Gln Ser Glu Ser Arg Leu Ala Glu Ser Lys
610 615 620
Pro Asn Glu Asn Arg Leu Val Glu Thr Lys Ser Ser Glu Asn Lys Leu
625 630 635 640
Glu Thr Lys Val Glu Thr Gln Thr Glu Glu Leu Lys Gln Asn Glu Ser
645 650 655
Arg Thr Thr Glu Cys Lys Gln Asn Glu Ser Thr Ile Val Glu Pro Lys
660 665 670
Gln Asn Glu Asn Arg Leu Ser Asp Thr Lys Pro Asn Asp Asn Lys Gln
675 680 685
Asn Asn Gly Arg Ser Glu Thr Thr Lys Ser Arg Pro Glu Thr Pro Lys
690 695 700
Gln Lys Gly Glu Ser Arg Pro Glu Thr Pro Lys Gln Lys Ser Asp Gly
705 710 715 720
His Pro Glu Thr Pro Lys Gln Lys Gly Asp Gly Arg Pro Glu Thr Pro
725 730 735
Lys Gln Lys Gly Glu Ser Arg Pro Glu Thr Pro Lys Gln Lys Asn Glu
740 745 750
Gly Arg Pro Glu Thr Pro Lys His Arg His Asp Asn Arg Arg Asp Ser
755 760 765
Gly Lys Pro Ser Thr Glu Lys Lys Pro Glu Val Ser Lys His Lys Gln
770 775 780
Asp Thr Lys Ser Asp Ser Pro Arg Leu Lys Ser Glu Arg Ala Glu Ala
785 790 795 800
Leu Lys Gln Arg Pro Asp Gly Arg Ser Val Ser Glu Ser Leu Arg Arg
805 810 815
Asp His Asp Asn Lys Gln Lys Ser Asp Asp Arg Gly Glu Ser Glu Arg
820 825 830
His Arg Gly Asp Gln Ser Arg Val Arg Arg Pro Glu Thr Leu Arg Ser
835 840 845
Ser Ser Arg Asn Glu His Gly Ile Lys Ser Asp Ser Ser Lys Thr Asp
850 855 860
Lys Leu Glu Arg Lys His Arg His Glu Ser Gly Asp Ser Arg Glu Arg
865 870 875 880
Pro Ser Ser Gly Glu Gln Lys Ser Arg Pro Asp Ser Pro Arg Val Lys
885 890 895
Gln Gly Asp Ser Asn Lys Ser Arg Ser Asp Lys Leu Gly Phe Lys Ser
900 905 910
Pro Thr Ser Lys Asp Asp Lys Arg Thr Glu Gly Asn Lys Ser Lys Val
915 920 925
Asp Thr Asn Lys Ala His Pro Asp Asn Lys Ala Glu Phe Pro Ser Tyr
930 935 940
Leu Leu Gly Gly Arg Ser Gly Ala Leu Lys Asn Phe Val Ile Pro Lys
945 950 955 960
Ile Lys Arg Asp Lys Asp Gly Asn Val Thr Gln Glu Thr Lys Lys Met
965 970 975
Glu Met Lys Gly Glu Pro Lys Asp Lys Val Glu Lys Ile Gly Leu Val
980 985 990
Glu Asp Leu Asn Lys Gly Ala Lys Pro Val Val Val Leu Gln Lys Leu
995 1000 1005
Ser Leu Asp Asp Val Gln Lys Leu Ile Lys Asp Arg Glu Asp Lys
1010 1015 1020
Ser Arg Ser Ser Leu Lys Pro Ile Lys Asn Lys Pro Ser Lys Ser
1025 1030 1035
Asn Lys Gly Ser Ile Asp Gln Ser Val Leu Lys Glu Leu Pro Pro
1040 1045 1050
Glu Leu Leu Ala Glu Ile Glu Ser Thr Met Pro Leu Cys Glu Arg
1055 1060 1065
Val Lys Met Asn Lys Arg Lys Arg Ser Thr Val Asn Glu Lys Pro
1070 1075 1080
Lys Tyr Ala Glu Ile Ser Ser Asp Glu Asp Asn Asp Ser Asp Glu
1085 1090 1095
Ala Phe Glu Ser Ser Arg Lys Arg His Lys Lys Asp Asp Asp Lys
1100 1105 1110
Ala Trp Glu Tyr Glu Glu Arg Asp Arg Arg Ser Ser Gly Asp His
1115 1120 1125
Arg Arg Ser Gly His Ser His Glu Gly Arg Arg Ser Ser Gly Gly
1130 1135 1140
Gly Arg Tyr Arg Asn Arg Ser Pro Ser Asp Ser Asp Met Glu Asp
1145 1150 1155
Tyr Ser Pro Pro Pro Ser Leu Ser Glu Val Ala Arg Lys Met Lys
1160 1165 1170
Lys Lys Glu Lys Gln Lys Lys Arg Lys Ala Tyr Glu Pro Lys Leu
1175 1180 1185
Thr Pro Glu Glu Met Met Asp Ser Ser Thr Phe Lys Arg Phe Thr
1190 1195 1200
Ala Ser Ile Glu Asn Ile Leu Asp Asn Leu Glu Asp Met Asp Phe
1205 1210 1215
Thr Ala Phe Gly Asp Asp Asp Glu Ile Pro Gln Glu Leu Leu Leu
1220 1225 1230
Gly Lys His Gln Leu Asn Glu Leu Gly Ser Glu Ser Ala Lys Ile
1235 1240 1245
Lys Ala Met Gly Ile Met Asp Lys Leu Ser Thr Asp Lys Thr Val
1250 1255 1260
Lys Val Leu Asn Ile Leu Glu Lys Asn Ile Gln Asp Gly Ser Lys
1265 1270 1275
Leu Ser Thr Leu Leu Asn His Asn Asn Asp Thr Glu Glu Glu Glu
1280 1285 1290
Arg Leu Trp Arg Asp Leu Ile Met Glu Arg Val Thr Lys Ser Ala
1295 1300 1305
Asp Ala Cys Leu Thr Thr Ile Asn Ile Met Thr Ser Pro Asn Met
1310 1315 1320
Pro Lys Ala Val Tyr Ile Glu Asp Val Ile Glu Arg Val Ile Gln
1325 1330 1335
Tyr Thr Lys Phe His Leu Gln Asn Thr Leu Tyr Pro Gln Tyr Asp
1340 1345 1350
Pro Val Tyr Arg Leu Asp Pro His Gly Gly Gly Leu Leu Ser Ser
1355 1360 1365
Lys Ala Lys Arg Ala Lys Cys Ser Thr His Lys Gln Arg Val Ile
1370 1375 1380
Val Met Leu Tyr Asn Lys Val Cys Asp Ile Val Ser Ser Leu Ser
1385 1390 1395
Glu Leu Leu Glu Ile Gln Leu Leu Thr Asp Thr Thr Ile Leu Gln
1400 1405 1410
Val Ser Ser Met Gly Ile Thr Pro Phe Phe Val Glu Asn Val Ser
1415 1420 1425
Glu Leu Gln Leu Cys Ala Ile Lys Leu Val Thr Ala Val Phe Ser
1430 1435 1440
Arg Tyr Glu Lys His Arg Gln Leu Ile Leu Glu Glu Ile Phe Thr
1445 1450 1455
Ser Leu Ala Arg Leu Pro Thr Ser Lys Arg Ser Leu Arg Asn Phe
1460 1465 1470
Arg Leu Asn Ser Ser Asp Met Asp Gly Glu Pro Met Tyr Ile Gln
1475 1480 1485
Met Val Thr Ala Leu Val Leu Gln Leu Ile Gln Cys Val Val His
1490 1495 1500
Leu Pro Ser Ser Glu Lys Asp Ser Asn Ala Glu Glu Asp Ser Asn
1505 1510 1515
Lys Lys Ile Asp Gln Asp Val Val Ile Thr Asn Ser Tyr Glu Thr
1520 1525 1530
Ala Met Arg Thr Ala Gln Asn Phe Leu Ser Ile Phe Leu Lys Lys
1535 1540 1545
Cys Gly Ser Lys Gln Gly Glu Glu Asp Tyr Arg Pro Leu Phe Glu
1550 1555 1560
Asn Phe Val Gln Asp Leu Leu Ser Thr Val Asn Lys Pro Glu Trp
1565 1570 1575
Pro Ala Ala Glu Leu Leu Leu Ser Leu Leu Gly Arg Leu Leu Val
1580 1585 1590
His Gln Phe Ser Asn Lys Ser Thr Glu Met Ala Leu Arg Val Ala
1595 1600 1605
Ser Leu Asp Tyr Leu Gly Thr Val Ala Ala Arg Leu Arg Lys Asp
1610 1615 1620
Ala Val Thr Ser Lys Met Asp Gln Gly Ser Ile Glu Arg Ile Leu
1625 1630 1635
Lys Gln Val Ser Gly Gly Glu Asp Glu Ile Gln Gln Leu Gln Lys
1640 1645 1650
Ala Leu Leu Asp Tyr Leu Asp Glu Asn Thr Glu Thr Asp Pro Ser
1655 1660 1665
Leu Val Phe Ser Arg Lys Phe Tyr Ile Ala Gln Trp Phe Arg Asp
1670 1675 1680
Thr Thr Leu Glu Thr Glu Lys Ala Met Lys Ser Gln Lys Asp Glu
1685 1690 1695
Glu Ser Ser Glu Gly Thr His His Ala Lys Glu Ile Glu Thr Thr
1700 1705 1710
Gly Gln Ile Met His Arg Ala Glu Asn Arg Lys Lys Phe Leu Arg
1715 1720 1725
Ser Ile Ile Lys Thr Thr Pro Ser Gln Phe Ser Thr Leu Lys Met
1730 1735 1740
Asn Ser Asp Thr Val Asp Tyr Asp Asp Ala Cys Leu Ile Val Arg
1745 1750 1755
Tyr Leu Ala Ser Met Arg Pro Phe Ala Gln Ser Phe Asp Ile Tyr
1760 1765 1770
Leu Thr Gln Ile Leu Arg Val Leu Gly Glu Asn Ala Ile Ala Val
1775 1780 1785
Arg Thr Lys Ala Met Lys Cys Leu Ser Glu Val Val Ala Val Asp
1790 1795 1800
Pro Ser Ile Leu Ala Arg Leu Asp Met Gln Arg Gly Val His Gly
1805 1810 1815
Arg Leu Met Asp Asn Ser Thr Ser Val Arg Glu Ala Ala Val Glu
1820 1825 1830
Leu Leu Gly Arg Phe Val Leu Cys Arg Pro Gln Leu Ala Glu Gln
1835 1840 1845
Tyr Tyr Asp Met Leu Ile Glu Arg Ile Leu Asp Thr Gly Ile Ser
1850 1855 1860
Val Arg Lys Arg Val Ile Lys Ile Leu Arg Asp Ile Cys Ile Glu
1865 1870 1875
Gln Pro Thr Phe Pro Lys Ile Thr Glu Met Cys Val Lys Met Ile
1880 1885 1890
Arg Arg Val Asn Asp Glu Glu Gly Ile Lys Lys Leu Val Asn Glu
1895 1900 1905
Thr Phe Gln Lys Leu Trp Phe Thr Pro Thr Pro His Asn Asp Lys
1910 1915 1920
Glu Ala Met Thr Arg Lys Ile Leu Asn Ile Thr Asp Val Val Ala
1925 1930 1935
Ala Cys Arg Asp Thr Gly Tyr Asp Trp Phe Glu Gln Leu Leu Gln
1940 1945 1950
Asn Leu Leu Lys Ser Glu Glu Asp Ser Ser Tyr Lys Pro Val Lys
1955 1960 1965
Lys Ala Cys Thr Gln Leu Val Asp Asn Leu Val Glu His Ile Leu
1970 1975 1980
Lys Tyr Glu Glu Ser Leu Ala Asp Ser Asp Asn Lys Gly Val Asn
1985 1990 1995
Ser Gly Arg Leu Val Ala Cys Ile Thr Thr Leu Phe Leu Phe Ser
2000 2005 2010
Lys Ile Arg Pro Gln Leu Met Val Lys His Ala Met Thr Met Gln
2015 2020 2025
Pro Tyr Leu Thr Thr Lys Cys Ser Thr Gln Asn Asp Phe Met Val
2030 2035 2040
Ile Cys Asn Val Ala Lys Ile Leu Glu Leu Val Val Pro Leu Met
2045 2050 2055
Glu His Pro Ser Glu Thr Phe Leu Ala Thr Ile Glu Glu Asp Leu
2060 2065 2070
Met Lys Leu Ile Ile Lys Tyr Gly Met Thr Val Val Gln His Cys
2075 2080 2085
Val Ser Cys Leu Gly Ala Val Val Asn Lys Val Thr Gln Asn Phe
2090 2095 2100
Lys Phe Val Trp Ala Cys Phe Asn Arg Tyr Tyr Gly Ala Ile Ser
2105 2110 2115
Lys Leu Lys Ser Gln His Gln Glu Asp Pro Asn Asn Thr Ser Leu
2120 2125 2130
Leu Thr Asn Lys Pro Ala Leu Leu Arg Ser Leu Phe Thr Val Gly
2135 2140 2145
Ala Leu Cys Arg His Phe Asp Phe Asp Leu Glu Asp Phe Lys Gly
2150 2155 2160
Asn Ser Lys Val Asn Ile Lys Asp Lys Val Leu Glu Leu Leu Met
2165 2170 2175
Tyr Phe Thr Lys His Ser Asp Glu Glu Val Gln Thr Lys Ala Ile
2180 2185 2190
Ile Gly Leu Gly Phe Ala Phe Ile Gln His Pro Ser Leu Met Phe
2195 2200 2205
Glu Gln Glu Val Lys Asn Leu Tyr Asn Asn Ile Leu Ser Asp Lys
2210 2215 2220
Asn Ser Ser Val Asn Leu Lys Ile Gln Val Leu Lys Asn Leu Gln
2225 2230 2235
Thr Tyr Leu Gln Glu Glu Asp Thr Arg Met Gln Gln Ala Asp Arg
2240 2245 2250
Asp Trp Lys Lys Val Ala Lys Gln Glu Asp Leu Lys Glu Met Gly
2255 2260 2265
Asp Val Ser Ser Gly Met Ser Ser Ser Ile Met Gln Leu Tyr Leu
2270 2275 2280
Lys Gln Val Leu Glu Ala Phe Phe His Thr Gln Ser Ser Val Arg
2285 2290 2295
His Phe Ala Leu Asn Val Ile Ala Leu Thr Leu Asn Gln Gly Leu
2300 2305 2310
Ile His Pro Val Gln Cys Val Pro Tyr Leu Ile Ala Met Gly Thr
2315 2320 2325
Asp Pro Glu Pro Ala Met Arg Asn Lys Ala Asp Gln Gln Leu Val
2330 2335 2340
Glu Ile Asp Lys Lys Tyr Ala Gly Phe Ile His Met Lys Ala Val
2345 2350 2355
Ala Gly Met Lys Met Ser Tyr Gln Val Gln Gln Ala Ile Asn Thr
2360 2365 2370
Cys Leu Lys Asp Pro Val Arg Gly Phe Arg Gln Asp Glu Ser Ser
2375 2380 2385
Ser Ala Leu Cys Ser His Leu Tyr Ser Met Ile Arg Gly Asn Arg
2390 2395 2400
Gln His Arg Arg Ala Phe Leu Ile Ser Leu Leu Asn Leu Phe Asp
2405 2410 2415
Asp Thr Ala Lys Thr Asp Val Thr Met Leu Leu Tyr Ile Ala Asp
2420 2425 2430
Asn Leu Ala Cys Phe Pro Tyr Gln Thr Gln Glu Glu Pro Leu Phe
2435 2440 2445
Ile Met His His Ile Asp Ile Thr Leu Ser Val Ser Gly Ser Asn
2450 2455 2460
Leu Leu Gln Ser Phe Lys Glu Ser Met Val Lys Asp Lys Arg Lys
2465 2470 2475
Glu Arg Lys Ser Ser Pro Ser Lys Glu Asn Glu Ser Ser Asp Ser
2480 2485 2490
Glu Glu Glu Val Ser Arg Pro Arg Lys Ser Arg Lys Arg Val Asp
2495 2500 2505
Ser Asp Ser Asp Ser Asp Ser Glu Asp Asp Ile Asn Ser Val Met
2510 2515 2520
Lys Cys Leu Pro Glu Asn Ser Ala Pro Leu Ile Glu Phe Ala Asn
2525 2530 2535
Val Ser Gln Gly Ile Leu Leu Leu Leu Met Leu Lys Gln His Leu
2540 2545 2550
Lys Asn Leu Cys Gly Phe Ser Asp Ser Lys Ile Gln Lys Tyr Ser
2555 2560 2565
Pro Ser Glu Ser Ala Lys Val Tyr Asp Lys Ala Ile Asn Arg Lys
2570 2575 2580
Thr Gly Val His Phe His Pro Lys Gln Thr Leu Asp Phe Leu Arg
2585 2590 2595
Ser Asp Met Ala Asn Ser Lys Ile Thr Glu Glu Val Lys Arg Ser
2600 2605 2610
Ile Val Lys Gln Tyr Leu Asp Phe Lys Leu Leu Met Glu His Leu
2615 2620 2625
Asp Pro Asp Glu Glu Glu Glu Glu Gly Glu Val Ser Ala Ser Thr
2630 2635 2640
Asn Ala Arg Asn Lys Ala Ile Thr Ser Leu Leu Gly Gly Gly Ser
2645 2650 2655
Pro Lys Asn Asn Thr Ala Ala Glu Thr Glu Asp Asp Glu Ser Asp
2660 2665 2670
Gly Glu Asp Arg Gly Gly Gly Thr Ser Gly Val Arg Arg Arg Arg
2675 2680 2685
Ser Gln Arg Ile Ser Gln Arg Ile Thr
2690 2695


13
4191
DNA
Homo sapiens

CDS
(121)..(3246)


13
catctccgca gtctgggccg ctgggtgcag aggctgccgc agacccagcg gccatcgcct 60
ccctcaatcc caatatccat tgtctcccac cccacctggc cctccacttc ccccacaacc 120
atg gcg cac gaa tcc gag agg agc tct cgt ctc ggg gtg ccc tgc ggg 168
Met Ala His Glu Ser Glu Arg Ser Ser Arg Leu Gly Val Pro Cys Gly
1 5 10 15
gag ccg gca gag ctc gga ggt gat gct agc gag gag gat cac ccc caa 216
Glu Pro Ala Glu Leu Gly Gly Asp Ala Ser Glu Glu Asp His Pro Gln
20 25 30
gtc tgt gcc aag tgc tgc gca caa ttc act gac cca act gaa ttc ctc 264
Val Cys Ala Lys Cys Cys Ala Gln Phe Thr Asp Pro Thr Glu Phe Leu
35 40 45
gcc cac cag aac gca tgt tct act gac cct cct gta atg gtg ata att 312
Ala His Gln Asn Ala Cys Ser Thr Asp Pro Pro Val Met Val Ile Ile
50 55 60
ggg ggc cag gag aac ccc aac aac tct tcg gcc tcc tct gaa ccc cgg 360
Gly Gly Gln Glu Asn Pro Asn Asn Ser Ser Ala Ser Ser Glu Pro Arg
65 70 75 80
cct gag ggt cac aat aat cct cag gtc atg gac aca gag cat agc aac 408
Pro Glu Gly His Asn Asn Pro Gln Val Met Asp Thr Glu His Ser Asn
85 90 95
ccc cca gat tct ggg tcc tcc gtg ccc acg gat ccc acc tgg ggc cca 456
Pro Pro Asp Ser Gly Ser Ser Val Pro Thr Asp Pro Thr Trp Gly Pro
100 105 110
gag agg aga gga gag gag tct tca ggg cat ttc ctg gtc gct gcc aca 504
Glu Arg Arg Gly Glu Glu Ser Ser Gly His Phe Leu Val Ala Ala Thr
115 120 125
ggt aca gcg gct ggg gga ggc ggg ggc ctg atc ttg gcc agt ccc aag 552
Gly Thr Ala Ala Gly Gly Gly Gly Gly Leu Ile Leu Ala Ser Pro Lys
130 135 140
ctg gga gca acc cca tta cct cca gaa tcg acc cct gca ccc cct cct 600
Leu Gly Ala Thr Pro Leu Pro Pro Glu Ser Thr Pro Ala Pro Pro Pro
145 150 155 160
cct cca cca ccc cct ccg ccc cca ggg gta ggc agt ggc cac ttg aat 648
Pro Pro Pro Pro Pro Pro Pro Pro Gly Val Gly Ser Gly His Leu Asn
165 170 175
atc ccc ctg atc ttg gaa gag cta cgg gtg ctg cag cag cgg cag atc 696
Ile Pro Leu Ile Leu Glu Glu Leu Arg Val Leu Gln Gln Arg Gln Ile
180 185 190
cat cag atg cag atg act gag caa atc tgc agg cag gtg ctg ttg ctt 744
His Gln Met Gln Met Thr Glu Gln Ile Cys Arg Gln Val Leu Leu Leu
195 200 205
ggc tcc tta ggc cag acg gtg ggt gcc cct gcc agt ccc tca gag cta 792
Gly Ser Leu Gly Gln Thr Val Gly Ala Pro Ala Ser Pro Ser Glu Leu
210 215 220
cct ggg aca ggg act gcc tct tcc acc aag ccc cta cta ccc ctc ttc 840
Pro Gly Thr Gly Thr Ala Ser Ser Thr Lys Pro Leu Leu Pro Leu Phe
225 230 235 240
agc ccc atc aag cct gtc caa acc agc aag aca ctg gca tct tcc tcc 888
Ser Pro Ile Lys Pro Val Gln Thr Ser Lys Thr Leu Ala Ser Ser Ser
245 250 255
tcc tcc tcc tct tcc tct tca ggg gca gaa acg ccc aag cag gcc ttc 936
Ser Ser Ser Ser Ser Ser Ser Gly Ala Glu Thr Pro Lys Gln Ala Phe
260 265 270
ttc cac ctt tac cac cca ctg ggg tca cag cat cct ttc tct gct gga 984
Phe His Leu Tyr His Pro Leu Gly Ser Gln His Pro Phe Ser Ala Gly
275 280 285
ggg gtt ggg cga agc cac aaa ccc acc cct gcc cct tcc cca gcc ttg 1032
Gly Val Gly Arg Ser His Lys Pro Thr Pro Ala Pro Ser Pro Ala Leu
290 295 300
cca ggc agc aca gat cag ctg att gcc tcg cct cat ctg gca ttc cca 1080
Pro Gly Ser Thr Asp Gln Leu Ile Ala Ser Pro His Leu Ala Phe Pro
305 310 315 320
agc acc acg gga cta ctg gca gca cag tgt ctt ggg gca gcc cga ggc 1128
Ser Thr Thr Gly Leu Leu Ala Ala Gln Cys Leu Gly Ala Ala Arg Gly
325 330 335
ctt gag gcc act gcc tcc cca ggg ctc ctg aag cca aag aat gga agt 1176
Leu Glu Ala Thr Ala Ser Pro Gly Leu Leu Lys Pro Lys Asn Gly Ser
340 345 350
ggt gag ctg agc tac gga gaa gtg atg ggt ccc ttg gag aag cct ggt 1224
Gly Glu Leu Ser Tyr Gly Glu Val Met Gly Pro Leu Glu Lys Pro Gly
355 360 365
gga agg cac aaa tgc cgc ttc tgt gcc aaa gta ttt ggc agt gac agt 1272
Gly Arg His Lys Cys Arg Phe Cys Ala Lys Val Phe Gly Ser Asp Ser
370 375 380
gcc ctg cag atc cac ctt cgt tcc cac acg ggt gag agg ccc tat aag 1320
Ala Leu Gln Ile His Leu Arg Ser His Thr Gly Glu Arg Pro Tyr Lys
385 390 395 400
tgc aat gtc tgt gga aac cgt ttt acc acc cgt ggc aac ctc aaa gtg 1368
Cys Asn Val Cys Gly Asn Arg Phe Thr Thr Arg Gly Asn Leu Lys Val
405 410 415
cat ttc cac cgg cat cgt gag aag tac cca cat gtg cag atg aac cca 1416
His Phe His Arg His Arg Glu Lys Tyr Pro His Val Gln Met Asn Pro
420 425 430
cac cca gta cca gag cac cta gac tat gtc att acc agc agt ggc ttg 1464
His Pro Val Pro Glu His Leu Asp Tyr Val Ile Thr Ser Ser Gly Leu
435 440 445
cct tat ggt atg tcc gtg cca cca gag aag gcc gag gag gag gca gcc 1512
Pro Tyr Gly Met Ser Val Pro Pro Glu Lys Ala Glu Glu Glu Ala Ala
450 455 460
act cca ggt gga ggg gtt gag cgc aag cct ctg gtg gcc tcc aca aca 1560
Thr Pro Gly Gly Gly Val Glu Arg Lys Pro Leu Val Ala Ser Thr Thr
465 470 475 480
gca ctc agt gcc aca gag agc ctg act ctg ctc tcc acc agt gca ggc 1608
Ala Leu Ser Ala Thr Glu Ser Leu Thr Leu Leu Ser Thr Ser Ala Gly
485 490 495
aca gcc acg gct cca gga ctc cct gct ttc aat aag ttt gtg ctc atg 1656
Thr Ala Thr Ala Pro Gly Leu Pro Ala Phe Asn Lys Phe Val Leu Met
500 505 510
aaa gca gtg gaa ccc aag aat aaa gct gat gaa aac acc ccc cca ggg 1704
Lys Ala Val Glu Pro Lys Asn Lys Ala Asp Glu Asn Thr Pro Pro Gly
515 520 525
agt gag ggc tca gcc atc agt gga gtg gca gaa agt agc acg gca act 1752
Ser Glu Gly Ser Ala Ile Ser Gly Val Ala Glu Ser Ser Thr Ala Thr
530 535 540
cgc atg caa cta agt aag ttg gtg act tca cta cca agc tgg gca ctg 1800
Arg Met Gln Leu Ser Lys Leu Val Thr Ser Leu Pro Ser Trp Ala Leu
545 550 555 560
ctt acc aac cac ttc aag tcc act ggc agc ttc ccc ttc ccc tat gtg 1848
Leu Thr Asn His Phe Lys Ser Thr Gly Ser Phe Pro Phe Pro Tyr Val
565 570 575
cta gag ccc ttg ggg gcc tca ccc tct gag aca tca aag ctg cag caa 1896
Leu Glu Pro Leu Gly Ala Ser Pro Ser Glu Thr Ser Lys Leu Gln Gln
580 585 590
ctg gta gaa aag att gac cgg caa gga gct gtg gcg gtg acc tca gct 1944
Leu Val Glu Lys Ile Asp Arg Gln Gly Ala Val Ala Val Thr Ser Ala
595 600 605
gcc tca gga gcc ccc acc acc tct gcc cct gca cct tca tcc tca gcc 1992
Ala Ser Gly Ala Pro Thr Thr Ser Ala Pro Ala Pro Ser Ser Ser Ala
610 615 620
tct tct gga cct aac cag tgt gtc atc tgt ctc cga gtg ctt agc tgt 2040
Ser Ser Gly Pro Asn Gln Cys Val Ile Cys Leu Arg Val Leu Ser Cys
625 630 635 640
cct cgg gcc cta cgc ctt cat tat ggc caa cat gga ggt gag agg ccc 2088
Pro Arg Ala Leu Arg Leu His Tyr Gly Gln His Gly Gly Glu Arg Pro
645 650 655
ttc aaa tgc aaa gtg tgt ggc aga gcc ttc tcc acc agg ggt aat ctg 2136
Phe Lys Cys Lys Val Cys Gly Arg Ala Phe Ser Thr Arg Gly Asn Leu
660 665 670
cgt gca cat ttc gtg ggc cac aag gcc agt cca gct gcc cgg gca cag 2184
Arg Ala His Phe Val Gly His Lys Ala Ser Pro Ala Ala Arg Ala Gln
675 680 685
aat tcc tgc ccc atc tgc cag aag aag ttc acc aat gct gtc act ctg 2232
Asn Ser Cys Pro Ile Cys Gln Lys Lys Phe Thr Asn Ala Val Thr Leu
690 695 700
cag cag cat gtc cgg atg cac ctg ggg ggc cag atc ccc aac ggt ggt 2280
Gln Gln His Val Arg Met His Leu Gly Gly Gln Ile Pro Asn Gly Gly
705 710 715 720
act gca ctc cct gaa ggt gga gga gct gct cag gag aat ggc tcc gag 2328
Thr Ala Leu Pro Glu Gly Gly Gly Ala Ala Gln Glu Asn Gly Ser Glu
725 730 735
caa tct aca gtc tcc ggg gca ggg agt ttc ccc cag cag cag tcc cag 2376
Gln Ser Thr Val Ser Gly Ala Gly Ser Phe Pro Gln Gln Gln Ser Gln
740 745 750
cag cca tca ccg gaa gag gag ttg tct gag gag gag gaa gag gag gat 2424
Gln Pro Ser Pro Glu Glu Glu Leu Ser Glu Glu Glu Glu Glu Glu Asp
755 760 765
gag gaa gaa gag gaa gat gtg act gat gaa gat tcc ctg gca ggg aga 2472
Glu Glu Glu Glu Glu Asp Val Thr Asp Glu Asp Ser Leu Ala Gly Arg
770 775 780
ggc tca gag agt gga ggt gag aag gca ata tca gtg aga ggt gat tca 2520
Gly Ser Glu Ser Gly Gly Glu Lys Ala Ile Ser Val Arg Gly Asp Ser
785 790 795 800
gaa gag gca tct ggg gca gag gag gag gtg ggg aca gtg gcg gca gca 2568
Glu Glu Ala Ser Gly Ala Glu Glu Glu Val Gly Thr Val Ala Ala Ala
805 810 815
gcc aca gct ggg aag gag atg gac agt aat gag aaa act act caa cag 2616
Ala Thr Ala Gly Lys Glu Met Asp Ser Asn Glu Lys Thr Thr Gln Gln
820 825 830
tct tct ttg cca cca cca cca cca cct gac agc ctg gat cag cct cag 2664
Ser Ser Leu Pro Pro Pro Pro Pro Pro Asp Ser Leu Asp Gln Pro Gln
835 840 845
cca atg gag cag gga agc agt ggt gtt tta gga ggc aag gaa gag ggg 2712
Pro Met Glu Gln Gly Ser Ser Gly Val Leu Gly Gly Lys Glu Glu Gly
850 855 860
ggc aaa ccg gag aga agc tca agt ccg gca tca gca ctc acc cca gaa 2760
Gly Lys Pro Glu Arg Ser Ser Ser Pro Ala Ser Ala Leu Thr Pro Glu
865 870 875 880
ggg gaa gcc acc agc gtg acc ttg gta gag gag ctg agc ctg cag gag 2808
Gly Glu Ala Thr Ser Val Thr Leu Val Glu Glu Leu Ser Leu Gln Glu
885 890 895
gca atg aga aag gag cca gga gag agc agc agc aga aag gcc tgc gaa 2856
Ala Met Arg Lys Glu Pro Gly Glu Ser Ser Ser Arg Lys Ala Cys Glu
900 905 910
gtg tgt ggc cag gcc ttt ccc tcc cag gca gct ctg gag gag cat cag 2904
Val Cys Gly Gln Ala Phe Pro Ser Gln Ala Ala Leu Glu Glu His Gln
915 920 925
aag acc cac ccc aag gag ggg ccg ctc ttc act tgt gtt ttc tgc agg 2952
Lys Thr His Pro Lys Glu Gly Pro Leu Phe Thr Cys Val Phe Cys Arg
930 935 940
cag ggc ttt ctt gag cgg gct acc ctc aag aag cat atg ctc ctg gca 3000
Gln Gly Phe Leu Glu Arg Ala Thr Leu Lys Lys His Met Leu Leu Ala
945 950 955 960
cac cac cag aac cag tat gtg gca ttc ctg tca aat ggc ctg ccc atg 3048
His His Gln Asn Gln Tyr Val Ala Phe Leu Ser Asn Gly Leu Pro Met
965 970 975
aag ccc tgg aat tcc agc tcc acc tcc act acc act cca agc ctg gcc 3096
Lys Pro Trp Asn Ser Ser Ser Thr Ser Thr Thr Thr Pro Ser Leu Ala
980 985 990
cca cca gtg ctg ttt ggc cta gga act gtg gct ggg aag gtg cct cca 3144
Pro Pro Val Leu Phe Gly Leu Gly Thr Val Ala Gly Lys Val Pro Pro
995 1000 1005
aca atg gga tcc agg gaa gcc aag gag aag aca gcc ccc ctc cta 3189
Thr Met Gly Ser Arg Glu Ala Lys Glu Lys Thr Ala Pro Leu Leu
1010 1015 1020
ttt cag cct cct gca ccc aag gca gtg cct gag aag ccc atc ata 3234
Phe Gln Pro Pro Ala Pro Lys Ala Val Pro Glu Lys Pro Ile Ile
1025 1030 1035
gac aag aag tag caaactgtac attccttctt cctccccctg ctccagaagg 3286
Asp Lys Lys
1040
tgccggtact gaagatgctc cagtaattgg tgacccaacc ctaggaagta gggagaaatg 3346
aaggaagggc ataggaaaat tttcccagta aatcccctga tggtcacatt aaggtaaagg 3406
ttttggctgg tcagtgtgcc aagacctctc cagcttctca ttcatgatga cctctcaaag 3466
ttgggaaaca agctgatttc ttgccaagag gtctcccagg agatatttgg gaaatgtgaa 3526
gttcgtatct ttaaggagca tttttggtca gcatggttga tgaactaatg atgagagagt 3586
taaggaatgt tgctagaaca tagggcttgc tggtacctat gtgactaaga aagggacatg 3646
atgtaaggga aaaggcctca aattcttgtg aatgtctgga cattctcgtt aatattcttt 3706
tgggctaata gtgacatagt gtgcagaggt gtaccaggga tcatggggga tttcctagca 3766
ctagtatgct tctagtttta gataactccc tcctttattc cctggcccct tgtattttcc 3826
ttatcttcct ctttcaagac ccctacccat tttgcctatc cgtaggctgg ggcttgtgtc 3886
tttgtcattg tctggttctt aagagtccca gactttggga gaccagctcc aggtggcgtc 3946
ctccctgcct ctccgtcttg taatgagttg tagtatttac tcttaacata ggatcatttg 4006
gaacaggagt tctgaggagg agagagtgag ggttttgcta ttgactgact tgaacgatgg 4066
cttctcctca agctgtaggc tccagagctt cctaacctag taaaatgtca agaacagacg 4126
ggagatatta gtgtctttcc ctctatcatt aaaggtgttt taaccaaaaa aaaaaaaaaa 4186
aaaaa 4191


14
1041
PRT
Homo sapiens

14
Met Ala His Glu Ser Glu Arg Ser Ser Arg Leu Gly Val Pro Cys Gly
1 5 10 15
Glu Pro Ala Glu Leu Gly Gly Asp Ala Ser Glu Glu Asp His Pro Gln
20 25 30
Val Cys Ala Lys Cys Cys Ala Gln Phe Thr Asp Pro Thr Glu Phe Leu
35 40 45
Ala His Gln Asn Ala Cys Ser Thr Asp Pro Pro Val Met Val Ile Ile
50 55 60
Gly Gly Gln Glu Asn Pro Asn Asn Ser Ser Ala Ser Ser Glu Pro Arg
65 70 75 80
Pro Glu Gly His Asn Asn Pro Gln Val Met Asp Thr Glu His Ser Asn
85 90 95
Pro Pro Asp Ser Gly Ser Ser Val Pro Thr Asp Pro Thr Trp Gly Pro
100 105 110
Glu Arg Arg Gly Glu Glu Ser Ser Gly His Phe Leu Val Ala Ala Thr
115 120 125
Gly Thr Ala Ala Gly Gly Gly Gly Gly Leu Ile Leu Ala Ser Pro Lys
130 135 140
Leu Gly Ala Thr Pro Leu Pro Pro Glu Ser Thr Pro Ala Pro Pro Pro
145 150 155 160
Pro Pro Pro Pro Pro Pro Pro Pro Gly Val Gly Ser Gly His Leu Asn
165 170 175
Ile Pro Leu Ile Leu Glu Glu Leu Arg Val Leu Gln Gln Arg Gln Ile
180 185 190
His Gln Met Gln Met Thr Glu Gln Ile Cys Arg Gln Val Leu Leu Leu
195 200 205
Gly Ser Leu Gly Gln Thr Val Gly Ala Pro Ala Ser Pro Ser Glu Leu
210 215 220
Pro Gly Thr Gly Thr Ala Ser Ser Thr Lys Pro Leu Leu Pro Leu Phe
225 230 235 240
Ser Pro Ile Lys Pro Val Gln Thr Ser Lys Thr Leu Ala Ser Ser Ser
245 250 255
Ser Ser Ser Ser Ser Ser Ser Gly Ala Glu Thr Pro Lys Gln Ala Phe
260 265 270
Phe His Leu Tyr His Pro Leu Gly Ser Gln His Pro Phe Ser Ala Gly
275 280 285
Gly Val Gly Arg Ser His Lys Pro Thr Pro Ala Pro Ser Pro Ala Leu
290 295 300
Pro Gly Ser Thr Asp Gln Leu Ile Ala Ser Pro His Leu Ala Phe Pro
305 310 315 320
Ser Thr Thr Gly Leu Leu Ala Ala Gln Cys Leu Gly Ala Ala Arg Gly
325 330 335
Leu Glu Ala Thr Ala Ser Pro Gly Leu Leu Lys Pro Lys Asn Gly Ser
340 345 350
Gly Glu Leu Ser Tyr Gly Glu Val Met Gly Pro Leu Glu Lys Pro Gly
355 360 365
Gly Arg His Lys Cys Arg Phe Cys Ala Lys Val Phe Gly Ser Asp Ser
370 375 380
Ala Leu Gln Ile His Leu Arg Ser His Thr Gly Glu Arg Pro Tyr Lys
385 390 395 400
Cys Asn Val Cys Gly Asn Arg Phe Thr Thr Arg Gly Asn Leu Lys Val
405 410 415
His Phe His Arg His Arg Glu Lys Tyr Pro His Val Gln Met Asn Pro
420 425 430
His Pro Val Pro Glu His Leu Asp Tyr Val Ile Thr Ser Ser Gly Leu
435 440 445
Pro Tyr Gly Met Ser Val Pro Pro Glu Lys Ala Glu Glu Glu Ala Ala
450 455 460
Thr Pro Gly Gly Gly Val Glu Arg Lys Pro Leu Val Ala Ser Thr Thr
465 470 475 480
Ala Leu Ser Ala Thr Glu Ser Leu Thr Leu Leu Ser Thr Ser Ala Gly
485 490 495
Thr Ala Thr Ala Pro Gly Leu Pro Ala Phe Asn Lys Phe Val Leu Met
500 505 510
Lys Ala Val Glu Pro Lys Asn Lys Ala Asp Glu Asn Thr Pro Pro Gly
515 520 525
Ser Glu Gly Ser Ala Ile Ser Gly Val Ala Glu Ser Ser Thr Ala Thr
530 535 540
Arg Met Gln Leu Ser Lys Leu Val Thr Ser Leu Pro Ser Trp Ala Leu
545 550 555 560
Leu Thr Asn His Phe Lys Ser Thr Gly Ser Phe Pro Phe Pro Tyr Val
565 570 575
Leu Glu Pro Leu Gly Ala Ser Pro Ser Glu Thr Ser Lys Leu Gln Gln
580 585 590
Leu Val Glu Lys Ile Asp Arg Gln Gly Ala Val Ala Val Thr Ser Ala
595 600 605
Ala Ser Gly Ala Pro Thr Thr Ser Ala Pro Ala Pro Ser Ser Ser Ala
610 615 620
Ser Ser Gly Pro Asn Gln Cys Val Ile Cys Leu Arg Val Leu Ser Cys
625 630 635 640
Pro Arg Ala Leu Arg Leu His Tyr Gly Gln His Gly Gly Glu Arg Pro
645 650 655
Phe Lys Cys Lys Val Cys Gly Arg Ala Phe Ser Thr Arg Gly Asn Leu
660 665 670
Arg Ala His Phe Val Gly His Lys Ala Ser Pro Ala Ala Arg Ala Gln
675 680 685
Asn Ser Cys Pro Ile Cys Gln Lys Lys Phe Thr Asn Ala Val Thr Leu
690 695 700
Gln Gln His Val Arg Met His Leu Gly Gly Gln Ile Pro Asn Gly Gly
705 710 715 720
Thr Ala Leu Pro Glu Gly Gly Gly Ala Ala Gln Glu Asn Gly Ser Glu
725 730 735
Gln Ser Thr Val Ser Gly Ala Gly Ser Phe Pro Gln Gln Gln Ser Gln
740 745 750
Gln Pro Ser Pro Glu Glu Glu Leu Ser Glu Glu Glu Glu Glu Glu Asp
755 760 765
Glu Glu Glu Glu Glu Asp Val Thr Asp Glu Asp Ser Leu Ala Gly Arg
770 775 780
Gly Ser Glu Ser Gly Gly Glu Lys Ala Ile Ser Val Arg Gly Asp Ser
785 790 795 800
Glu Glu Ala Ser Gly Ala Glu Glu Glu Val Gly Thr Val Ala Ala Ala
805 810 815
Ala Thr Ala Gly Lys Glu Met Asp Ser Asn Glu Lys Thr Thr Gln Gln
820 825 830
Ser Ser Leu Pro Pro Pro Pro Pro Pro Asp Ser Leu Asp Gln Pro Gln
835 840 845
Pro Met Glu Gln Gly Ser Ser Gly Val Leu Gly Gly Lys Glu Glu Gly
850 855 860
Gly Lys Pro Glu Arg Ser Ser Ser Pro Ala Ser Ala Leu Thr Pro Glu
865 870 875 880
Gly Glu Ala Thr Ser Val Thr Leu Val Glu Glu Leu Ser Leu Gln Glu
885 890 895
Ala Met Arg Lys Glu Pro Gly Glu Ser Ser Ser Arg Lys Ala Cys Glu
900 905 910
Val Cys Gly Gln Ala Phe Pro Ser Gln Ala Ala Leu Glu Glu His Gln
915 920 925
Lys Thr His Pro Lys Glu Gly Pro Leu Phe Thr Cys Val Phe Cys Arg
930 935 940
Gln Gly Phe Leu Glu Arg Ala Thr Leu Lys Lys His Met Leu Leu Ala
945 950 955 960
His His Gln Asn Gln Tyr Val Ala Phe Leu Ser Asn Gly Leu Pro Met
965 970 975
Lys Pro Trp Asn Ser Ser Ser Thr Ser Thr Thr Thr Pro Ser Leu Ala
980 985 990
Pro Pro Val Leu Phe Gly Leu Gly Thr Val Ala Gly Lys Val Pro Pro
995 1000 1005
Thr Met Gly Ser Arg Glu Ala Lys Glu Lys Thr Ala Pro Leu Leu
1010 1015 1020
Phe Gln Pro Pro Ala Pro Lys Ala Val Pro Glu Lys Pro Ile Ile
1025 1030 1035
Asp Lys Lys
1040


15
3138
DNA
Homo sapiens

CDS
(182)..(913)


15
cctcgctctc cttccatctc tctcgccccc tctccctccg tcccgtcctc gccgctcccc 60
tcaccccgcc tctctccccc tcccccagcc cctcctctcc tcaccccacc cggcctccct 120
ccctccctcg cccgcccggc gctcgcagaa ccgacaccag gggggctctc gatgtagcac 180
c atg aca ggc atc gcc gcc gcc tcc ttc ttc tcc aat acc tgc cga ttc 229
Met Thr Gly Ile Ala Ala Ala Ser Phe Phe Ser Asn Thr Cys Arg Phe
1 5 10 15
ggg ggc tgc gga ctc cac ttc ccc acc ctg gcc gac ctc atc gag cac 277
Gly Gly Cys Gly Leu His Phe Pro Thr Leu Ala Asp Leu Ile Glu His
20 25 30
atc gag gac aac cac atc gat aca gat cca cgg gtt tta gaa aaa caa 325
Ile Glu Asp Asn His Ile Asp Thr Asp Pro Arg Val Leu Glu Lys Gln
35 40 45
gaa tta cag cag cca acc tat gtt gcc ctg agt tac ata aat aga ttc 373
Glu Leu Gln Gln Pro Thr Tyr Val Ala Leu Ser Tyr Ile Asn Arg Phe
50 55 60
atg aca gat gct gcc cgc cga gag cag gag tcc cta aag aag aag att 421
Met Thr Asp Ala Ala Arg Arg Glu Gln Glu Ser Leu Lys Lys Lys Ile
65 70 75 80
cag ccg aag ctc tcg ctg act ctg tcc agc tca gtg tct cga ggg aat 469
Gln Pro Lys Leu Ser Leu Thr Leu Ser Ser Ser Val Ser Arg Gly Asn
85 90 95
gtg tcc act ccc cca cgc cac agc agt gga agc ctt act ccc ccc gtg 517
Val Ser Thr Pro Pro Arg His Ser Ser Gly Ser Leu Thr Pro Pro Val
100 105 110
acc cca ccc atc acc ccc tcc tct tca ttc cgc agc agc act ccg aca 565
Thr Pro Pro Ile Thr Pro Ser Ser Ser Phe Arg Ser Ser Thr Pro Thr
115 120 125
ggc agc gag tat gac gag gag gag gtg gac tat gag gag tcg gac agc 613
Gly Ser Glu Tyr Asp Glu Glu Glu Val Asp Tyr Glu Glu Ser Asp Ser
130 135 140
gat gag tcc tgg acc aca gag agt gcc atc agc tcc gaa gcc atc ctc 661
Asp Glu Ser Trp Thr Thr Glu Ser Ala Ile Ser Ser Glu Ala Ile Leu
145 150 155 160
agc tcc atg tgc atg aat gga ggg gaa gag aag cct ttt gcc tgc cca 709
Ser Ser Met Cys Met Asn Gly Gly Glu Glu Lys Pro Phe Ala Cys Pro
165 170 175
gtt cct gga tgt aaa aag aga tac aag aat gtg aat ggc ata aag tat 757
Val Pro Gly Cys Lys Lys Arg Tyr Lys Asn Val Asn Gly Ile Lys Tyr
180 185 190
cac gct aag aat ggt cac aga aca cag att cgt gtc cgc aaa cca ttc 805
His Ala Lys Asn Gly His Arg Thr Gln Ile Arg Val Arg Lys Pro Phe
195 200 205
aag tgt cgc tgt ggg aag agt tac aag aca gct cag ggc ctg cgg cac 853
Lys Cys Arg Cys Gly Lys Ser Tyr Lys Thr Ala Gln Gly Leu Arg His
210 215 220
cac aca atc aat ttc cat ccc ccg gtg tcg gct gag att atc agg aag 901
His Thr Ile Asn Phe His Pro Pro Val Ser Ala Glu Ile Ile Arg Lys
225 230 235 240
atg cag caa taa catgctggtc ataactgtgc caagaaatcc tcaccagcag 953
Met Gln Gln
ttgctgattt tgaaaacagc cacctttttt caggggaagc attcagcaac cctttaaaga 1013
aaaagaatta aatgcatgct ttaaattttt tctgtaattt tggaatgatg tatctttgta 1073
gagttaatga ttttgtacat ttgcacatgt aatcatcata cccattttca ttactttgat 1133
ataaggtgct aaacaaaaaa agctctaggt tcttcagcac atttccccca aaacaaaata 1193
aaattgaggg catgttgcat attgttgaat tgtattgcgg tggtatcaac ctggggggag 1253
gaggggctgg cactgagatt tttttttcaa gattgtaatg tgattgaagt tttcaacaca 1313
tcaactcaca tatgttcaaa accaaaataa taccttcatt atcaaactgg ttaccatgcc 1373
ttacataatg gagttagtat ttgtgagtag aaagacttta ggtaatggaa atataaataa 1433
gaaagaatgt ttaacataat atgctaaaaa tattttcata tttaaataac atacgtaaag 1493
gtgtgctttc tgtgttttat attatcttgc aaatcctttt gccctttaaa aagctgaaaa 1553
tcttgccatc tgacttacta gtcattttag tgttataaat ggcattttgt acaaaatagt 1613
ctattcagtt cgttcattca tttaacacac attgattgag tgcctgctgg gtacaaggga 1673
ttcaatttat gcctattgat atctgcggac caagataccc ayttagtgaa atactttttt 1733
ccctgaaatc tgttagaaaa gactttgaaa tacttcagtg caaagtgtgt gtgtgtgaag 1793
tttagttata tcttcatctt cagatgaagt tttaaagcac tttgtagttc tctattgcca 1853
acaatttaat gtttatgtgt tgccaattct tgcaaccact gccctaccaa acctgtgggt 1913
tgcaaatcag aactaaaatt ctaagcacgt ttcaaagatg aacacttttg ttaagacccc 1973
tattgcctct tcttcatgct cattttttac tttttttaaa aggtactttt ctcatcacat 2033
tgtagagagg tctgcattct cattggaaat gtctgtttag ctttataaaa caaacacttt 2093
gctgaaatag gaaaatgagc cttattgaca attaagtgct tcttgcagca ggtggtcaaa 2153
gaaaagcatg actaatacga cctattagag taatctacat ctggaccatt ccttaagttt 2213
ttcctcaccg acagtaccat catgccttga gtgttctttt ctcccaagtg ctattcctta 2273
aacacgagag tttaccagtt gcctaataat gcaataaaaa atgctttgag atagctaact 2333
gcccataaaa caaactcaaa ttgcttataa agtttcttcc catgttccca tttgatgaaa 2393
agtcttacat cacatataac tgggaagcag gggtccctcc tcaattttca gacattttga 2453
aaggatgaca gttctgtttg ttagatgagt aaacctctat attcataagt tctaaaatcc 2513
ttcattatga gggattcaaa gtatttataa aaacactgcc ctctaaaaat ttcctcagat 2573
ctgaagtatg gtcttggtcc tgaatataca gtgttatcct atgtttaaaa gggtgatcca 2633
gacatgagac gcaactagtt ggtgcataag aaggccccac ttggctattt catatctacc 2693
tacaattgac caaaaaaaat tttttaggcc agcaattatt atttagcttc gctctttcta 2753
gtgcaagaaa ctgcaggctg gatcagtagt tcaacagcta aacagtcata aaatagtcat 2813
tgtgcatgtt aaatttcttt cratgctttc aaagataaat tccaatttct atttacttat 2873
tcattgtgac agtattacta aacaggtaag gatgggaata ttttgttata ctgtgtatag 2933
tgaatgtatt gtactgtgtc tgtgaaaact gtgctttaaa ttatattttc atatgttttg 2993
ttggggacag agcacattaa gtctgaaagc aacagaggtt tgttttagaa ctgaaggcaa 3053
tttaatcaaa attcctgtca agaaaagctg cttataaatg taaatgaaat cacatttaaa 3113
ataaactgcc tctgacccaa aaaaa 3138


16
243
PRT
Homo sapiens

16
Met Thr Gly Ile Ala Ala Ala Ser Phe Phe Ser Asn Thr Cys Arg Phe
1 5 10 15
Gly Gly Cys Gly Leu His Phe Pro Thr Leu Ala Asp Leu Ile Glu His
20 25 30
Ile Glu Asp Asn His Ile Asp Thr Asp Pro Arg Val Leu Glu Lys Gln
35 40 45
Glu Leu Gln Gln Pro Thr Tyr Val Ala Leu Ser Tyr Ile Asn Arg Phe
50 55 60
Met Thr Asp Ala Ala Arg Arg Glu Gln Glu Ser Leu Lys Lys Lys Ile
65 70 75 80
Gln Pro Lys Leu Ser Leu Thr Leu Ser Ser Ser Val Ser Arg Gly Asn
85 90 95
Val Ser Thr Pro Pro Arg His Ser Ser Gly Ser Leu Thr Pro Pro Val
100 105 110
Thr Pro Pro Ile Thr Pro Ser Ser Ser Phe Arg Ser Ser Thr Pro Thr
115 120 125
Gly Ser Glu Tyr Asp Glu Glu Glu Val Asp Tyr Glu Glu Ser Asp Ser
130 135 140
Asp Glu Ser Trp Thr Thr Glu Ser Ala Ile Ser Ser Glu Ala Ile Leu
145 150 155 160
Ser Ser Met Cys Met Asn Gly Gly Glu Glu Lys Pro Phe Ala Cys Pro
165 170 175
Val Pro Gly Cys Lys Lys Arg Tyr Lys Asn Val Asn Gly Ile Lys Tyr
180 185 190
His Ala Lys Asn Gly His Arg Thr Gln Ile Arg Val Arg Lys Pro Phe
195 200 205
Lys Cys Arg Cys Gly Lys Ser Tyr Lys Thr Ala Gln Gly Leu Arg His
210 215 220
His Thr Ile Asn Phe His Pro Pro Val Ser Ala Glu Ile Ile Arg Lys
225 230 235 240
Met Gln Gln


17
3387
DNA
Homo sapiens

CDS
(8)..(2377)


17
agcgggc atg gcc tgc cgg gag ggg gca ggt agc cgg cgg gcc cgg tcc 49
Met Ala Cys Arg Glu Gly Ala Gly Ser Arg Arg Ala Arg Ser
1 5 10
aat ggg tgc cgg ctt ccg agg aga ggg cgg agg aga gga gga agg agg 97
Asn Gly Cys Arg Leu Pro Arg Arg Gly Arg Arg Arg Gly Gly Arg Arg
15 20 25 30
cga act gtg ggc ccc ggc ccc att cat tgc cgt ggc cgg cgg gca ctg 145
Arg Thr Val Gly Pro Gly Pro Ile His Cys Arg Gly Arg Arg Ala Leu
35 40 45
ggg ccc cgt gtt ttc aga gtc atg gag gcg cta att cct gtc ata aac 193
Gly Pro Arg Val Phe Arg Val Met Glu Ala Leu Ile Pro Val Ile Asn
50 55 60
aag ctc cag gac gtc ttc aac acg gtg ggc gcc gac atc atc cag ctg 241
Lys Leu Gln Asp Val Phe Asn Thr Val Gly Ala Asp Ile Ile Gln Leu
65 70 75
cct caa atc gtc gta gtg gga acg cag agc agc gga aag agc tca gtg 289
Pro Gln Ile Val Val Val Gly Thr Gln Ser Ser Gly Lys Ser Ser Val
80 85 90
cta gaa agc ctg gtg ggg agg gac ctg ctt ccc aga ggt act gga att 337
Leu Glu Ser Leu Val Gly Arg Asp Leu Leu Pro Arg Gly Thr Gly Ile
95 100 105 110
gtc acc cgg aga cct ctc att ctg caa ctg gtc cat gtg aca caa gaa 385
Val Thr Arg Arg Pro Leu Ile Leu Gln Leu Val His Val Thr Gln Glu
115 120 125
gat aaa cgg aaa aca aca gga gaa gaa aat ggg gtg gaa gca gaa gaa 433
Asp Lys Arg Lys Thr Thr Gly Glu Glu Asn Gly Val Glu Ala Glu Glu
130 135 140
tgg ggt aaa ttt ctt cac acc aaa aat aag ctt tac acg gat ttt gat 481
Trp Gly Lys Phe Leu His Thr Lys Asn Lys Leu Tyr Thr Asp Phe Asp
145 150 155
gaa att cga caa gaa att gaa aat gaa aca gaa aga att tca gga aat 529
Glu Ile Arg Gln Glu Ile Glu Asn Glu Thr Glu Arg Ile Ser Gly Asn
160 165 170
aat aag gga gta agc cct gaa cca att cat ctt aag att ttt tca ccc 577
Asn Lys Gly Val Ser Pro Glu Pro Ile His Leu Lys Ile Phe Ser Pro
175 180 185 190
aac gtt gtc aat ttg aca ctt gtg gat ttg cca gga atg acc aag gtg 625
Asn Val Val Asn Leu Thr Leu Val Asp Leu Pro Gly Met Thr Lys Val
195 200 205
cct gta ggt gat caa cct aag gat att gag ctt caa atc aga gag ctc 673
Pro Val Gly Asp Gln Pro Lys Asp Ile Glu Leu Gln Ile Arg Glu Leu
210 215 220
att ctt cgg ttc atc agt aat cct aat tcc att atc ctc gct gtc act 721
Ile Leu Arg Phe Ile Ser Asn Pro Asn Ser Ile Ile Leu Ala Val Thr
225 230 235
gct gct aat aca gat atg gca aca tca gag gca ctt aaa att tca aga 769
Ala Ala Asn Thr Asp Met Ala Thr Ser Glu Ala Leu Lys Ile Ser Arg
240 245 250
gag gta gat cca gat ggt cgc aga acc cta gct gta atc act aaa ctt 817
Glu Val Asp Pro Asp Gly Arg Arg Thr Leu Ala Val Ile Thr Lys Leu
255 260 265 270
gat ctc atg gat gcg ggt act gat gcc atg gat gta ttg atg gga agg 865
Asp Leu Met Asp Ala Gly Thr Asp Ala Met Asp Val Leu Met Gly Arg
275 280 285
gtt att cca gtc aaa ctt gga ata att gga gta gtt aac agg agc cag 913
Val Ile Pro Val Lys Leu Gly Ile Ile Gly Val Val Asn Arg Ser Gln
290 295 300
cta gat att aac aac aag aag agt gta act gat tca atc cgt gat gag 961
Leu Asp Ile Asn Asn Lys Lys Ser Val Thr Asp Ser Ile Arg Asp Glu
305 310 315
tat gct ttt ctt caa aag aaa tat cca tct ctg gcc aat aga aat gga 1009
Tyr Ala Phe Leu Gln Lys Lys Tyr Pro Ser Leu Ala Asn Arg Asn Gly
320 325 330
aca aag tat ctt gct agg act cta aac agg tta ctg atg cat cac atc 1057
Thr Lys Tyr Leu Ala Arg Thr Leu Asn Arg Leu Leu Met His His Ile
335 340 345 350
aga gat tgt tta cca gag ttg aaa aca aga ata aat gtt cta gct gct 1105
Arg Asp Cys Leu Pro Glu Leu Lys Thr Arg Ile Asn Val Leu Ala Ala
355 360 365
cag tat cag tct ctt cta aat agc tac ggt gaa ccc gtg gat gat aaa 1153
Gln Tyr Gln Ser Leu Leu Asn Ser Tyr Gly Glu Pro Val Asp Asp Lys
370 375 380
agt gct act tta ctc caa ctt att acc aaa ttt gcc aca gaa tat tgt 1201
Ser Ala Thr Leu Leu Gln Leu Ile Thr Lys Phe Ala Thr Glu Tyr Cys
385 390 395
aac act att gaa gga act gca aaa tat att gaa act tcg gag cta tgc 1249
Asn Thr Ile Glu Gly Thr Ala Lys Tyr Ile Glu Thr Ser Glu Leu Cys
400 405 410
ggt ggt gct aga att tgt tat att ttc cat gag act ttt ggg cga acc 1297
Gly Gly Ala Arg Ile Cys Tyr Ile Phe His Glu Thr Phe Gly Arg Thr
415 420 425 430
tta gaa tct gtt gat cca ctt ggt ggc ctt aac act att gac att ttg 1345
Leu Glu Ser Val Asp Pro Leu Gly Gly Leu Asn Thr Ile Asp Ile Leu
435 440 445
act gcc att aga aat gct act ggt cct cgt cct gct tta ttt gtg cct 1393
Thr Ala Ile Arg Asn Ala Thr Gly Pro Arg Pro Ala Leu Phe Val Pro
450 455 460
gag gtt tca ttt gag tta ctg gtg aag cgg caa atc aaa cgt cta gaa 1441
Glu Val Ser Phe Glu Leu Leu Val Lys Arg Gln Ile Lys Arg Leu Glu
465 470 475
gag ccc agc ctc cgc tgt gtg gaa ctg gtt cat gag gaa atg caa agg 1489
Glu Pro Ser Leu Arg Cys Val Glu Leu Val His Glu Glu Met Gln Arg
480 485 490
atc att cag cac tgt agc aat tac agt aca cag gaa ttg tta cga ttt 1537
Ile Ile Gln His Cys Ser Asn Tyr Ser Thr Gln Glu Leu Leu Arg Phe
495 500 505 510
cct aaa ctt cat gat gcc ata gtt gaa gtg gtg act tgt ctt ctt cgt 1585
Pro Lys Leu His Asp Ala Ile Val Glu Val Val Thr Cys Leu Leu Arg
515 520 525
aaa agg ttg cct gtt aca aat gaa atg gtc cat aac tta gtg gca att 1633
Lys Arg Leu Pro Val Thr Asn Glu Met Val His Asn Leu Val Ala Ile
530 535 540
gaa ctg gct tat atc aac aca aaa cat cca gac ttt gct gat gct tgt 1681
Glu Leu Ala Tyr Ile Asn Thr Lys His Pro Asp Phe Ala Asp Ala Cys
545 550 555
ggg cta atg aac aat aat ata gag gaa caa agg aga aac agg cta gcc 1729
Gly Leu Met Asn Asn Asn Ile Glu Glu Gln Arg Arg Asn Arg Leu Ala
560 565 570
aga gaa tta cct tca gct gta tca cga gac aag tct tct aaa gtt cca 1777
Arg Glu Leu Pro Ser Ala Val Ser Arg Asp Lys Ser Ser Lys Val Pro
575 580 585 590
agt gct ttg gca cct gcc tcc cag gag ccc tcc ccc gct gct tct gct 1825
Ser Ala Leu Ala Pro Ala Ser Gln Glu Pro Ser Pro Ala Ala Ser Ala
595 600 605
gag gct gat ggc aag tta att cag gac agc aga aga gaa act aaa aat 1873
Glu Ala Asp Gly Lys Leu Ile Gln Asp Ser Arg Arg Glu Thr Lys Asn
610 615 620
gtt gca tct gga ggt ggt ggg gtt gga gat ggt gtt caa gaa cca acc 1921
Val Ala Ser Gly Gly Gly Gly Val Gly Asp Gly Val Gln Glu Pro Thr
625 630 635
aca ggc aac tgg aga gga atg ctg aaa act tca aaa gct gaa gag tta 1969
Thr Gly Asn Trp Arg Gly Met Leu Lys Thr Ser Lys Ala Glu Glu Leu
640 645 650
tta gca gaa gaa aaa tca aaa ccc att cca att atg cca gcc agt cca 2017
Leu Ala Glu Glu Lys Ser Lys Pro Ile Pro Ile Met Pro Ala Ser Pro
655 660 665 670
caa aaa ggt cat gcc gtg aac ctg cta gat gtg cca gtt cct gtt gca 2065
Gln Lys Gly His Ala Val Asn Leu Leu Asp Val Pro Val Pro Val Ala
675 680 685
cga aaa cta tct gct cgg gaa cag cga gat tgt gag gtt att gaa cga 2113
Arg Lys Leu Ser Ala Arg Glu Gln Arg Asp Cys Glu Val Ile Glu Arg
690 695 700
ctc att aaa tca tat ttt ctc att gtc aga aag aat att caa gac agt 2161
Leu Ile Lys Ser Tyr Phe Leu Ile Val Arg Lys Asn Ile Gln Asp Ser
705 710 715
gtg cca aag gca gta atg cat ttt ttg gtt aat cat gtg aaa gac act 2209
Val Pro Lys Ala Val Met His Phe Leu Val Asn His Val Lys Asp Thr
720 725 730
ctt cag agt gag cta gta ggc cag ctg tat aaa tca tcc tta ttg gat 2257
Leu Gln Ser Glu Leu Val Gly Gln Leu Tyr Lys Ser Ser Leu Leu Asp
735 740 745 750
gat ctt ctg aca gaa tct gag gac atg gca cag cgc agg aaa gaa gca 2305
Asp Leu Leu Thr Glu Ser Glu Asp Met Ala Gln Arg Arg Lys Glu Ala
755 760 765
gct gat atg cta aag gca tta caa gga gcc agt caa att att gct gaa 2353
Ala Asp Met Leu Lys Ala Leu Gln Gly Ala Ser Gln Ile Ile Ala Glu
770 775 780
atc cgg gag act cat ctt tgg tga agagaactat gtaatactga gactttgttg 2407
Ile Arg Glu Thr His Leu Trp
785
actcaaaact tgctagttac tgcctacctg agtagaatct tatttatgaa ctcctgtgta 2467
ttgcaatggt atgaatctgc tcatgtggag actggctata aactgaaaag tgtattccaa 2527
attgcagaac acatcacaca tttaatccaa ataataaatg gctgtttcta aagtttccca 2587
gtatatataa aatacatcaa gtctgtcttg tgacagtttc atctgaactt aacttaaaaa 2647
caactgttaa tgttctagtt gtgcaaagca gtttgcctgt ggataagatg acctgtgtaa 2707
taatctttgt tagtagtctt aaagctgctg ccatagtcct ccaagaagaa agcaccaaga 2767
caacatttca tatgactata atgcatgtac tatataagct gatctggctt tgaaagatgt 2827
gagttggcaa gttcctcaca tagagtcatt gtattccacc tgtccttcaa tttagttttt 2887
tctgagcttc tttgcagcct ttgatgtgtt tttaagaaag ctgaatgcac aagaggatct 2947
gtgacactga catggctgtg gtgtgcatac tgtgtagtta catagccctt ccaattctgg 3007
gtccatttgc actagcaaat taaaatatgc tttgattcat acttaaacct gaaagcagga 3067
atgcctacat taattcctac attaaaaaca gccatctacc cttgattatc tagaaagact 3127
tggtaatgat ggtcagttcc ttttagattt cagaaaatca aatgatgacc taaatttccc 3187
ttaatttgca aatacagtag taattaaggt acatctctaa agtggagcac ttacaccagg 3247
ctctaagatt cactttgagg tggaacttaa aaccagtgta ctgtatgtat gcattggtaa 3307
tagctacttt tgcttcatag cttcatacca acaaaatata tttattagaa tagtatgaaa 3367
gtactgaagg agttgaaaga 3387


18
789
PRT
Homo sapiens

18
Met Ala Cys Arg Glu Gly Ala Gly Ser Arg Arg Ala Arg Ser Asn Gly
1 5 10 15
Cys Arg Leu Pro Arg Arg Gly Arg Arg Arg Gly Gly Arg Arg Arg Thr
20 25 30
Val Gly Pro Gly Pro Ile His Cys Arg Gly Arg Arg Ala Leu Gly Pro
35 40 45
Arg Val Phe Arg Val Met Glu Ala Leu Ile Pro Val Ile Asn Lys Leu
50 55 60
Gln Asp Val Phe Asn Thr Val Gly Ala Asp Ile Ile Gln Leu Pro Gln
65 70 75 80
Ile Val Val Val Gly Thr Gln Ser Ser Gly Lys Ser Ser Val Leu Glu
85 90 95
Ser Leu Val Gly Arg Asp Leu Leu Pro Arg Gly Thr Gly Ile Val Thr
100 105 110
Arg Arg Pro Leu Ile Leu Gln Leu Val His Val Thr Gln Glu Asp Lys
115 120 125
Arg Lys Thr Thr Gly Glu Glu Asn Gly Val Glu Ala Glu Glu Trp Gly
130 135 140
Lys Phe Leu His Thr Lys Asn Lys Leu Tyr Thr Asp Phe Asp Glu Ile
145 150 155 160
Arg Gln Glu Ile Glu Asn Glu Thr Glu Arg Ile Ser Gly Asn Asn Lys
165 170 175
Gly Val Ser Pro Glu Pro Ile His Leu Lys Ile Phe Ser Pro Asn Val
180 185 190
Val Asn Leu Thr Leu Val Asp Leu Pro Gly Met Thr Lys Val Pro Val
195 200 205
Gly Asp Gln Pro Lys Asp Ile Glu Leu Gln Ile Arg Glu Leu Ile Leu
210 215 220
Arg Phe Ile Ser Asn Pro Asn Ser Ile Ile Leu Ala Val Thr Ala Ala
225 230 235 240
Asn Thr Asp Met Ala Thr Ser Glu Ala Leu Lys Ile Ser Arg Glu Val
245 250 255
Asp Pro Asp Gly Arg Arg Thr Leu Ala Val Ile Thr Lys Leu Asp Leu
260 265 270
Met Asp Ala Gly Thr Asp Ala Met Asp Val Leu Met Gly Arg Val Ile
275 280 285
Pro Val Lys Leu Gly Ile Ile Gly Val Val Asn Arg Ser Gln Leu Asp
290 295 300
Ile Asn Asn Lys Lys Ser Val Thr Asp Ser Ile Arg Asp Glu Tyr Ala
305 310 315 320
Phe Leu Gln Lys Lys Tyr Pro Ser Leu Ala Asn Arg Asn Gly Thr Lys
325 330 335
Tyr Leu Ala Arg Thr Leu Asn Arg Leu Leu Met His His Ile Arg Asp
340 345 350
Cys Leu Pro Glu Leu Lys Thr Arg Ile Asn Val Leu Ala Ala Gln Tyr
355 360 365
Gln Ser Leu Leu Asn Ser Tyr Gly Glu Pro Val Asp Asp Lys Ser Ala
370 375 380
Thr Leu Leu Gln Leu Ile Thr Lys Phe Ala Thr Glu Tyr Cys Asn Thr
385 390 395 400
Ile Glu Gly Thr Ala Lys Tyr Ile Glu Thr Ser Glu Leu Cys Gly Gly
405 410 415
Ala Arg Ile Cys Tyr Ile Phe His Glu Thr Phe Gly Arg Thr Leu Glu
420 425 430
Ser Val Asp Pro Leu Gly Gly Leu Asn Thr Ile Asp Ile Leu Thr Ala
435 440 445
Ile Arg Asn Ala Thr Gly Pro Arg Pro Ala Leu Phe Val Pro Glu Val
450 455 460
Ser Phe Glu Leu Leu Val Lys Arg Gln Ile Lys Arg Leu Glu Glu Pro
465 470 475 480
Ser Leu Arg Cys Val Glu Leu Val His Glu Glu Met Gln Arg Ile Ile
485 490 495
Gln His Cys Ser Asn Tyr Ser Thr Gln Glu Leu Leu Arg Phe Pro Lys
500 505 510
Leu His Asp Ala Ile Val Glu Val Val Thr Cys Leu Leu Arg Lys Arg
515 520 525
Leu Pro Val Thr Asn Glu Met Val His Asn Leu Val Ala Ile Glu Leu
530 535 540
Ala Tyr Ile Asn Thr Lys His Pro Asp Phe Ala Asp Ala Cys Gly Leu
545 550 555 560
Met Asn Asn Asn Ile Glu Glu Gln Arg Arg Asn Arg Leu Ala Arg Glu
565 570 575
Leu Pro Ser Ala Val Ser Arg Asp Lys Ser Ser Lys Val Pro Ser Ala
580 585 590
Leu Ala Pro Ala Ser Gln Glu Pro Ser Pro Ala Ala Ser Ala Glu Ala
595 600 605
Asp Gly Lys Leu Ile Gln Asp Ser Arg Arg Glu Thr Lys Asn Val Ala
610 615 620
Ser Gly Gly Gly Gly Val Gly Asp Gly Val Gln Glu Pro Thr Thr Gly
625 630 635 640
Asn Trp Arg Gly Met Leu Lys Thr Ser Lys Ala Glu Glu Leu Leu Ala
645 650 655
Glu Glu Lys Ser Lys Pro Ile Pro Ile Met Pro Ala Ser Pro Gln Lys
660 665 670
Gly His Ala Val Asn Leu Leu Asp Val Pro Val Pro Val Ala Arg Lys
675 680 685
Leu Ser Ala Arg Glu Gln Arg Asp Cys Glu Val Ile Glu Arg Leu Ile
690 695 700
Lys Ser Tyr Phe Leu Ile Val Arg Lys Asn Ile Gln Asp Ser Val Pro
705 710 715 720
Lys Ala Val Met His Phe Leu Val Asn His Val Lys Asp Thr Leu Gln
725 730 735
Ser Glu Leu Val Gly Gln Leu Tyr Lys Ser Ser Leu Leu Asp Asp Leu
740 745 750
Leu Thr Glu Ser Glu Asp Met Ala Gln Arg Arg Lys Glu Ala Ala Asp
755 760 765
Met Leu Lys Ala Leu Gln Gly Ala Ser Gln Ile Ile Ala Glu Ile Arg
770 775 780
Glu Thr His Leu Trp
785


19
2509
DNA
Homo sapiens

CDS
(8)..(2299)


19
agcgggc atg gcc tgc cgg gag ggg gca ggt agc cgg cgg gcc cgg tcc 49
Met Ala Cys Arg Glu Gly Ala Gly Ser Arg Arg Ala Arg Ser
1 5 10
aat ggg tgc cgg ctt ccg agg aga ggg cgg agg aga gga gga agg agg 97
Asn Gly Cys Arg Leu Pro Arg Arg Gly Arg Arg Arg Gly Gly Arg Arg
15 20 25 30
cga act gtg ggc ccc ggc ccc att cat tgc cgt ggc cgg cgg gca ctg 145
Arg Thr Val Gly Pro Gly Pro Ile His Cys Arg Gly Arg Arg Ala Leu
35 40 45
ggg ccc cgt gtt ttc aga gtc atg gag gcg cta att cct gtc ata aac 193
Gly Pro Arg Val Phe Arg Val Met Glu Ala Leu Ile Pro Val Ile Asn
50 55 60
aag ctc cag gac gtc ttc aac acg gtg ggc gcc gac atc atc cag ctg 241
Lys Leu Gln Asp Val Phe Asn Thr Val Gly Ala Asp Ile Ile Gln Leu
65 70 75
cct caa atc gtc gta gtg gga acg cag agc agc gga aag agc tca gtg 289
Pro Gln Ile Val Val Val Gly Thr Gln Ser Ser Gly Lys Ser Ser Val
80 85 90
cta gaa agc ctg gtg ggg agg gac ctg ctt ccc aga ggt act gga att 337
Leu Glu Ser Leu Val Gly Arg Asp Leu Leu Pro Arg Gly Thr Gly Ile
95 100 105 110
gtc acc cgg aga cct ctc att ctg caa ctg gtc cat gtg aca caa gaa 385
Val Thr Arg Arg Pro Leu Ile Leu Gln Leu Val His Val Thr Gln Glu
115 120 125
gat aaa cgg aaa aca aca gga gaa gaa aat ggg gtg gaa gca gaa gaa 433
Asp Lys Arg Lys Thr Thr Gly Glu Glu Asn Gly Val Glu Ala Glu Glu
130 135 140
tgg ggt aaa ttt ctt cac acc aaa aat aag ctt tac acg gat ttt gat 481
Trp Gly Lys Phe Leu His Thr Lys Asn Lys Leu Tyr Thr Asp Phe Asp
145 150 155
gaa att cga caa gaa att gaa aat gaa aca gaa aga att tca gga aat 529
Glu Ile Arg Gln Glu Ile Glu Asn Glu Thr Glu Arg Ile Ser Gly Asn
160 165 170
aat aag gga gta agc cct gaa cca att cat ctt aag att ttt tca ccc 577
Asn Lys Gly Val Ser Pro Glu Pro Ile His Leu Lys Ile Phe Ser Pro
175 180 185 190
aac gtt gtc aat ttg aca ctt gtg gat ttg cca gga atg acc aag gtg 625
Asn Val Val Asn Leu Thr Leu Val Asp Leu Pro Gly Met Thr Lys Val
195 200 205
cct gta ggt gat caa cct aag gat att gag ctt caa atc aga gag ctc 673
Pro Val Gly Asp Gln Pro Lys Asp Ile Glu Leu Gln Ile Arg Glu Leu
210 215 220
att ctt cgg ttc atc agt aat cct aat tcc att atc ctc gct gtc act 721
Ile Leu Arg Phe Ile Ser Asn Pro Asn Ser Ile Ile Leu Ala Val Thr
225 230 235
gct gct aat aca gat atg gca aca tca gag gca ctt aaa att tca aga 769
Ala Ala Asn Thr Asp Met Ala Thr Ser Glu Ala Leu Lys Ile Ser Arg
240 245 250
gag gta gat cca gat ggt cgc aga acc cta gct gta atc act aaa ctt 817
Glu Val Asp Pro Asp Gly Arg Arg Thr Leu Ala Val Ile Thr Lys Leu
255 260 265 270
gat ctc atg gat gcg ggt act gat gcc atg gat gta ttg atg gga agg 865
Asp Leu Met Asp Ala Gly Thr Asp Ala Met Asp Val Leu Met Gly Arg
275 280 285
gtt att cca gtc aaa ctt gga ata att gga gta gtt aac agg agc cag 913
Val Ile Pro Val Lys Leu Gly Ile Ile Gly Val Val Asn Arg Ser Gln
290 295 300
cta gat att aac aac aag aag agt gta act gat tca atc cgt gat gag 961
Leu Asp Ile Asn Asn Lys Lys Ser Val Thr Asp Ser Ile Arg Asp Glu
305 310 315
tat gct ttt ctt caa aag aaa tat cca tct ctg gcc aat aga aat gga 1009
Tyr Ala Phe Leu Gln Lys Lys Tyr Pro Ser Leu Ala Asn Arg Asn Gly
320 325 330
aca aag tat ctt gct agg act cta aac agg tta ctg atg cat cac atc 1057
Thr Lys Tyr Leu Ala Arg Thr Leu Asn Arg Leu Leu Met His His Ile
335 340 345 350
aga gat tgt tta cca gag ttg aaa aca aga ata aat gtt cta gct gct 1105
Arg Asp Cys Leu Pro Glu Leu Lys Thr Arg Ile Asn Val Leu Ala Ala
355 360 365
cag tat cag tct ctt cta aat agc tac ggt gaa ccc gtg gat gat aaa 1153
Gln Tyr Gln Ser Leu Leu Asn Ser Tyr Gly Glu Pro Val Asp Asp Lys
370 375 380
agt gct act tta ctc caa ctt att acc aaa ttt gcc aca gaa tat tgt 1201
Ser Ala Thr Leu Leu Gln Leu Ile Thr Lys Phe Ala Thr Glu Tyr Cys
385 390 395
aac act att gaa gga act gca aaa tat att gaa act tcg gag cta tgc 1249
Asn Thr Ile Glu Gly Thr Ala Lys Tyr Ile Glu Thr Ser Glu Leu Cys
400 405 410
ggt ggt gct aga att tgt tat att ttc cat gag act ttt ggg cga acc 1297
Gly Gly Ala Arg Ile Cys Tyr Ile Phe His Glu Thr Phe Gly Arg Thr
415 420 425 430
tta gaa tct gtt gat cca ctt ggt ggc ctt aac act att gac att ttg 1345
Leu Glu Ser Val Asp Pro Leu Gly Gly Leu Asn Thr Ile Asp Ile Leu
435 440 445
act gcc att aga aat gct act ggt cct cgt cct gct tta ttt gtg cct 1393
Thr Ala Ile Arg Asn Ala Thr Gly Pro Arg Pro Ala Leu Phe Val Pro
450 455 460
gag gtt tca ttt gag tta ctg gtg aag cgg caa atc aaa cgt cta gaa 1441
Glu Val Ser Phe Glu Leu Leu Val Lys Arg Gln Ile Lys Arg Leu Glu
465 470 475
gag ccc agc ctc cgc tgt gtg gaa ctg gtt cat gag gaa atg caa agg 1489
Glu Pro Ser Leu Arg Cys Val Glu Leu Val His Glu Glu Met Gln Arg
480 485 490
atc att cag cac tgt agc aat tac agt aca cag gaa ttg tta cga ttt 1537
Ile Ile Gln His Cys Ser Asn Tyr Ser Thr Gln Glu Leu Leu Arg Phe
495 500 505 510
cct aaa ctt cat gat gcc ata gtt gaa gtg gtg act tgt ctt ctt cgt 1585
Pro Lys Leu His Asp Ala Ile Val Glu Val Val Thr Cys Leu Leu Arg
515 520 525
aaa agg ttg cct gtt aca aat gaa atg gtc cat aac tta gtg gca att 1633
Lys Arg Leu Pro Val Thr Asn Glu Met Val His Asn Leu Val Ala Ile
530 535 540
gaa ctg gct tat atc aac aca aaa cat cca gac ttt gct gat gct tgt 1681
Glu Leu Ala Tyr Ile Asn Thr Lys His Pro Asp Phe Ala Asp Ala Cys
545 550 555
ggg cta atg aac aat aat ata gag gaa caa agg aga aac agg cta gcc 1729
Gly Leu Met Asn Asn Asn Ile Glu Glu Gln Arg Arg Asn Arg Leu Ala
560 565 570
aga gaa tta cct tca gct gta tca cga gac aag tta att cag gac agc 1777
Arg Glu Leu Pro Ser Ala Val Ser Arg Asp Lys Leu Ile Gln Asp Ser
575 580 585 590
aga aga gaa act aaa aat gtt gca tct gga ggt ggt ggg gtt gga gat 1825
Arg Arg Glu Thr Lys Asn Val Ala Ser Gly Gly Gly Gly Val Gly Asp
595 600 605
ggt gtt caa gaa cca acc aca ggc aac tgg aga gga atg ctg aaa act 1873
Gly Val Gln Glu Pro Thr Thr Gly Asn Trp Arg Gly Met Leu Lys Thr
610 615 620
tca aaa gct gaa gag tta tta gca gaa gaa aaa tca aaa ccc att cca 1921
Ser Lys Ala Glu Glu Leu Leu Ala Glu Glu Lys Ser Lys Pro Ile Pro
625 630 635
att atg cca gcc agt cca caa aaa ggt cat gcc gtg aac ctg cta gat 1969
Ile Met Pro Ala Ser Pro Gln Lys Gly His Ala Val Asn Leu Leu Asp
640 645 650
gtg cca gtt cct gtt gca cga aaa cta tct gct cgg gaa cag cga gat 2017
Val Pro Val Pro Val Ala Arg Lys Leu Ser Ala Arg Glu Gln Arg Asp
655 660 665 670
tgt gag gtt att gaa cga ctc att aaa tca tat ttt ctc att gtc aga 2065
Cys Glu Val Ile Glu Arg Leu Ile Lys Ser Tyr Phe Leu Ile Val Arg
675 680 685
aag aat att caa gac agt gtg cca aag gca gta atg cat ttt ttg gtt 2113
Lys Asn Ile Gln Asp Ser Val Pro Lys Ala Val Met His Phe Leu Val
690 695 700
aat cat gtg aaa gac act ctt cag agt gag cta gta ggc cag ctg tat 2161
Asn His Val Lys Asp Thr Leu Gln Ser Glu Leu Val Gly Gln Leu Tyr
705 710 715
aaa tca tcc tta ttg gat gat ctt ctg aca gaa tct gag gac atg gca 2209
Lys Ser Ser Leu Leu Asp Asp Leu Leu Thr Glu Ser Glu Asp Met Ala
720 725 730
cag cgc agg aaa gaa gca gct gat atg cta aag gca tta caa gga gcc 2257
Gln Arg Arg Lys Glu Ala Ala Asp Met Leu Lys Ala Leu Gln Gly Ala
735 740 745 750
agt caa att att gct gaa atc cgg gag act cat ctt tgg tga 2299
Ser Gln Ile Ile Ala Glu Ile Arg Glu Thr His Leu Trp
755 760
agagaactat gtaatactga gactttgttg actcaaaact tgctagttac tgcctacctg 2359
agtagaatct tatttatgaa ctcctgtgta ttgcaatggt atgaatctgc tcatgtggag 2419
actggctata aactgaaaag tgtattccaa attgcagaac acatcacaca tttaatccaa 2479
ataataaatg gctgtttcta aaaaaaaaaa 2509


20
763
PRT
Homo sapiens

20
Met Ala Cys Arg Glu Gly Ala Gly Ser Arg Arg Ala Arg Ser Asn Gly
1 5 10 15
Cys Arg Leu Pro Arg Arg Gly Arg Arg Arg Gly Gly Arg Arg Arg Thr
20 25 30
Val Gly Pro Gly Pro Ile His Cys Arg Gly Arg Arg Ala Leu Gly Pro
35 40 45
Arg Val Phe Arg Val Met Glu Ala Leu Ile Pro Val Ile Asn Lys Leu
50 55 60
Gln Asp Val Phe Asn Thr Val Gly Ala Asp Ile Ile Gln Leu Pro Gln
65 70 75 80
Ile Val Val Val Gly Thr Gln Ser Ser Gly Lys Ser Ser Val Leu Glu
85 90 95
Ser Leu Val Gly Arg Asp Leu Leu Pro Arg Gly Thr Gly Ile Val Thr
100 105 110
Arg Arg Pro Leu Ile Leu Gln Leu Val His Val Thr Gln Glu Asp Lys
115 120 125
Arg Lys Thr Thr Gly Glu Glu Asn Gly Val Glu Ala Glu Glu Trp Gly
130 135 140
Lys Phe Leu His Thr Lys Asn Lys Leu Tyr Thr Asp Phe Asp Glu Ile
145 150 155 160
Arg Gln Glu Ile Glu Asn Glu Thr Glu Arg Ile Ser Gly Asn Asn Lys
165 170 175
Gly Val Ser Pro Glu Pro Ile His Leu Lys Ile Phe Ser Pro Asn Val
180 185 190
Val Asn Leu Thr Leu Val Asp Leu Pro Gly Met Thr Lys Val Pro Val
195 200 205
Gly Asp Gln Pro Lys Asp Ile Glu Leu Gln Ile Arg Glu Leu Ile Leu
210 215 220
Arg Phe Ile Ser Asn Pro Asn Ser Ile Ile Leu Ala Val Thr Ala Ala
225 230 235 240
Asn Thr Asp Met Ala Thr Ser Glu Ala Leu Lys Ile Ser Arg Glu Val
245 250 255
Asp Pro Asp Gly Arg Arg Thr Leu Ala Val Ile Thr Lys Leu Asp Leu
260 265 270
Met Asp Ala Gly Thr Asp Ala Met Asp Val Leu Met Gly Arg Val Ile
275 280 285
Pro Val Lys Leu Gly Ile Ile Gly Val Val Asn Arg Ser Gln Leu Asp
290 295 300
Ile Asn Asn Lys Lys Ser Val Thr Asp Ser Ile Arg Asp Glu Tyr Ala
305 310 315 320
Phe Leu Gln Lys Lys Tyr Pro Ser Leu Ala Asn Arg Asn Gly Thr Lys
325 330 335
Tyr Leu Ala Arg Thr Leu Asn Arg Leu Leu Met His His Ile Arg Asp
340 345 350
Cys Leu Pro Glu Leu Lys Thr Arg Ile Asn Val Leu Ala Ala Gln Tyr
355 360 365
Gln Ser Leu Leu Asn Ser Tyr Gly Glu Pro Val Asp Asp Lys Ser Ala
370 375 380
Thr Leu Leu Gln Leu Ile Thr Lys Phe Ala Thr Glu Tyr Cys Asn Thr
385 390 395 400
Ile Glu Gly Thr Ala Lys Tyr Ile Glu Thr Ser Glu Leu Cys Gly Gly
405 410 415
Ala Arg Ile Cys Tyr Ile Phe His Glu Thr Phe Gly Arg Thr Leu Glu
420 425 430
Ser Val Asp Pro Leu Gly Gly Leu Asn Thr Ile Asp Ile Leu Thr Ala
435 440 445
Ile Arg Asn Ala Thr Gly Pro Arg Pro Ala Leu Phe Val Pro Glu Val
450 455 460
Ser Phe Glu Leu Leu Val Lys Arg Gln Ile Lys Arg Leu Glu Glu Pro
465 470 475 480
Ser Leu Arg Cys Val Glu Leu Val His Glu Glu Met Gln Arg Ile Ile
485 490 495
Gln His Cys Ser Asn Tyr Ser Thr Gln Glu Leu Leu Arg Phe Pro Lys
500 505 510
Leu His Asp Ala Ile Val Glu Val Val Thr Cys Leu Leu Arg Lys Arg
515 520 525
Leu Pro Val Thr Asn Glu Met Val His Asn Leu Val Ala Ile Glu Leu
530 535 540
Ala Tyr Ile Asn Thr Lys His Pro Asp Phe Ala Asp Ala Cys Gly Leu
545 550 555 560
Met Asn Asn Asn Ile Glu Glu Gln Arg Arg Asn Arg Leu Ala Arg Glu
565 570 575
Leu Pro Ser Ala Val Ser Arg Asp Lys Leu Ile Gln Asp Ser Arg Arg
580 585 590
Glu Thr Lys Asn Val Ala Ser Gly Gly Gly Gly Val Gly Asp Gly Val
595 600 605
Gln Glu Pro Thr Thr Gly Asn Trp Arg Gly Met Leu Lys Thr Ser Lys
610 615 620
Ala Glu Glu Leu Leu Ala Glu Glu Lys Ser Lys Pro Ile Pro Ile Met
625 630 635 640
Pro Ala Ser Pro Gln Lys Gly His Ala Val Asn Leu Leu Asp Val Pro
645 650 655
Val Pro Val Ala Arg Lys Leu Ser Ala Arg Glu Gln Arg Asp Cys Glu
660 665 670
Val Ile Glu Arg Leu Ile Lys Ser Tyr Phe Leu Ile Val Arg Lys Asn
675 680 685
Ile Gln Asp Ser Val Pro Lys Ala Val Met His Phe Leu Val Asn His
690 695 700
Val Lys Asp Thr Leu Gln Ser Glu Leu Val Gly Gln Leu Tyr Lys Ser
705 710 715 720
Ser Leu Leu Asp Asp Leu Leu Thr Glu Ser Glu Asp Met Ala Gln Arg
725 730 735
Arg Lys Glu Ala Ala Asp Met Leu Lys Ala Leu Gln Gly Ala Ser Gln
740 745 750
Ile Ile Ala Glu Ile Arg Glu Thr His Leu Trp
755 760


21
2539
DNA
Homo sapiens

CDS
(8)..(2266)


21
agcgggc atg gcc tgc cgg gag ggg gca ggt agc cgg cgg gcc cgg tcc 49
Met Ala Cys Arg Glu Gly Ala Gly Ser Arg Arg Ala Arg Ser
1 5 10
aat ggg tgc cgg ctt ccg agg aga ggg cgg agg aga gga gga agg agg 97
Asn Gly Cys Arg Leu Pro Arg Arg Gly Arg Arg Arg Gly Gly Arg Arg
15 20 25 30
cga act gtg ggc ccc ggc ccc att cat tgc cgt ggc cgg cgg gca ctg 145
Arg Thr Val Gly Pro Gly Pro Ile His Cys Arg Gly Arg Arg Ala Leu
35 40 45
ggg ccc cgt gtt ttc aga gtc atg gag gcg cta att cct gtc ata aac 193
Gly Pro Arg Val Phe Arg Val Met Glu Ala Leu Ile Pro Val Ile Asn
50 55 60
aag ctc cag gac gtc ttc aac acg gtg ggc gcc gac atc atc cag ctg 241
Lys Leu Gln Asp Val Phe Asn Thr Val Gly Ala Asp Ile Ile Gln Leu
65 70 75
cct caa atc gtc gta gtg gga acg cag agc agc gga aag agc tca gtg 289
Pro Gln Ile Val Val Val Gly Thr Gln Ser Ser Gly Lys Ser Ser Val
80 85 90
cta gaa agc ctg gtg ggg agg gac ctg ctt ccc aga ggt act gga att 337
Leu Glu Ser Leu Val Gly Arg Asp Leu Leu Pro Arg Gly Thr Gly Ile
95 100 105 110
gtc acc cgg aga cct ctc att ctg caa ctg gtc cat gtg aca caa gaa 385
Val Thr Arg Arg Pro Leu Ile Leu Gln Leu Val His Val Thr Gln Glu
115 120 125
gat aaa cgg aaa aca aca gga gaa gaa aat ggg gtg gaa gca gaa gaa 433
Asp Lys Arg Lys Thr Thr Gly Glu Glu Asn Gly Val Glu Ala Glu Glu
130 135 140
tgg ggt aaa ttt ctt cac acc aaa aat aag ctt tac acg gat ttt gat 481
Trp Gly Lys Phe Leu His Thr Lys Asn Lys Leu Tyr Thr Asp Phe Asp
145 150 155
gaa att cga caa gaa att gaa aat gaa aca gaa aga att tca gga aat 529
Glu Ile Arg Gln Glu Ile Glu Asn Glu Thr Glu Arg Ile Ser Gly Asn
160 165 170
aat aag gga gta agc cct gaa cca att cat ctt aag att ttt tca ccc 577
Asn Lys Gly Val Ser Pro Glu Pro Ile His Leu Lys Ile Phe Ser Pro
175 180 185 190
aac gtt gtc aat ttg aca ctt gtg gat ttg cca gga atg acc aag gtg 625
Asn Val Val Asn Leu Thr Leu Val Asp Leu Pro Gly Met Thr Lys Val
195 200 205
cct gta ggt gat caa cct aag gat att gag ctt caa atc aga gag ctc 673
Pro Val Gly Asp Gln Pro Lys Asp Ile Glu Leu Gln Ile Arg Glu Leu
210 215 220
att ctt cgg ttc atc agt aat cct aat tcc att atc ctc gct gtc act 721
Ile Leu Arg Phe Ile Ser Asn Pro Asn Ser Ile Ile Leu Ala Val Thr
225 230 235
gct gct aat aca gat atg gca aca tca gag gca ctt aaa att tca aga 769
Ala Ala Asn Thr Asp Met Ala Thr Ser Glu Ala Leu Lys Ile Ser Arg
240 245 250
gag gta gat cca gat ggc tgc aga acc cta gct gta atc act aaa ctt 817
Glu Val Asp Pro Asp Gly Cys Arg Thr Leu Ala Val Ile Thr Lys Leu
255 260 265 270
gat ctc atg gat gcg ggt act gat gcc atg gat gta ttg atg gga agg 865
Asp Leu Met Asp Ala Gly Thr Asp Ala Met Asp Val Leu Met Gly Arg
275 280 285
gtt att cca gtc aaa ctt gga ata att gga gta gtt aac agg agc cag 913
Val Ile Pro Val Lys Leu Gly Ile Ile Gly Val Val Asn Arg Ser Gln
290 295 300
cta gat att aac aac aag aag agt gta act gat tca atc cgt gat gag 961
Leu Asp Ile Asn Asn Lys Lys Ser Val Thr Asp Ser Ile Arg Asp Glu
305 310 315
tat gct ttt ctt caa aag aaa tat cca tct ctg gcc aat aga aat gga 1009
Tyr Ala Phe Leu Gln Lys Lys Tyr Pro Ser Leu Ala Asn Arg Asn Gly
320 325 330
aca aag tat ctt gct agg act cta aac agg tta ctg atg cat cac atc 1057
Thr Lys Tyr Leu Ala Arg Thr Leu Asn Arg Leu Leu Met His His Ile
335 340 345 350
aga gat tgt tta cca gag ttg aaa aca aga ata aat gtt cta gct gct 1105
Arg Asp Cys Leu Pro Glu Leu Lys Thr Arg Ile Asn Val Leu Ala Ala
355 360 365
cag tat cag tct ctt cta aat agc tac ggt gaa ccc gtg gat gat aaa 1153
Gln Tyr Gln Ser Leu Leu Asn Ser Tyr Gly Glu Pro Val Asp Asp Lys
370 375 380
agt gct act tta ctc caa ctt att acc aaa ttt gcc aca gaa tat tgt 1201
Ser Ala Thr Leu Leu Gln Leu Ile Thr Lys Phe Ala Thr Glu Tyr Cys
385 390 395
aac act att gaa gga act gca aaa tat att gaa act tcg gag cta tgc 1249
Asn Thr Ile Glu Gly Thr Ala Lys Tyr Ile Glu Thr Ser Glu Leu Cys
400 405 410
ggt ggt gct aga att tgt tat att ttc cat gag act ttt ggg cga acc 1297
Gly Gly Ala Arg Ile Cys Tyr Ile Phe His Glu Thr Phe Gly Arg Thr
415 420 425 430
tta gaa tct gtt gat cca ctt ggt ggc ctt aac act att gac att ttg 1345
Leu Glu Ser Val Asp Pro Leu Gly Gly Leu Asn Thr Ile Asp Ile Leu
435 440 445
act gcc att aga aat gct act ggt cct cgt cct gct tta ttt gtg cct 1393
Thr Ala Ile Arg Asn Ala Thr Gly Pro Arg Pro Ala Leu Phe Val Pro
450 455 460
gag gtt tca ttt gag tta ctg gtg aag cgg caa atc aaa cgt cta gaa 1441
Glu Val Ser Phe Glu Leu Leu Val Lys Arg Gln Ile Lys Arg Leu Glu
465 470 475
gag ccc agc ctc cgc tgt gtg gaa ctg gtt cat gag gaa atg caa agg 1489
Glu Pro Ser Leu Arg Cys Val Glu Leu Val His Glu Glu Met Gln Arg
480 485 490
atc att cag cac tgt agc aat tac agt aca cag gaa ttg tta cga ttt 1537
Ile Ile Gln His Cys Ser Asn Tyr Ser Thr Gln Glu Leu Leu Arg Phe
495 500 505 510
cct aaa ctt cat gat gcc ata gtt gaa gtg gtg act tgt ctt ctt cgt 1585
Pro Lys Leu His Asp Ala Ile Val Glu Val Val Thr Cys Leu Leu Arg
515 520 525
aaa agg ttg cct gtt aca aat gaa atg gtc cat aac tta gtg gca att 1633
Lys Arg Leu Pro Val Thr Asn Glu Met Val His Asn Leu Val Ala Ile
530 535 540
gaa ctg gct tat atc aac aca aaa cat cca gac ttt gct gat gct tgt 1681
Glu Leu Ala Tyr Ile Asn Thr Lys His Pro Asp Phe Ala Asp Ala Cys
545 550 555
ggg cta atg aac aat aat ata gag gaa caa agg aga aac agg cta gcc 1729
Gly Leu Met Asn Asn Asn Ile Glu Glu Gln Arg Arg Asn Arg Leu Ala
560 565 570
aga gaa tta cct tca gct gta tca cga gac aag gtt gca tct gga ggt 1777
Arg Glu Leu Pro Ser Ala Val Ser Arg Asp Lys Val Ala Ser Gly Gly
575 580 585 590
ggt ggg gtt gga gat ggt gtt caa gaa cca acc aca ggc aac tgg aga 1825
Gly Gly Val Gly Asp Gly Val Gln Glu Pro Thr Thr Gly Asn Trp Arg
595 600 605
gga atg ctg aaa act tca aaa gct gaa gag tta tta gca gaa gaa aaa 1873
Gly Met Leu Lys Thr Ser Lys Ala Glu Glu Leu Leu Ala Glu Glu Lys
610 615 620
tca aaa ccc att cca att atg cca gcc agt cca caa aaa ggt cat gcc 1921
Ser Lys Pro Ile Pro Ile Met Pro Ala Ser Pro Gln Lys Gly His Ala
625 630 635
gtg aac ctg cta gat gtg cca gtt cct gtt gca cga aaa cta tct gct 1969
Val Asn Leu Leu Asp Val Pro Val Pro Val Ala Arg Lys Leu Ser Ala
640 645 650
cgg gaa cag cga gat tgt gag gtt att gaa cga ctc att aaa tca tat 2017
Arg Glu Gln Arg Asp Cys Glu Val Ile Glu Arg Leu Ile Lys Ser Tyr
655 660 665 670
ttt ctc att gtc aga aag aat att caa gac agt gtg cca aag gca gta 2065
Phe Leu Ile Val Arg Lys Asn Ile Gln Asp Ser Val Pro Lys Ala Val
675 680 685
atg cat ttt ttg gtt aat cat gtg aaa gac act ctt cag agt gag cta 2113
Met His Phe Leu Val Asn His Val Lys Asp Thr Leu Gln Ser Glu Leu
690 695 700
gta ggc cag ctg tat aaa tca tcc tta ttg gat gat ctt ctg aca gaa 2161
Val Gly Gln Leu Tyr Lys Ser Ser Leu Leu Asp Asp Leu Leu Thr Glu
705 710 715
tct gag gac atg gca cag cgc agg aaa gaa gca gct gat atg cta aag 2209
Ser Glu Asp Met Ala Gln Arg Arg Lys Glu Ala Ala Asp Met Leu Lys
720 725 730
gca tta caa gga gcc agt caa att att gct gaa atc cgg gag act cat 2257
Ala Leu Gln Gly Ala Ser Gln Ile Ile Ala Glu Ile Arg Glu Thr His
735 740 745 750
ctt tgg tga agagaactat gtaatactga gactttgttg actcaaaact 2306
Leu Trp
tgctagttac tgcctacctg agtagaatct tatttatgaa ctcctgtgta ttgcaatggt 2366
atgaatctgc tcatgtggag actggctata aactgaaaag tgtattctaa attgcagaac 2426
acatcacaca tttaatccaa ataataaatg gctgtttcaa aaaaaaaaaa aaaaaaaaaa 2486
aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaa 2539


22
752
PRT
Homo sapiens

22
Met Ala Cys Arg Glu Gly Ala Gly Ser Arg Arg Ala Arg Ser Asn Gly
1 5 10 15
Cys Arg Leu Pro Arg Arg Gly Arg Arg Arg Gly Gly Arg Arg Arg Thr
20 25 30
Val Gly Pro Gly Pro Ile His Cys Arg Gly Arg Arg Ala Leu Gly Pro
35 40 45
Arg Val Phe Arg Val Met Glu Ala Leu Ile Pro Val Ile Asn Lys Leu
50 55 60
Gln Asp Val Phe Asn Thr Val Gly Ala Asp Ile Ile Gln Leu Pro Gln
65 70 75 80
Ile Val Val Val Gly Thr Gln Ser Ser Gly Lys Ser Ser Val Leu Glu
85 90 95
Ser Leu Val Gly Arg Asp Leu Leu Pro Arg Gly Thr Gly Ile Val Thr
100 105 110
Arg Arg Pro Leu Ile Leu Gln Leu Val His Val Thr Gln Glu Asp Lys
115 120 125
Arg Lys Thr Thr Gly Glu Glu Asn Gly Val Glu Ala Glu Glu Trp Gly
130 135 140
Lys Phe Leu His Thr Lys Asn Lys Leu Tyr Thr Asp Phe Asp Glu Ile
145 150 155 160
Arg Gln Glu Ile Glu Asn Glu Thr Glu Arg Ile Ser Gly Asn Asn Lys
165 170 175
Gly Val Ser Pro Glu Pro Ile His Leu Lys Ile Phe Ser Pro Asn Val
180 185 190
Val Asn Leu Thr Leu Val Asp Leu Pro Gly Met Thr Lys Val Pro Val
195 200 205
Gly Asp Gln Pro Lys Asp Ile Glu Leu Gln Ile Arg Glu Leu Ile Leu
210 215 220
Arg Phe Ile Ser Asn Pro Asn Ser Ile Ile Leu Ala Val Thr Ala Ala
225 230 235 240
Asn Thr Asp Met Ala Thr Ser Glu Ala Leu Lys Ile Ser Arg Glu Val
245 250 255
Asp Pro Asp Gly Cys Arg Thr Leu Ala Val Ile Thr Lys Leu Asp Leu
260 265 270
Met Asp Ala Gly Thr Asp Ala Met Asp Val Leu Met Gly Arg Val Ile
275 280 285
Pro Val Lys Leu Gly Ile Ile Gly Val Val Asn Arg Ser Gln Leu Asp
290 295 300
Ile Asn Asn Lys Lys Ser Val Thr Asp Ser Ile Arg Asp Glu Tyr Ala
305 310 315 320
Phe Leu Gln Lys Lys Tyr Pro Ser Leu Ala Asn Arg Asn Gly Thr Lys
325 330 335
Tyr Leu Ala Arg Thr Leu Asn Arg Leu Leu Met His His Ile Arg Asp
340 345 350
Cys Leu Pro Glu Leu Lys Thr Arg Ile Asn Val Leu Ala Ala Gln Tyr
355 360 365
Gln Ser Leu Leu Asn Ser Tyr Gly Glu Pro Val Asp Asp Lys Ser Ala
370 375 380
Thr Leu Leu Gln Leu Ile Thr Lys Phe Ala Thr Glu Tyr Cys Asn Thr
385 390 395 400
Ile Glu Gly Thr Ala Lys Tyr Ile Glu Thr Ser Glu Leu Cys Gly Gly
405 410 415
Ala Arg Ile Cys Tyr Ile Phe His Glu Thr Phe Gly Arg Thr Leu Glu
420 425 430
Ser Val Asp Pro Leu Gly Gly Leu Asn Thr Ile Asp Ile Leu Thr Ala
435 440 445
Ile Arg Asn Ala Thr Gly Pro Arg Pro Ala Leu Phe Val Pro Glu Val
450 455 460
Ser Phe Glu Leu Leu Val Lys Arg Gln Ile Lys Arg Leu Glu Glu Pro
465 470 475 480
Ser Leu Arg Cys Val Glu Leu Val His Glu Glu Met Gln Arg Ile Ile
485 490 495
Gln His Cys Ser Asn Tyr Ser Thr Gln Glu Leu Leu Arg Phe Pro Lys
500 505 510
Leu His Asp Ala Ile Val Glu Val Val Thr Cys Leu Leu Arg Lys Arg
515 520 525
Leu Pro Val Thr Asn Glu Met Val His Asn Leu Val Ala Ile Glu Leu
530 535 540
Ala Tyr Ile Asn Thr Lys His Pro Asp Phe Ala Asp Ala Cys Gly Leu
545 550 555 560
Met Asn Asn Asn Ile Glu Glu Gln Arg Arg Asn Arg Leu Ala Arg Glu
565 570 575
Leu Pro Ser Ala Val Ser Arg Asp Lys Val Ala Ser Gly Gly Gly Gly
580 585 590
Val Gly Asp Gly Val Gln Glu Pro Thr Thr Gly Asn Trp Arg Gly Met
595 600 605
Leu Lys Thr Ser Lys Ala Glu Glu Leu Leu Ala Glu Glu Lys Ser Lys
610 615 620
Pro Ile Pro Ile Met Pro Ala Ser Pro Gln Lys Gly His Ala Val Asn
625 630 635 640
Leu Leu Asp Val Pro Val Pro Val Ala Arg Lys Leu Ser Ala Arg Glu
645 650 655
Gln Arg Asp Cys Glu Val Ile Glu Arg Leu Ile Lys Ser Tyr Phe Leu
660 665 670
Ile Val Arg Lys Asn Ile Gln Asp Ser Val Pro Lys Ala Val Met His
675 680 685
Phe Leu Val Asn His Val Lys Asp Thr Leu Gln Ser Glu Leu Val Gly
690 695 700
Gln Leu Tyr Lys Ser Ser Leu Leu Asp Asp Leu Leu Thr Glu Ser Glu
705 710 715 720
Asp Met Ala Gln Arg Arg Lys Glu Ala Ala Asp Met Leu Lys Ala Leu
725 730 735
Gln Gly Ala Ser Gln Ile Ile Ala Glu Ile Arg Glu Thr His Leu Trp
740 745 750


23
6289
DNA
Homo sapiens

CDS
(1177)..(5931)


23
atgcctcagt ttttaaaaaa ggatccttac acttcatgtc tcctagccat cagaagagga 60
atgagacagc aaaagttcaa atggcctgtt tcaagtttct gatataaaac gatgacattt 120
tcaggaaaat cctgcatttc cagagagaga ctggctggtt aaatttctga aagaggacac 180
cagctaaaag aaggtattgc atctcacccg agcagactgt gtctgtggaa agtgtaagcc 240
ccttgccaga agagcagctt cccagcaaag gcagagggtg aaaacagcaa aggtcttaag 300
acactgggga cctagagtca aaagggacct cctccaggga aaacgctgtg tgagaaatgg 360
cctcattcgg tgactgtgag tgacacagca gaaagttggg tcattccggc tgcttttttg 420
agaagtccct gaagagatca ataacagcaa gagggaacct ggcaaggaag ctattcctat 480
aatccaggaa agagatgagg aaggcttgga ccaggtggta gtggtgtcag gtagtcaaat 540
gctgggtata ttttgaagat acaccccata ggatttgctc cacattgaat gtggaatgct 600
ggaagagaga taaagtgtac ctgtcacata ctttttgagt tttatttatt ttcttagaag 660
taagtacaca aagagatgct acctaggaga agggtattct tttcactatt ctttcaaatt 720
ttctgtatgt tcgaacattt tcatagtaga aagttggggg gaaaatctgt ttcataaaca 780
tttcctcagc agcagtccag tctattgcat tttaattggt tgtgatatca ttgttttatg 840
caatacgttc tcaacaagta tatcctccgg caaactgaac aaggaccaag tctgttctgc 900
ctacagctct gcttcctcat agctgctttc cagaacgtga ctcttgcaaa ttatcaagaa 960
aggggaacta atctaaggga tccagatcaa acagcctcat gaagacttat tttatgtttc 1020
taatataaag atagaagttt tcagaaaagc cctgctacac agaggatcag agcaggggtg 1080
ggcctgctgg gctgcagctg ggattctgag catcctttcc cggaggcacg gaaagtgagt 1140
gagtgagccc agtgaggaag aagttgaagc tttgat atg agt aaa caa gta tct 1194
Met Ser Lys Gln Val Ser
1 5
cta cct gaa atg att aaa gac tgg acc aaa gag cat gtg aaa aaa tgg 1242
Leu Pro Glu Met Ile Lys Asp Trp Thr Lys Glu His Val Lys Lys Trp
10 15 20
gta aat gaa gac ctt aag att aat gag caa tac ggg caa att ctg ctc 1290
Val Asn Glu Asp Leu Lys Ile Asn Glu Gln Tyr Gly Gln Ile Leu Leu
25 30 35
agt gaa gaa gta aca gga tta gtc ctg cag gaa tta act gag aag gac 1338
Ser Glu Glu Val Thr Gly Leu Val Leu Gln Glu Leu Thr Glu Lys Asp
40 45 50
ctt gta gaa atg ggg cta cca tgg ggt cca gca ctt ttg ata aaa cgt 1386
Leu Val Glu Met Gly Leu Pro Trp Gly Pro Ala Leu Leu Ile Lys Arg
55 60 65 70
tca tac aac aaa ttg aat agt aag tcc cct gaa agt gac aat cat gat 1434
Ser Tyr Asn Lys Leu Asn Ser Lys Ser Pro Glu Ser Asp Asn His Asp
75 80 85
ccg gga caa tta gat aat tca aaa ccg tcc aaa aca gaa cac caa aaa 1482
Pro Gly Gln Leu Asp Asn Ser Lys Pro Ser Lys Thr Glu His Gln Lys
90 95 100
aat cca aaa cac acc aaa aag gaa gaa gaa aat tca atg tca tct aat 1530
Asn Pro Lys His Thr Lys Lys Glu Glu Glu Asn Ser Met Ser Ser Asn
105 110 115
att gat tat gat ccc aga gag atc aga gat atc aaa caa gaa gaa tca 1578
Ile Asp Tyr Asp Pro Arg Glu Ile Arg Asp Ile Lys Gln Glu Glu Ser
120 125 130
att ctt atg aaa gaa aat gtg tta gat gaa gta gca aat gct aaa cac 1626
Ile Leu Met Lys Glu Asn Val Leu Asp Glu Val Ala Asn Ala Lys His
135 140 145 150
aag aaa aag ggt aag cta aaa cct gaa caa ttg act tgt atg cca tat 1674
Lys Lys Lys Gly Lys Leu Lys Pro Glu Gln Leu Thr Cys Met Pro Tyr
155 160 165
cct ttt gat cag ttc cat gac agc cat cgc tac ata gaa cat tat act 1722
Pro Phe Asp Gln Phe His Asp Ser His Arg Tyr Ile Glu His Tyr Thr
170 175 180
cta caa cct gaa aca gga gca ctc aat ctc att gat cca ata cat gag 1770
Leu Gln Pro Glu Thr Gly Ala Leu Asn Leu Ile Asp Pro Ile His Glu
185 190 195
ttc aaa gct ctc aca aac aca gaa aca gcc acg gaa gtg gac att aag 1818
Phe Lys Ala Leu Thr Asn Thr Glu Thr Ala Thr Glu Val Asp Ile Lys
200 205 210
atg aaa ttc agc aat gaa gtc ttc cga ttt gca tca gct tgt atg aat 1866
Met Lys Phe Ser Asn Glu Val Phe Arg Phe Ala Ser Ala Cys Met Asn
215 220 225 230
tca cgc acc aat ggc acc atc cat ttt gga gtc aag gac aaa ccc cat 1914
Ser Arg Thr Asn Gly Thr Ile His Phe Gly Val Lys Asp Lys Pro His
235 240 245
gga gaa att gtt ggt gtg aaa atc acc agt aag gct gcc ttc att gac 1962
Gly Glu Ile Val Gly Val Lys Ile Thr Ser Lys Ala Ala Phe Ile Asp
250 255 260
cac ttc aat gta atg atc aaa aag tat ttt gaa gaa agt gag atc aat 2010
His Phe Asn Val Met Ile Lys Lys Tyr Phe Glu Glu Ser Glu Ile Asn
265 270 275
gaa gcc aag aag tgt att cgg gag cca agg ttt gtg gaa gtc ctt ctg 2058
Glu Ala Lys Lys Cys Ile Arg Glu Pro Arg Phe Val Glu Val Leu Leu
280 285 290
cag aac aat aca cca tct gac aga ttt gtc att gaa gtt gat act att 2106
Gln Asn Asn Thr Pro Ser Asp Arg Phe Val Ile Glu Val Asp Thr Ile
295 300 305 310
cca aaa cac tct ata tgt aat gat aag tat ttc tac att cag atg caa 2154
Pro Lys His Ser Ile Cys Asn Asp Lys Tyr Phe Tyr Ile Gln Met Gln
315 320 325
att tgt aaa gat aaa ata tgg aaa caa aac caa aat ctt tca ctg ttt 2202
Ile Cys Lys Asp Lys Ile Trp Lys Gln Asn Gln Asn Leu Ser Leu Phe
330 335 340
gta aga gaa ggg gct agc tct agg gat atc ctg gcc aat tcc aag caa 2250
Val Arg Glu Gly Ala Ser Ser Arg Asp Ile Leu Ala Asn Ser Lys Gln
345 350 355
cgg gat gta gat ttc aag gca ttt tta caa aat tta aag tca ctg gta 2298
Arg Asp Val Asp Phe Lys Ala Phe Leu Gln Asn Leu Lys Ser Leu Val
360 365 370
gca tct aga aaa gag gct gaa gaa gag tat gga atg aag gca atg aag 2346
Ala Ser Arg Lys Glu Ala Glu Glu Glu Tyr Gly Met Lys Ala Met Lys
375 380 385 390
aag gag agt gaa gga cta aag ctg gtt aaa ctt ctc ata gga aac cga 2394
Lys Glu Ser Glu Gly Leu Lys Leu Val Lys Leu Leu Ile Gly Asn Arg
395 400 405
gac tca ctg gat aat tca tac tat gac tgg tac att ctt gta aca aat 2442
Asp Ser Leu Asp Asn Ser Tyr Tyr Asp Trp Tyr Ile Leu Val Thr Asn
410 415 420
aaa tgc cat cca aac caa ata aag cac tta gat ttt tta aaa gaa att 2490
Lys Cys His Pro Asn Gln Ile Lys His Leu Asp Phe Leu Lys Glu Ile
425 430 435
aaa tgg ttt gct gtg ttg gag ttt gat cct gaa tct atg atc aat gga 2538
Lys Trp Phe Ala Val Leu Glu Phe Asp Pro Glu Ser Met Ile Asn Gly
440 445 450
gtg gtc aaa gct tac aaa gaa agt cgg gtg gca aac ctt cac ttt cca 2586
Val Val Lys Ala Tyr Lys Glu Ser Arg Val Ala Asn Leu His Phe Pro
455 460 465 470
aat caa tat gaa gac aag aca act aac atg tgg gag aag att tct act 2634
Asn Gln Tyr Glu Asp Lys Thr Thr Asn Met Trp Glu Lys Ile Ser Thr
475 480 485
ctt aat ctt tac caa cag ccc agc tgg att ttc tgc aac ggc aga tca 2682
Leu Asn Leu Tyr Gln Gln Pro Ser Trp Ile Phe Cys Asn Gly Arg Ser
490 495 500
gac ctg aaa agc gag aca tat aaa cct cta gaa cca cat tta tgg cag 2730
Asp Leu Lys Ser Glu Thr Tyr Lys Pro Leu Glu Pro His Leu Trp Gln
505 510 515
aga gaa aga gct tca gaa gtc agg aaa cta att tta ttt ctc aca gat 2778
Arg Glu Arg Ala Ser Glu Val Arg Lys Leu Ile Leu Phe Leu Thr Asp
520 525 530
gaa aat ata atg aca aga gga aaa ttt ttg gta gtg ttt cta tta ctc 2826
Glu Asn Ile Met Thr Arg Gly Lys Phe Leu Val Val Phe Leu Leu Leu
535 540 545 550
tct tca gtg gaa agc cca gga gat cca ctc att gaa act ttc tgg gct 2874
Ser Ser Val Glu Ser Pro Gly Asp Pro Leu Ile Glu Thr Phe Trp Ala
555 560 565
ttc tat caa gct ctc aaa gga atg gaa aat atg ttg tgt atc tct gta 2922
Phe Tyr Gln Ala Leu Lys Gly Met Glu Asn Met Leu Cys Ile Ser Val
570 575 580
aac tca cat att tat caa cga tgg aaa gat cta cta caa aca aga acg 2970
Asn Ser His Ile Tyr Gln Arg Trp Lys Asp Leu Leu Gln Thr Arg Thr
585 590 595
aag atg gaa gat gaa cta aca aac cac agt att tcc act tta aat ata 3018
Lys Met Glu Asp Glu Leu Thr Asn His Ser Ile Ser Thr Leu Asn Ile
600 605 610
gaa ctg gta aac agc act atc ctt aaa cta aaa tcg gtg act cgg tca 3066
Glu Leu Val Asn Ser Thr Ile Leu Lys Leu Lys Ser Val Thr Arg Ser
615 620 625 630
tca aga agg ttt ttg ccc gcc cgt gga tct tct tca gtt atc cta gag 3114
Ser Arg Arg Phe Leu Pro Ala Arg Gly Ser Ser Ser Val Ile Leu Glu
635 640 645
aaa aag aaa gag gat gtc ttg act gca ctg gaa atc ctc tgt gaa aat 3162
Lys Lys Lys Glu Asp Val Leu Thr Ala Leu Glu Ile Leu Cys Glu Asn
650 655 660
gag tgt aca gag aca gac atc gag aaa gac aaa tct aaa ttc ctg gag 3210
Glu Cys Thr Glu Thr Asp Ile Glu Lys Asp Lys Ser Lys Phe Leu Glu
665 670 675
ttt aag aaa tca aaa gaa gaa cac ttt tat cga ggt ggc aaa gta tcc 3258
Phe Lys Lys Ser Lys Glu Glu His Phe Tyr Arg Gly Gly Lys Val Ser
680 685 690
tgg tgg aac ttc tat ttt tct tct gaa aac tat tct tca gat ttt gtt 3306
Trp Trp Asn Phe Tyr Phe Ser Ser Glu Asn Tyr Ser Ser Asp Phe Val
695 700 705 710
aaa agg gac agt tat gaa aag ctt aaa gat tta ata cac tgc tgg gca 3354
Lys Arg Asp Ser Tyr Glu Lys Leu Lys Asp Leu Ile His Cys Trp Ala
715 720 725
gag tct cct aaa cca ata ttt gca aaa atc atc aat ctt tat cat cat 3402
Glu Ser Pro Lys Pro Ile Phe Ala Lys Ile Ile Asn Leu Tyr His His
730 735 740
cca ggc tgt gga ggt acc aca ctg gct atg cat gtt ctc tgg gac tta 3450
Pro Gly Cys Gly Gly Thr Thr Leu Ala Met His Val Leu Trp Asp Leu
745 750 755
aag aaa aac ttc aga tgt gct gtg tta aaa aac aag aca act gat ttt 3498
Lys Lys Asn Phe Arg Cys Ala Val Leu Lys Asn Lys Thr Thr Asp Phe
760 765 770
gca gaa att gca gag caa gtg atc aat ctg gtc acc tat agg gca aag 3546
Ala Glu Ile Ala Glu Gln Val Ile Asn Leu Val Thr Tyr Arg Ala Lys
775 780 785 790
agc cat cag gat tac att cct gtg ctt ctc ctt gtg gat gat ttt gaa 3594
Ser His Gln Asp Tyr Ile Pro Val Leu Leu Leu Val Asp Asp Phe Glu
795 800 805
gaa caa gaa aat gtc tac ttt cta caa aat gcc atc cat tcc gtt tta 3642
Glu Gln Glu Asn Val Tyr Phe Leu Gln Asn Ala Ile His Ser Val Leu
810 815 820
gca gaa aag gat ttg cga tat gaa aaa aca ttg gta att atc tta aac 3690
Ala Glu Lys Asp Leu Arg Tyr Glu Lys Thr Leu Val Ile Ile Leu Asn
825 830 835
tgc atg aga tcc cgg aat cca gat gaa agt gca aaa ttg gca gac agt 3738
Cys Met Arg Ser Arg Asn Pro Asp Glu Ser Ala Lys Leu Ala Asp Ser
840 845 850
att gca cta aat tac caa ctt tct tcc aag gaa caa aga gcc ttt ggt 3786
Ile Ala Leu Asn Tyr Gln Leu Ser Ser Lys Glu Gln Arg Ala Phe Gly
855 860 865 870
gcc aaa ctg aag gaa att gaa aag cag cac aag aac tgt gaa aac ttt 3834
Ala Lys Leu Lys Glu Ile Glu Lys Gln His Lys Asn Cys Glu Asn Phe
875 880 885
tat tcc ttc atg atc atg aaa agc aat ttt gat gaa aca tat ata gaa 3882
Tyr Ser Phe Met Ile Met Lys Ser Asn Phe Asp Glu Thr Tyr Ile Glu
890 895 900
aat gta gtc agg aat atc cta aaa gga cag gat gtt gac agc aag gaa 3930
Asn Val Val Arg Asn Ile Leu Lys Gly Gln Asp Val Asp Ser Lys Glu
905 910 915
gca caa ctc att tcc ttc ctg gct tta ctc agc tct tat gtt act gac 3978
Ala Gln Leu Ile Ser Phe Leu Ala Leu Leu Ser Ser Tyr Val Thr Asp
920 925 930
tct aca att tca gtt tca cag tgt gaa ata ttt ttg gga atc ata tac 4026
Ser Thr Ile Ser Val Ser Gln Cys Glu Ile Phe Leu Gly Ile Ile Tyr
935 940 945 950
act agt aca ccc tgg gaa cct gaa agc tta gaa gac aag atg gga act 4074
Thr Ser Thr Pro Trp Glu Pro Glu Ser Leu Glu Asp Lys Met Gly Thr
955 960 965
tat tct aca ctt cta ata aaa aca gaa gtt gca gaa tat ggg aga tac 4122
Tyr Ser Thr Leu Leu Ile Lys Thr Glu Val Ala Glu Tyr Gly Arg Tyr
970 975 980
aca ggt gtg cgt atc att cac cct ctg att gcc ctg tac tgt cta aaa 4170
Thr Gly Val Arg Ile Ile His Pro Leu Ile Ala Leu Tyr Cys Leu Lys
985 990 995
gaa ctg gaa aga agc tat cac ttg gat aaa tgt caa att gca ttg 4215
Glu Leu Glu Arg Ser Tyr His Leu Asp Lys Cys Gln Ile Ala Leu
1000 1005 1010
aat ata tta gaa gag aat tta ttc tat gat tct gga ata gga aga 4260
Asn Ile Leu Glu Glu Asn Leu Phe Tyr Asp Ser Gly Ile Gly Arg
1015 1020 1025
gac aaa ttt caa cat gat gtt caa act ctt ctg ctt aca aga cag 4305
Asp Lys Phe Gln His Asp Val Gln Thr Leu Leu Leu Thr Arg Gln
1030 1035 1040
cgc aag gtg tat gga gat gaa aca gac act ctg ttt tcc cca tta 4350
Arg Lys Val Tyr Gly Asp Glu Thr Asp Thr Leu Phe Ser Pro Leu
1045 1050 1055
atg gaa gct tta cag aat aaa gac att gaa aag gtc ttg agt gca 4395
Met Glu Ala Leu Gln Asn Lys Asp Ile Glu Lys Val Leu Ser Ala
1060 1065 1070
gga agt aga cga ttc cca caa aat gca ttc att tgt caa gcc tta 4440
Gly Ser Arg Arg Phe Pro Gln Asn Ala Phe Ile Cys Gln Ala Leu
1075 1080 1085
gca aga cat ttc tac att aaa gag aag gac ttt aac aca gct ctg 4485
Ala Arg His Phe Tyr Ile Lys Glu Lys Asp Phe Asn Thr Ala Leu
1090 1095 1100
gac tgg gca cgt cag gcc aaa atg aaa gca cct aaa aat tcc tat 4530
Asp Trp Ala Arg Gln Ala Lys Met Lys Ala Pro Lys Asn Ser Tyr
1105 1110 1115
att tca gat aca cta ggt caa gtc tac aaa agt gaa atc aaa tgg 4575
Ile Ser Asp Thr Leu Gly Gln Val Tyr Lys Ser Glu Ile Lys Trp
1120 1125 1130
tgg ttg gat ggg aac aaa aac tgt agg agc att act gtt aat gac 4620
Trp Leu Asp Gly Asn Lys Asn Cys Arg Ser Ile Thr Val Asn Asp
1135 1140 1145
cta aca cat ctc cta gaa gct gcg gaa aaa gcc tca aga gct ttc 4665
Leu Thr His Leu Leu Glu Ala Ala Glu Lys Ala Ser Arg Ala Phe
1150 1155 1160
aaa gaa tcc caa agg caa act gat agt aaa aac tat gaa acc gag 4710
Lys Glu Ser Gln Arg Gln Thr Asp Ser Lys Asn Tyr Glu Thr Glu
1165 1170 1175
aac tgg tca cca cag aag tcc cag aga cga tat gac atg tat aac 4755
Asn Trp Ser Pro Gln Lys Ser Gln Arg Arg Tyr Asp Met Tyr Asn
1180 1185 1190
aca gct tgt ttc ttg ggt gaa ata gaa gtt ggt ctt tac act atc 4800
Thr Ala Cys Phe Leu Gly Glu Ile Glu Val Gly Leu Tyr Thr Ile
1195 1200 1205
cag att ctt cag ctc act ccc ttt ttc cac aaa gaa aat gaa tta 4845
Gln Ile Leu Gln Leu Thr Pro Phe Phe His Lys Glu Asn Glu Leu
1210 1215 1220
tcc aaa aaa cat atg gtg caa ttt tta tca gga aag tgg acc att 4890
Ser Lys Lys His Met Val Gln Phe Leu Ser Gly Lys Trp Thr Ile
1225 1230 1235
cct cct gat ccc aga aat gaa tgt tat ttg gct ctt agc aag ttc 4935
Pro Pro Asp Pro Arg Asn Glu Cys Tyr Leu Ala Leu Ser Lys Phe
1240 1245 1250
aca tcc cac cta aaa aat tta caa tca gat ctg aaa agg tgc ttt 4980
Thr Ser His Leu Lys Asn Leu Gln Ser Asp Leu Lys Arg Cys Phe
1255 1260 1265
gac ttt ttt att gat tat atg gtt ctt ctg aaa atg agg tat acc 5025
Asp Phe Phe Ile Asp Tyr Met Val Leu Leu Lys Met Arg Tyr Thr
1270 1275 1280
caa aaa gaa att gca gaa atc atg tta agc aag aaa gtc agt cgt 5070
Gln Lys Glu Ile Ala Glu Ile Met Leu Ser Lys Lys Val Ser Arg
1285 1290 1295
tgt ttc agg aaa tac aca gaa ctt ttc tgt cat ttg gat cca tgt 5115
Cys Phe Arg Lys Tyr Thr Glu Leu Phe Cys His Leu Asp Pro Cys
1300 1305 1310
cta tta caa agt aaa gag agt caa tta ctc cag gag gag aat tgc 5160
Leu Leu Gln Ser Lys Glu Ser Gln Leu Leu Gln Glu Glu Asn Cys
1315 1320 1325
agg aaa aag cta gaa gct ctg aga gca gat agg ttt gct gga ctc 5205
Arg Lys Lys Leu Glu Ala Leu Arg Ala Asp Arg Phe Ala Gly Leu
1330 1335 1340
ttg gaa tat ctt aat cca aac tac aaa gat gct acc acc atg gaa 5250
Leu Glu Tyr Leu Asn Pro Asn Tyr Lys Asp Ala Thr Thr Met Glu
1345 1350 1355
agt ata gtg aat gaa tat gcc ttc cta ctg cag caa aac tca aaa 5295
Ser Ile Val Asn Glu Tyr Ala Phe Leu Leu Gln Gln Asn Ser Lys
1360 1365 1370
aag ccc atg aca aat gag aaa caa aat tcc att ttg gcc aac att 5340
Lys Pro Met Thr Asn Glu Lys Gln Asn Ser Ile Leu Ala Asn Ile
1375 1380 1385
att ctg agt tgt cta aag ccc aac tcc aag tta att caa cca ctt 5385
Ile Leu Ser Cys Leu Lys Pro Asn Ser Lys Leu Ile Gln Pro Leu
1390 1395 1400
acc acg cta aaa aaa caa ctc cga gag gtc ttg caa ttt gta gga 5430
Thr Thr Leu Lys Lys Gln Leu Arg Glu Val Leu Gln Phe Val Gly
1405 1410 1415
cta agt cat caa tat cca ggt cct tat ttc ttg gcc tgc ctc ctg 5475
Leu Ser His Gln Tyr Pro Gly Pro Tyr Phe Leu Ala Cys Leu Leu
1420 1425 1430
ttc tgg cca gaa aat caa gag cta gat caa gat tcc aaa cta ata 5520
Phe Trp Pro Glu Asn Gln Glu Leu Asp Gln Asp Ser Lys Leu Ile
1435 1440 1445
gaa aag tat gtt tca tcc tta aat aga tcc ttc agg gga cag tac 5565
Glu Lys Tyr Val Ser Ser Leu Asn Arg Ser Phe Arg Gly Gln Tyr
1450 1455 1460
aag cgc atg tgc agg tcc aag cag gca agc aca ctt ttc tat ctg 5610
Lys Arg Met Cys Arg Ser Lys Gln Ala Ser Thr Leu Phe Tyr Leu
1465 1470 1475
ggc aaa agg aag ggt cta aac agt att gtt cac aag gcc aaa ata 5655
Gly Lys Arg Lys Gly Leu Asn Ser Ile Val His Lys Ala Lys Ile
1480 1485 1490
gag cag tac ttt gat aaa gca caa aat aca aat tcc ctc tgg cac 5700
Glu Gln Tyr Phe Asp Lys Ala Gln Asn Thr Asn Ser Leu Trp His
1495 1500 1505
agt ggg gat gtg tgg aaa aaa aat gaa gtc aaa gac ctc ctg cgt 5745
Ser Gly Asp Val Trp Lys Lys Asn Glu Val Lys Asp Leu Leu Arg
1510 1515 1520
cgt cta act ggt cag gct gaa ggc aag cta atc tct gta gaa tat 5790
Arg Leu Thr Gly Gln Ala Glu Gly Lys Leu Ile Ser Val Glu Tyr
1525 1530 1535
gga aca gag gaa aaa ata aaa ata cca gta ata tct gtt tat tca 5835
Gly Thr Glu Glu Lys Ile Lys Ile Pro Val Ile Ser Val Tyr Ser
1540 1545 1550
ggt cca ctc aga agt ggt agg aac ata gaa aga gtg tct ttc tac 5880
Gly Pro Leu Arg Ser Gly Arg Asn Ile Glu Arg Val Ser Phe Tyr
1555 1560 1565
cta gga ttt tcc att gaa ggc cct ctg gca tat gat ata gaa gta 5925
Leu Gly Phe Ser Ile Glu Gly Pro Leu Ala Tyr Asp Ile Glu Val
1570 1575 1580
att taa gacaatacat cacctgtagt tcaaatatgt ttatttatat ctttatgatt 5981
Ile
ttattctctc tctctattct catggcactt tcataacatt atggctaacc tctaattaca 6041
gattttgctt ttgcctccct gaatgaatta caagcctttt taagatatga aatatgccta 6101
cccgcagagc ttggcacaaa gtggagtcaa tcttttaatg ttttaaatat gcattttcag 6161
actcaaataa ttaagaagtt tcattgatat ccactggtca catcataact gtctataggg 6221
caataaaatc tgtgttaaac tcaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa 6281
aaaaaaaa 6289


24
1584
PRT
Homo sapiens

24
Met Ser Lys Gln Val Ser Leu Pro Glu Met Ile Lys Asp Trp Thr Lys
1 5 10 15
Glu His Val Lys Lys Trp Val Asn Glu Asp Leu Lys Ile Asn Glu Gln
20 25 30
Tyr Gly Gln Ile Leu Leu Ser Glu Glu Val Thr Gly Leu Val Leu Gln
35 40 45
Glu Leu Thr Glu Lys Asp Leu Val Glu Met Gly Leu Pro Trp Gly Pro
50 55 60
Ala Leu Leu Ile Lys Arg Ser Tyr Asn Lys Leu Asn Ser Lys Ser Pro
65 70 75 80
Glu Ser Asp Asn His Asp Pro Gly Gln Leu Asp Asn Ser Lys Pro Ser
85 90 95
Lys Thr Glu His Gln Lys Asn Pro Lys His Thr Lys Lys Glu Glu Glu
100 105 110
Asn Ser Met Ser Ser Asn Ile Asp Tyr Asp Pro Arg Glu Ile Arg Asp
115 120 125
Ile Lys Gln Glu Glu Ser Ile Leu Met Lys Glu Asn Val Leu Asp Glu
130 135 140
Val Ala Asn Ala Lys His Lys Lys Lys Gly Lys Leu Lys Pro Glu Gln
145 150 155 160
Leu Thr Cys Met Pro Tyr Pro Phe Asp Gln Phe His Asp Ser His Arg
165 170 175
Tyr Ile Glu His Tyr Thr Leu Gln Pro Glu Thr Gly Ala Leu Asn Leu
180 185 190
Ile Asp Pro Ile His Glu Phe Lys Ala Leu Thr Asn Thr Glu Thr Ala
195 200 205
Thr Glu Val Asp Ile Lys Met Lys Phe Ser Asn Glu Val Phe Arg Phe
210 215 220
Ala Ser Ala Cys Met Asn Ser Arg Thr Asn Gly Thr Ile His Phe Gly
225 230 235 240
Val Lys Asp Lys Pro His Gly Glu Ile Val Gly Val Lys Ile Thr Ser
245 250 255
Lys Ala Ala Phe Ile Asp His Phe Asn Val Met Ile Lys Lys Tyr Phe
260 265 270
Glu Glu Ser Glu Ile Asn Glu Ala Lys Lys Cys Ile Arg Glu Pro Arg
275 280 285
Phe Val Glu Val Leu Leu Gln Asn Asn Thr Pro Ser Asp Arg Phe Val
290 295 300
Ile Glu Val Asp Thr Ile Pro Lys His Ser Ile Cys Asn Asp Lys Tyr
305 310 315 320
Phe Tyr Ile Gln Met Gln Ile Cys Lys Asp Lys Ile Trp Lys Gln Asn
325 330 335
Gln Asn Leu Ser Leu Phe Val Arg Glu Gly Ala Ser Ser Arg Asp Ile
340 345 350
Leu Ala Asn Ser Lys Gln Arg Asp Val Asp Phe Lys Ala Phe Leu Gln
355 360 365
Asn Leu Lys Ser Leu Val Ala Ser Arg Lys Glu Ala Glu Glu Glu Tyr
370 375 380
Gly Met Lys Ala Met Lys Lys Glu Ser Glu Gly Leu Lys Leu Val Lys
385 390 395 400
Leu Leu Ile Gly Asn Arg Asp Ser Leu Asp Asn Ser Tyr Tyr Asp Trp
405 410 415
Tyr Ile Leu Val Thr Asn Lys Cys His Pro Asn Gln Ile Lys His Leu
420 425 430
Asp Phe Leu Lys Glu Ile Lys Trp Phe Ala Val Leu Glu Phe Asp Pro
435 440 445
Glu Ser Met Ile Asn Gly Val Val Lys Ala Tyr Lys Glu Ser Arg Val
450 455 460
Ala Asn Leu His Phe Pro Asn Gln Tyr Glu Asp Lys Thr Thr Asn Met
465 470 475 480
Trp Glu Lys Ile Ser Thr Leu Asn Leu Tyr Gln Gln Pro Ser Trp Ile
485 490 495
Phe Cys Asn Gly Arg Ser Asp Leu Lys Ser Glu Thr Tyr Lys Pro Leu
500 505 510
Glu Pro His Leu Trp Gln Arg Glu Arg Ala Ser Glu Val Arg Lys Leu
515 520 525
Ile Leu Phe Leu Thr Asp Glu Asn Ile Met Thr Arg Gly Lys Phe Leu
530 535 540
Val Val Phe Leu Leu Leu Ser Ser Val Glu Ser Pro Gly Asp Pro Leu
545 550 555 560
Ile Glu Thr Phe Trp Ala Phe Tyr Gln Ala Leu Lys Gly Met Glu Asn
565 570 575
Met Leu Cys Ile Ser Val Asn Ser His Ile Tyr Gln Arg Trp Lys Asp
580 585 590
Leu Leu Gln Thr Arg Thr Lys Met Glu Asp Glu Leu Thr Asn His Ser
595 600 605
Ile Ser Thr Leu Asn Ile Glu Leu Val Asn Ser Thr Ile Leu Lys Leu
610 615 620
Lys Ser Val Thr Arg Ser Ser Arg Arg Phe Leu Pro Ala Arg Gly Ser
625 630 635 640
Ser Ser Val Ile Leu Glu Lys Lys Lys Glu Asp Val Leu Thr Ala Leu
645 650 655
Glu Ile Leu Cys Glu Asn Glu Cys Thr Glu Thr Asp Ile Glu Lys Asp
660 665 670
Lys Ser Lys Phe Leu Glu Phe Lys Lys Ser Lys Glu Glu His Phe Tyr
675 680 685
Arg Gly Gly Lys Val Ser Trp Trp Asn Phe Tyr Phe Ser Ser Glu Asn
690 695 700
Tyr Ser Ser Asp Phe Val Lys Arg Asp Ser Tyr Glu Lys Leu Lys Asp
705 710 715 720
Leu Ile His Cys Trp Ala Glu Ser Pro Lys Pro Ile Phe Ala Lys Ile
725 730 735
Ile Asn Leu Tyr His His Pro Gly Cys Gly Gly Thr Thr Leu Ala Met
740 745 750
His Val Leu Trp Asp Leu Lys Lys Asn Phe Arg Cys Ala Val Leu Lys
755 760 765
Asn Lys Thr Thr Asp Phe Ala Glu Ile Ala Glu Gln Val Ile Asn Leu
770 775 780
Val Thr Tyr Arg Ala Lys Ser His Gln Asp Tyr Ile Pro Val Leu Leu
785 790 795 800
Leu Val Asp Asp Phe Glu Glu Gln Glu Asn Val Tyr Phe Leu Gln Asn
805 810 815
Ala Ile His Ser Val Leu Ala Glu Lys Asp Leu Arg Tyr Glu Lys Thr
820 825 830
Leu Val Ile Ile Leu Asn Cys Met Arg Ser Arg Asn Pro Asp Glu Ser
835 840 845
Ala Lys Leu Ala Asp Ser Ile Ala Leu Asn Tyr Gln Leu Ser Ser Lys
850 855 860
Glu Gln Arg Ala Phe Gly Ala Lys Leu Lys Glu Ile Glu Lys Gln His
865 870 875 880
Lys Asn Cys Glu Asn Phe Tyr Ser Phe Met Ile Met Lys Ser Asn Phe
885 890 895
Asp Glu Thr Tyr Ile Glu Asn Val Val Arg Asn Ile Leu Lys Gly Gln
900 905 910
Asp Val Asp Ser Lys Glu Ala Gln Leu Ile Ser Phe Leu Ala Leu Leu
915 920 925
Ser Ser Tyr Val Thr Asp Ser Thr Ile Ser Val Ser Gln Cys Glu Ile
930 935 940
Phe Leu Gly Ile Ile Tyr Thr Ser Thr Pro Trp Glu Pro Glu Ser Leu
945 950 955 960
Glu Asp Lys Met Gly Thr Tyr Ser Thr Leu Leu Ile Lys Thr Glu Val
965 970 975
Ala Glu Tyr Gly Arg Tyr Thr Gly Val Arg Ile Ile His Pro Leu Ile
980 985 990
Ala Leu Tyr Cys Leu Lys Glu Leu Glu Arg Ser Tyr His Leu Asp Lys
995 1000 1005
Cys Gln Ile Ala Leu Asn Ile Leu Glu Glu Asn Leu Phe Tyr Asp
1010 1015 1020
Ser Gly Ile Gly Arg Asp Lys Phe Gln His Asp Val Gln Thr Leu
1025 1030 1035
Leu Leu Thr Arg Gln Arg Lys Val Tyr Gly Asp Glu Thr Asp Thr
1040 1045 1050
Leu Phe Ser Pro Leu Met Glu Ala Leu Gln Asn Lys Asp Ile Glu
1055 1060 1065
Lys Val Leu Ser Ala Gly Ser Arg Arg Phe Pro Gln Asn Ala Phe
1070 1075 1080
Ile Cys Gln Ala Leu Ala Arg His Phe Tyr Ile Lys Glu Lys Asp
1085 1090 1095
Phe Asn Thr Ala Leu Asp Trp Ala Arg Gln Ala Lys Met Lys Ala
1100 1105 1110
Pro Lys Asn Ser Tyr Ile Ser Asp Thr Leu Gly Gln Val Tyr Lys
1115 1120 1125
Ser Glu Ile Lys Trp Trp Leu Asp Gly Asn Lys Asn Cys Arg Ser
1130 1135 1140
Ile Thr Val Asn Asp Leu Thr His Leu Leu Glu Ala Ala Glu Lys
1145 1150 1155
Ala Ser Arg Ala Phe Lys Glu Ser Gln Arg Gln Thr Asp Ser Lys
1160 1165 1170
Asn Tyr Glu Thr Glu Asn Trp Ser Pro Gln Lys Ser Gln Arg Arg
1175 1180 1185
Tyr Asp Met Tyr Asn Thr Ala Cys Phe Leu Gly Glu Ile Glu Val
1190 1195 1200
Gly Leu Tyr Thr Ile Gln Ile Leu Gln Leu Thr Pro Phe Phe His
1205 1210 1215
Lys Glu Asn Glu Leu Ser Lys Lys His Met Val Gln Phe Leu Ser
1220 1225 1230
Gly Lys Trp Thr Ile Pro Pro Asp Pro Arg Asn Glu Cys Tyr Leu
1235 1240 1245
Ala Leu Ser Lys Phe Thr Ser His Leu Lys Asn Leu Gln Ser Asp
1250 1255 1260
Leu Lys Arg Cys Phe Asp Phe Phe Ile Asp Tyr Met Val Leu Leu
1265 1270 1275
Lys Met Arg Tyr Thr Gln Lys Glu Ile Ala Glu Ile Met Leu Ser
1280 1285 1290
Lys Lys Val Ser Arg Cys Phe Arg Lys Tyr Thr Glu Leu Phe Cys
1295 1300 1305
His Leu Asp Pro Cys Leu Leu Gln Ser Lys Glu Ser Gln Leu Leu
1310 1315 1320
Gln Glu Glu Asn Cys Arg Lys Lys Leu Glu Ala Leu Arg Ala Asp
1325 1330 1335
Arg Phe Ala Gly Leu Leu Glu Tyr Leu Asn Pro Asn Tyr Lys Asp
1340 1345 1350
Ala Thr Thr Met Glu Ser Ile Val Asn Glu Tyr Ala Phe Leu Leu
1355 1360 1365
Gln Gln Asn Ser Lys Lys Pro Met Thr Asn Glu Lys Gln Asn Ser
1370 1375 1380
Ile Leu Ala Asn Ile Ile Leu Ser Cys Leu Lys Pro Asn Ser Lys
1385 1390 1395
Leu Ile Gln Pro Leu Thr Thr Leu Lys Lys Gln Leu Arg Glu Val
1400 1405 1410
Leu Gln Phe Val Gly Leu Ser His Gln Tyr Pro Gly Pro Tyr Phe
1415 1420 1425
Leu Ala Cys Leu Leu Phe Trp Pro Glu Asn Gln Glu Leu Asp Gln
1430 1435 1440
Asp Ser Lys Leu Ile Glu Lys Tyr Val Ser Ser Leu Asn Arg Ser
1445 1450 1455
Phe Arg Gly Gln Tyr Lys Arg Met Cys Arg Ser Lys Gln Ala Ser
1460 1465 1470
Thr Leu Phe Tyr Leu Gly Lys Arg Lys Gly Leu Asn Ser Ile Val
1475 1480 1485
His Lys Ala Lys Ile Glu Gln Tyr Phe Asp Lys Ala Gln Asn Thr
1490 1495 1500
Asn Ser Leu Trp His Ser Gly Asp Val Trp Lys Lys Asn Glu Val
1505 1510 1515
Lys Asp Leu Leu Arg Arg Leu Thr Gly Gln Ala Glu Gly Lys Leu
1520 1525 1530
Ile Ser Val Glu Tyr Gly Thr Glu Glu Lys Ile Lys Ile Pro Val
1535 1540 1545
Ile Ser Val Tyr Ser Gly Pro Leu Arg Ser Gly Arg Asn Ile Glu
1550 1555 1560
Arg Val Ser Phe Tyr Leu Gly Phe Ser Ile Glu Gly Pro Leu Ala
1565 1570 1575
Tyr Asp Ile Glu Val Ile
1580


25
3345
DNA
Homo sapiens

CDS
(67)..(3108)


25
cttctgccag cagaagcagc agccgcagca cctgagccgc tactgccgct cactcaggac 60
aacgct atg gct gag cct ggg cac agc cac cat ctc tcc gcc aga gtc 108
Met Ala Glu Pro Gly His Ser His His Leu Ser Ala Arg Val
1 5 10
agg gga aga act gag agg cgc ata ccc cgg ctg tgg cgg ctg ctg ctc 156
Arg Gly Arg Thr Glu Arg Arg Ile Pro Arg Leu Trp Arg Leu Leu Leu
15 20 25 30
tgg gct ggg acc gcc ttc cag gtg acc cag gga acg gga ccg gag ctt 204
Trp Ala Gly Thr Ala Phe Gln Val Thr Gln Gly Thr Gly Pro Glu Leu
35 40 45
cac gcc tgc aaa gag tct gag tac cac tat gag tac acg gcg tgt gac 252
His Ala Cys Lys Glu Ser Glu Tyr His Tyr Glu Tyr Thr Ala Cys Asp
50 55 60
agc acg ggt tcc agg tgg agg gtc gcc gtg ccg cat acc ccg ggc ctg 300
Ser Thr Gly Ser Arg Trp Arg Val Ala Val Pro His Thr Pro Gly Leu
65 70 75
tgc acc agc ctg cct gac ccc gtc aag ggc acc gag tgc tcc ttc tcc 348
Cys Thr Ser Leu Pro Asp Pro Val Lys Gly Thr Glu Cys Ser Phe Ser
80 85 90
tgc aac gcc ggg gag ttt ctg gat atg aag gac cag tca tgt aag cca 396
Cys Asn Ala Gly Glu Phe Leu Asp Met Lys Asp Gln Ser Cys Lys Pro
95 100 105 110
tgc gct gag ggc cgc tac tcc ctc ggc aca ggc att cgg ttt gat gag 444
Cys Ala Glu Gly Arg Tyr Ser Leu Gly Thr Gly Ile Arg Phe Asp Glu
115 120 125
tgg gat gag ctg ccc cat ggc ttt gcc agc ctc tca gcc aac atg gag 492
Trp Asp Glu Leu Pro His Gly Phe Ala Ser Leu Ser Ala Asn Met Glu
130 135 140
ctg gat gac agt gct gct gag tcc acc ggg aac tgt act tcg tcc aag 540
Leu Asp Asp Ser Ala Ala Glu Ser Thr Gly Asn Cys Thr Ser Ser Lys
145 150 155
tgg gtt ccc cgg ggc gac tac atc gcc tcc aac acg gac gaa tgc aca 588
Trp Val Pro Arg Gly Asp Tyr Ile Ala Ser Asn Thr Asp Glu Cys Thr
160 165 170
gcc aca ctg atg tac gcc gtc aac ctg aag caa tct ggc acc gtt aac 636
Ala Thr Leu Met Tyr Ala Val Asn Leu Lys Gln Ser Gly Thr Val Asn
175 180 185 190
ttc gaa tac tac tat cca gac tcc agc atc atc ttt gag ttt ttc gtt 684
Phe Glu Tyr Tyr Tyr Pro Asp Ser Ser Ile Ile Phe Glu Phe Phe Val
195 200 205
cag aat gac cag tgc cag ccc aat gca gat gac tcc agg tgg atg aag 732
Gln Asn Asp Gln Cys Gln Pro Asn Ala Asp Asp Ser Arg Trp Met Lys
210 215 220
acc aca gag aaa gga tgg gaa ttc cac agt gtg gag cta aat cga ggc 780
Thr Thr Glu Lys Gly Trp Glu Phe His Ser Val Glu Leu Asn Arg Gly
225 230 235
aat aat gtc ctc tat tgg aga acc aca gcc ttc tca gta tgg acc aaa 828
Asn Asn Val Leu Tyr Trp Arg Thr Thr Ala Phe Ser Val Trp Thr Lys
240 245 250
gta ccc aag cct gtg ctg gtg aga aac att gcc ata aca ggg gtg gcc 876
Val Pro Lys Pro Val Leu Val Arg Asn Ile Ala Ile Thr Gly Val Ala
255 260 265 270
tac act tca gaa tgc ttc ccc tgc aaa cct ggc acg tat gca gac aag 924
Tyr Thr Ser Glu Cys Phe Pro Cys Lys Pro Gly Thr Tyr Ala Asp Lys
275 280 285
cag ggc tcc tct ttc tgc aaa ctt tgc cca gcc aac tct tat tca aat 972
Gln Gly Ser Ser Phe Cys Lys Leu Cys Pro Ala Asn Ser Tyr Ser Asn
290 295 300
aaa gga gaa act tct tgc cac cag tgt gac cct gac aaa tac tca gag 1020
Lys Gly Glu Thr Ser Cys His Gln Cys Asp Pro Asp Lys Tyr Ser Glu
305 310 315
aaa gga tct tct tcc tgt aac gtg cgc cca gct tgc aca gac aaa gat 1068
Lys Gly Ser Ser Ser Cys Asn Val Arg Pro Ala Cys Thr Asp Lys Asp
320 325 330
tat ttc tac aca cac acg gcc tgc gat gcc aac gga gag aca caa ctc 1116
Tyr Phe Tyr Thr His Thr Ala Cys Asp Ala Asn Gly Glu Thr Gln Leu
335 340 345 350
atg tac aaa tgg gcc aag ccg aaa atc tgt agc gag gac ctt gag ggg 1164
Met Tyr Lys Trp Ala Lys Pro Lys Ile Cys Ser Glu Asp Leu Glu Gly
355 360 365
gca gtg aag ctg cct gcc tct ggt gtg aag acc cac tgc cca ccc tgc 1212
Ala Val Lys Leu Pro Ala Ser Gly Val Lys Thr His Cys Pro Pro Cys
370 375 380
aac cca ggc ttc ttc aaa acc aac aac agc acc tgc cag ccc tgc cca 1260
Asn Pro Gly Phe Phe Lys Thr Asn Asn Ser Thr Cys Gln Pro Cys Pro
385 390 395
tat ggt tcc tac tcc aat ggc tca gac tgt acc cgc tgc cct gca ggg 1308
Tyr Gly Ser Tyr Ser Asn Gly Ser Asp Cys Thr Arg Cys Pro Ala Gly
400 405 410
act gaa cct gct gtg gga ttt gaa tac aaa tgg tgg aac acg ctg ccc 1356
Thr Glu Pro Ala Val Gly Phe Glu Tyr Lys Trp Trp Asn Thr Leu Pro
415 420 425 430
aca aac atg gaa acg acc gtt ctc agt ggg atc aac ttc gag tac aag 1404
Thr Asn Met Glu Thr Thr Val Leu Ser Gly Ile Asn Phe Glu Tyr Lys
435 440 445
ggc atg aca ggc tgg gag gtg gct ggt gat cac att tac aca gct gct 1452
Gly Met Thr Gly Trp Glu Val Ala Gly Asp His Ile Tyr Thr Ala Ala
450 455 460
gga gcc tca gac aat gac ttc atg att ctc act ctg gtt gtg cca gga 1500
Gly Ala Ser Asp Asn Asp Phe Met Ile Leu Thr Leu Val Val Pro Gly
465 470 475
ttt aga cct ccg cag tcg gtg atg gca gac aca gag aat aaa gag gtg 1548
Phe Arg Pro Pro Gln Ser Val Met Ala Asp Thr Glu Asn Lys Glu Val
480 485 490
gcc aga atc aca ttt gtc ttt gag acc ctc tgt tct gtg aac tgt gag 1596
Ala Arg Ile Thr Phe Val Phe Glu Thr Leu Cys Ser Val Asn Cys Glu
495 500 505 510
ctc tac ttc atg gtg ggt gtg aat tct agg acc aac act cct gtg gag 1644
Leu Tyr Phe Met Val Gly Val Asn Ser Arg Thr Asn Thr Pro Val Glu
515 520 525
acg tgg aaa ggt tcc aaa ggc aaa cag tcc tat acc tac atc att gag 1692
Thr Trp Lys Gly Ser Lys Gly Lys Gln Ser Tyr Thr Tyr Ile Ile Glu
530 535 540
gag aac act acc acg agc ttc acc tgg gcc ttc cag agg acc act ttt 1740
Glu Asn Thr Thr Thr Ser Phe Thr Trp Ala Phe Gln Arg Thr Thr Phe
545 550 555
cat gag gca agc agg aag tac acc aat gac gtt gcc aag atc tac tcc 1788
His Glu Ala Ser Arg Lys Tyr Thr Asn Asp Val Ala Lys Ile Tyr Ser
560 565 570
atc aat gtc acc aat gtt atg aat ggc gtg gcc tcc tac tgc cgt ccc 1836
Ile Asn Val Thr Asn Val Met Asn Gly Val Ala Ser Tyr Cys Arg Pro
575 580 585 590
tgt gcc cta gaa gcc tct gat gtg ggc tcc tcc tgc acc tct tgt cct 1884
Cys Ala Leu Glu Ala Ser Asp Val Gly Ser Ser Cys Thr Ser Cys Pro
595 600 605
gct ggt tac tat att gac cga gat tca gga acc tgc cac tcc tgc ccc 1932
Ala Gly Tyr Tyr Ile Asp Arg Asp Ser Gly Thr Cys His Ser Cys Pro
610 615 620
cct aac aca att ctg aaa gcc cac cag cct tat ggt gtc cag gcc tgt 1980
Pro Asn Thr Ile Leu Lys Ala His Gln Pro Tyr Gly Val Gln Ala Cys
625 630 635
gtg ccc tgt ggt cca ggg acc aag aac aac aag atc cac tct ctg tgc 2028
Val Pro Cys Gly Pro Gly Thr Lys Asn Asn Lys Ile His Ser Leu Cys
640 645 650
tac aat gat tgc acc ttc tca cgc aac act cca acc agg act ttc aac 2076
Tyr Asn Asp Cys Thr Phe Ser Arg Asn Thr Pro Thr Arg Thr Phe Asn
655 660 665 670
tac aac ttc tcc gct ttg gca aac acc gtc act ctt gct gga ggg cca 2124
Tyr Asn Phe Ser Ala Leu Ala Asn Thr Val Thr Leu Ala Gly Gly Pro
675 680 685
agc ttc act tcc aaa ggg ttg aaa tac ttc cat cac ttt acc ctc agt 2172
Ser Phe Thr Ser Lys Gly Leu Lys Tyr Phe His His Phe Thr Leu Ser
690 695 700
ctc tgt gga aac cag ggt agg aaa atg tct gtg tgc acc gac aat gtc 2220
Leu Cys Gly Asn Gln Gly Arg Lys Met Ser Val Cys Thr Asp Asn Val
705 710 715
act gac ctc cgg att cct gag ggt gag tca ggg ttc tcc aaa tct atc 2268
Thr Asp Leu Arg Ile Pro Glu Gly Glu Ser Gly Phe Ser Lys Ser Ile
720 725 730
aca gcc tac gtc tgc cag gca gtc atc atc ccc cca gag gtg aca ggc 2316
Thr Ala Tyr Val Cys Gln Ala Val Ile Ile Pro Pro Glu Val Thr Gly
735 740 745 750
tac aag gcc ggg gtt tcc tca cag cct gtc agc ctt gct gat cga ctt 2364
Tyr Lys Ala Gly Val Ser Ser Gln Pro Val Ser Leu Ala Asp Arg Leu
755 760 765
att ggg gtg aca aca gat atg act ctg gat gga atc acc tcc cca gct 2412
Ile Gly Val Thr Thr Asp Met Thr Leu Asp Gly Ile Thr Ser Pro Ala
770 775 780
gaa ctt ttc cac ctg gag tcc ttg gga ata ccg gac gtg atc ttc ttt 2460
Glu Leu Phe His Leu Glu Ser Leu Gly Ile Pro Asp Val Ile Phe Phe
785 790 795
tat agg tcc aat gat gtg acc cag tcc tgc agt tct ggg aga tca acc 2508
Tyr Arg Ser Asn Asp Val Thr Gln Ser Cys Ser Ser Gly Arg Ser Thr
800 805 810
acc atc cgc gtc agg tgc agt cca cag aaa act gtc cct gga agt ttg 2556
Thr Ile Arg Val Arg Cys Ser Pro Gln Lys Thr Val Pro Gly Ser Leu
815 820 825 830
ctg ctg cca gga acg tgc tca gat ggg acc tgt gat ggc tgc aac ttc 2604
Leu Leu Pro Gly Thr Cys Ser Asp Gly Thr Cys Asp Gly Cys Asn Phe
835 840 845
cac ttc ctg tgg gag agc gcg gct gct tgc ccg ctc tgc tca gtg gct 2652
His Phe Leu Trp Glu Ser Ala Ala Ala Cys Pro Leu Cys Ser Val Ala
850 855 860
gac tac cat gct atc gtc agc agc tgt gtg gct ggg atc cag aag act 2700
Asp Tyr His Ala Ile Val Ser Ser Cys Val Ala Gly Ile Gln Lys Thr
865 870 875
act tac gtg tgg cga gaa ccc aag cta tgc tct ggt ggc att tct ctg 2748
Thr Tyr Val Trp Arg Glu Pro Lys Leu Cys Ser Gly Gly Ile Ser Leu
880 885 890
cct gag cag aga gtc acc atc tgc aaa acc ata gat ttc tgg ctg aaa 2796
Pro Glu Gln Arg Val Thr Ile Cys Lys Thr Ile Asp Phe Trp Leu Lys
895 900 905 910
gtg ggc atc tct gca ggc acc tgt act gcc atc ctg ctc acc gtc ttg 2844
Val Gly Ile Ser Ala Gly Thr Cys Thr Ala Ile Leu Leu Thr Val Leu
915 920 925
acc tgc tac ttt tgg aaa aag aat caa aaa cta gag tac aag tac tcc 2892
Thr Cys Tyr Phe Trp Lys Lys Asn Gln Lys Leu Glu Tyr Lys Tyr Ser
930 935 940
aag ctg gtg atg aat gct act ctc aag gac tgt gac ctg cca gca gct 2940
Lys Leu Val Met Asn Ala Thr Leu Lys Asp Cys Asp Leu Pro Ala Ala
945 950 955
gac agc tgc gcc atc atg gaa ggc gag gat gta gag gac gac ctc atc 2988
Asp Ser Cys Ala Ile Met Glu Gly Glu Asp Val Glu Asp Asp Leu Ile
960 965 970
ttt acc agc aag aag tca ctc ttt ggg aag atc aaa tca ttt acc tcc 3036
Phe Thr Ser Lys Lys Ser Leu Phe Gly Lys Ile Lys Ser Phe Thr Ser
975 980 985 990
aag agg act cct gat gga ttt gac tca gtg ccg ctg aag aca tcc tca 3084
Lys Arg Thr Pro Asp Gly Phe Asp Ser Val Pro Leu Lys Thr Ser Ser
995 1000 1005
gga ggc cca gac atg gac ctg tga gaggcactgc ctgcctcacc tgcctcctca 3138
Gly Gly Pro Asp Met Asp Leu
1010
ccttgcatag cacctttgca agcctgcggc gatttgggtg ccagcatcct gcaacaccca 3198
ctgctggaaa tctcttcatt gtggccttat cagatgtttg aatttcagat ctttttttat 3258
agagtaccca aaccctcctt tctgcttgcc tcaaacctgc caaatatacc cacactttgt 3318
ttgtaaatta aaaaaaaaaa aaaaaaa 3345


26
1013
PRT
Homo sapiens

26
Met Ala Glu Pro Gly His Ser His His Leu Ser Ala Arg Val Arg Gly
1 5 10 15
Arg Thr Glu Arg Arg Ile Pro Arg Leu Trp Arg Leu Leu Leu Trp Ala
20 25 30
Gly Thr Ala Phe Gln Val Thr Gln Gly Thr Gly Pro Glu Leu His Ala
35 40 45
Cys Lys Glu Ser Glu Tyr His Tyr Glu Tyr Thr Ala Cys Asp Ser Thr
50 55 60
Gly Ser Arg Trp Arg Val Ala Val Pro His Thr Pro Gly Leu Cys Thr
65 70 75 80
Ser Leu Pro Asp Pro Val Lys Gly Thr Glu Cys Ser Phe Ser Cys Asn
85 90 95
Ala Gly Glu Phe Leu Asp Met Lys Asp Gln Ser Cys Lys Pro Cys Ala
100 105 110
Glu Gly Arg Tyr Ser Leu Gly Thr Gly Ile Arg Phe Asp Glu Trp Asp
115 120 125
Glu Leu Pro His Gly Phe Ala Ser Leu Ser Ala Asn Met Glu Leu Asp
130 135 140
Asp Ser Ala Ala Glu Ser Thr Gly Asn Cys Thr Ser Ser Lys Trp Val
145 150 155 160
Pro Arg Gly Asp Tyr Ile Ala Ser Asn Thr Asp Glu Cys Thr Ala Thr
165 170 175
Leu Met Tyr Ala Val Asn Leu Lys Gln Ser Gly Thr Val Asn Phe Glu
180 185 190
Tyr Tyr Tyr Pro Asp Ser Ser Ile Ile Phe Glu Phe Phe Val Gln Asn
195 200 205
Asp Gln Cys Gln Pro Asn Ala Asp Asp Ser Arg Trp Met Lys Thr Thr
210 215 220
Glu Lys Gly Trp Glu Phe His Ser Val Glu Leu Asn Arg Gly Asn Asn
225 230 235 240
Val Leu Tyr Trp Arg Thr Thr Ala Phe Ser Val Trp Thr Lys Val Pro
245 250 255
Lys Pro Val Leu Val Arg Asn Ile Ala Ile Thr Gly Val Ala Tyr Thr
260 265 270
Ser Glu Cys Phe Pro Cys Lys Pro Gly Thr Tyr Ala Asp Lys Gln Gly
275 280 285
Ser Ser Phe Cys Lys Leu Cys Pro Ala Asn Ser Tyr Ser Asn Lys Gly
290 295 300
Glu Thr Ser Cys His Gln Cys Asp Pro Asp Lys Tyr Ser Glu Lys Gly
305 310 315 320
Ser Ser Ser Cys Asn Val Arg Pro Ala Cys Thr Asp Lys Asp Tyr Phe
325 330 335
Tyr Thr His Thr Ala Cys Asp Ala Asn Gly Glu Thr Gln Leu Met Tyr
340 345 350
Lys Trp Ala Lys Pro Lys Ile Cys Ser Glu Asp Leu Glu Gly Ala Val
355 360 365
Lys Leu Pro Ala Ser Gly Val Lys Thr His Cys Pro Pro Cys Asn Pro
370 375 380
Gly Phe Phe Lys Thr Asn Asn Ser Thr Cys Gln Pro Cys Pro Tyr Gly
385 390 395 400
Ser Tyr Ser Asn Gly Ser Asp Cys Thr Arg Cys Pro Ala Gly Thr Glu
405 410 415
Pro Ala Val Gly Phe Glu Tyr Lys Trp Trp Asn Thr Leu Pro Thr Asn
420 425 430
Met Glu Thr Thr Val Leu Ser Gly Ile Asn Phe Glu Tyr Lys Gly Met
435 440 445
Thr Gly Trp Glu Val Ala Gly Asp His Ile Tyr Thr Ala Ala Gly Ala
450 455 460
Ser Asp Asn Asp Phe Met Ile Leu Thr Leu Val Val Pro Gly Phe Arg
465 470 475 480
Pro Pro Gln Ser Val Met Ala Asp Thr Glu Asn Lys Glu Val Ala Arg
485 490 495
Ile Thr Phe Val Phe Glu Thr Leu Cys Ser Val Asn Cys Glu Leu Tyr
500 505 510
Phe Met Val Gly Val Asn Ser Arg Thr Asn Thr Pro Val Glu Thr Trp
515 520 525
Lys Gly Ser Lys Gly Lys Gln Ser Tyr Thr Tyr Ile Ile Glu Glu Asn
530 535 540
Thr Thr Thr Ser Phe Thr Trp Ala Phe Gln Arg Thr Thr Phe His Glu
545 550 555 560
Ala Ser Arg Lys Tyr Thr Asn Asp Val Ala Lys Ile Tyr Ser Ile Asn
565 570 575
Val Thr Asn Val Met Asn Gly Val Ala Ser Tyr Cys Arg Pro Cys Ala
580 585 590
Leu Glu Ala Ser Asp Val Gly Ser Ser Cys Thr Ser Cys Pro Ala Gly
595 600 605
Tyr Tyr Ile Asp Arg Asp Ser Gly Thr Cys His Ser Cys Pro Pro Asn
610 615 620
Thr Ile Leu Lys Ala His Gln Pro Tyr Gly Val Gln Ala Cys Val Pro
625 630 635 640
Cys Gly Pro Gly Thr Lys Asn Asn Lys Ile His Ser Leu Cys Tyr Asn
645 650 655
Asp Cys Thr Phe Ser Arg Asn Thr Pro Thr Arg Thr Phe Asn Tyr Asn
660 665 670
Phe Ser Ala Leu Ala Asn Thr Val Thr Leu Ala Gly Gly Pro Ser Phe
675 680 685
Thr Ser Lys Gly Leu Lys Tyr Phe His His Phe Thr Leu Ser Leu Cys
690 695 700
Gly Asn Gln Gly Arg Lys Met Ser Val Cys Thr Asp Asn Val Thr Asp
705 710 715 720
Leu Arg Ile Pro Glu Gly Glu Ser Gly Phe Ser Lys Ser Ile Thr Ala
725 730 735
Tyr Val Cys Gln Ala Val Ile Ile Pro Pro Glu Val Thr Gly Tyr Lys
740 745 750
Ala Gly Val Ser Ser Gln Pro Val Ser Leu Ala Asp Arg Leu Ile Gly
755 760 765
Val Thr Thr Asp Met Thr Leu Asp Gly Ile Thr Ser Pro Ala Glu Leu
770 775 780
Phe His Leu Glu Ser Leu Gly Ile Pro Asp Val Ile Phe Phe Tyr Arg
785 790 795 800
Ser Asn Asp Val Thr Gln Ser Cys Ser Ser Gly Arg Ser Thr Thr Ile
805 810 815
Arg Val Arg Cys Ser Pro Gln Lys Thr Val Pro Gly Ser Leu Leu Leu
820 825 830
Pro Gly Thr Cys Ser Asp Gly Thr Cys Asp Gly Cys Asn Phe His Phe
835 840 845
Leu Trp Glu Ser Ala Ala Ala Cys Pro Leu Cys Ser Val Ala Asp Tyr
850 855 860
His Ala Ile Val Ser Ser Cys Val Ala Gly Ile Gln Lys Thr Thr Tyr
865 870 875 880
Val Trp Arg Glu Pro Lys Leu Cys Ser Gly Gly Ile Ser Leu Pro Glu
885 890 895
Gln Arg Val Thr Ile Cys Lys Thr Ile Asp Phe Trp Leu Lys Val Gly
900 905 910
Ile Ser Ala Gly Thr Cys Thr Ala Ile Leu Leu Thr Val Leu Thr Cys
915 920 925
Tyr Phe Trp Lys Lys Asn Gln Lys Leu Glu Tyr Lys Tyr Ser Lys Leu
930 935 940
Val Met Asn Ala Thr Leu Lys Asp Cys Asp Leu Pro Ala Ala Asp Ser
945 950 955 960
Cys Ala Ile Met Glu Gly Glu Asp Val Glu Asp Asp Leu Ile Phe Thr
965 970 975
Ser Lys Lys Ser Leu Phe Gly Lys Ile Lys Ser Phe Thr Ser Lys Arg
980 985 990
Thr Pro Asp Gly Phe Asp Ser Val Pro Leu Lys Thr Ser Ser Gly Gly
995 1000 1005
Pro Asp Met Asp Leu
1010


27
2998
DNA
Homo sapiens

CDS
(218)..(733)


27
gttcgtcctg ggactgcact tgctcccgtc gggtcgcccg gcttcaccgg acccgcaggc 60
tcccggggca gggccggggc cagagctcgc gtgtcggcgg gacatgcgct gcgtcgcctc 120
taacctcggg ctgtgctctt tttccaggtg gcccgccggt ttctgagcct tctgccctgc 180
ggggacacgg tctgcaccct gcccgcggcc acggacc atg acc atg acc ctc cac 235
Met Thr Met Thr Leu His
1 5
acc aaa gca tct ggg atg gcc cta ctg cat cag atc caa ggg aac gag 283
Thr Lys Ala Ser Gly Met Ala Leu Leu His Gln Ile Gln Gly Asn Glu
10 15 20
ctg gag ccc ctg aac cgt ccg cag ctc aag atc ccc ctg gag cgg ccc 331
Leu Glu Pro Leu Asn Arg Pro Gln Leu Lys Ile Pro Leu Glu Arg Pro
25 30 35
ctg ggc gag gtg tac ctg gac agc agc aag ccc gcc gtg tac aac tac 379
Leu Gly Glu Val Tyr Leu Asp Ser Ser Lys Pro Ala Val Tyr Asn Tyr
40 45 50
ccc gag ggc gcc gcc tac gag ttc aac gcc gcg gcc gcc gcc aac gcg 427
Pro Glu Gly Ala Ala Tyr Glu Phe Asn Ala Ala Ala Ala Ala Asn Ala
55 60 65 70
cag gtc tac ggt cag acc ggc ctc ccc tac ggc ccc ggg tct gag gct 475
Gln Val Tyr Gly Gln Thr Gly Leu Pro Tyr Gly Pro Gly Ser Glu Ala
75 80 85
gcg gcg ttc ggc tcc aac ggc ctg ggg ggt ttc ccc cca ctc aac agc 523
Ala Ala Phe Gly Ser Asn Gly Leu Gly Gly Phe Pro Pro Leu Asn Ser
90 95 100
gtg tct ccg agc ccg ctg atg cta ctg cac ccg ccg ccg cag ctg tcg 571
Val Ser Pro Ser Pro Leu Met Leu Leu His Pro Pro Pro Gln Leu Ser
105 110 115
cct ttc ctg cag ccc cac ggc cag cag gtg ccc tac tac ctg gag aac 619
Pro Phe Leu Gln Pro His Gly Gln Gln Val Pro Tyr Tyr Leu Glu Asn
120 125 130
gag ccc agc ggc tac acg gtg cgc gag gcc ggc ccg ccg gca ttc tac 667
Glu Pro Ser Gly Tyr Thr Val Arg Glu Ala Gly Pro Pro Ala Phe Tyr
135 140 145 150
aga atg gtg ctg tca tgt gga ctg tcc tcc cga gtg tcc cac tgg atg 715
Arg Met Val Leu Ser Cys Gly Leu Ser Ser Arg Val Ser His Trp Met
155 160 165
ttc aga gaa ttt atg tga aggtcacgtc atttagcatt gagatgctgt 763
Phe Arg Glu Phe Met
170
ggttaccttc ttccatttct tccataatat gcagccacat ctatgtgtga agaaatgtaa 823
tagataaaat ttctctggac gcataataat gtgagaaaga ttgtcacatg tcccagcaaa 883
ttgttattaa tataaatttg ttacttggca agctgagatt ttgcaagatg ttactcaaaa 943
tttcacaatg aaggaaacag ggagtcatct tatcctgggt tcctttttta gatttcaaac 1003
aacttaggaa ctttgaataa aactaaagat gaagcttaac tatatcaact atccttttta 1063
aagttctaat taggaattta atgctgcatg cttatttcag ttttattact cagtattctt 1123
aaaagttaga catctctcac ttctccaaaa aacttggcaa atgtataaat cttttgcatc 1183
aaaatcaatg ccctgctaat ttgtatcctg gccatctgca tattttggac aactaatttt 1243
tccactggtg atcatttgaa actctttctc aactttgaat agagactgat ttccaaagtg 1303
agatttaagt gactaagttt caagtttccg atacattttt ccttttactt agataacatt 1363
tcagccccct tcctttctga tcttactttt ttattaattt aaattgttac tgattacgtg 1423
acactttgtg ctggtctaag aatagtccag agtcacatat tccctggtga atgagcatat 1483
tttcggatga aaacggaatc acatcttcaa tccccatttc attttcacct cctccatgtg 1543
gcttgtacct gtttggaaga aagctcctga aggataattg ccacttattc taatctttct 1603
cacactcatt taatttggat ccctggctaa agttgttatt tacttttgtg attatactta 1663
gtctatgaca ttcataattt gggaaaattc tcaggtttga gaattttggc ggcttgggat 1723
ttcttttagt ttcttatagt tttaaggata tgtaagacag gtgtaagaaa ctgccaaggg 1783
gaggaaccat agatatcagg aaaaactaga aaagatgcca gacttaccat taatgaatga 1843
tgagacaata gtaactttgt taagtgagat tgtatatgtg aaagtggtat agaaactaaa 1903
caaacattag gtgtttttat tattttactc acatgttaat atttgttttg gtgctttcat 1963
aggctaaaaa gctgggaaat aacagattta agtggtcagg aattttgtta taaatataga 2023
atgatgatta tatgaaatct tttcctgtga aagtcaaatt taagtaaaat ctttatcacc 2083
atctgcaaca tttgtctgca gcctggctta ccaggttatc ataaagaaca tttattttac 2143
agatacatta aagaaagtca aaaccctgat tatgtgtaaa caattttaca taaggaaata 2203
tatgaatttt aattatattt ttctaaaatc cgtactcagc atgaaattaa tacatcttaa 2263
cccctccctg tgacttcatt attattttta atgtaacttt agaagaaccc agtagagaga 2323
gcagcgtgct aagtgtgttt ctttcttttc cagacaactt tgaatggaga ggagcaaatt 2383
agtcttttgg tttaattctg tctcagtttg cttatctaaa gaaaggaaaa cagagtggct 2443
acacttgttt agaaccatat gcatactcca gagaaagatg ctctattaat ccaaaaaata 2503
cagccacttg aaaccagcca aagcgaaagt gtaagggact tcatggaaag gaggcagttc 2563
accaaagtta ttgaggggtt ttatatttta aactccgcca gtgaattgac gtgtaatgtc 2623
acttacaaaa aaaaaaaaaa gtatgtctga gctgttcgct acttcgtctc taaaatatac 2683
tcatactgat ctctgaaatc ccagaattta agtgggctgg aggttacggg aagcaccttt 2743
ataatatcct taatctcatg agggaagaaa ccataattgc tgaattctct gccttggata 2803
atatcaggag ggactctgaa gaaagttttg cagtaatcaa caatgtttta aattatgtgt 2863
atatttttag atcacctcaa aaaatatagg aagcacagaa tgacaactat tctggtctca 2923
actgacacaa ttttatgtag tttaataaag taataatttc aagaaacgtg ggcaaataaa 2983
aaaaaaaaaa aaaaa 2998


28
171
PRT
Homo sapiens

28
Met Thr Met Thr Leu His Thr Lys Ala Ser Gly Met Ala Leu Leu His
1 5 10 15
Gln Ile Gln Gly Asn Glu Leu Glu Pro Leu Asn Arg Pro Gln Leu Lys
20 25 30
Ile Pro Leu Glu Arg Pro Leu Gly Glu Val Tyr Leu Asp Ser Ser Lys
35 40 45
Pro Ala Val Tyr Asn Tyr Pro Glu Gly Ala Ala Tyr Glu Phe Asn Ala
50 55 60
Ala Ala Ala Ala Asn Ala Gln Val Tyr Gly Gln Thr Gly Leu Pro Tyr
65 70 75 80
Gly Pro Gly Ser Glu Ala Ala Ala Phe Gly Ser Asn Gly Leu Gly Gly
85 90 95
Phe Pro Pro Leu Asn Ser Val Ser Pro Ser Pro Leu Met Leu Leu His
100 105 110
Pro Pro Pro Gln Leu Ser Pro Phe Leu Gln Pro His Gly Gln Gln Val
115 120 125
Pro Tyr Tyr Leu Glu Asn Glu Pro Ser Gly Tyr Thr Val Arg Glu Ala
130 135 140
Gly Pro Pro Ala Phe Tyr Arg Met Val Leu Ser Cys Gly Leu Ser Ser
145 150 155 160
Arg Val Ser His Trp Met Phe Arg Glu Phe Met
165 170


29
14955
DNA
Homo sapiens

CDS
(95)..(6760)


29
taggcgccca gggccaggca gcggttgctt ccccggcccg gctcgcccgc gcttctctcc 60
ctgtgggcgg cggcccggcg cctggaaggt caag atg gaa gaa atc ctg agg aag 115
Met Glu Glu Ile Leu Arg Lys
1 5
ctg cag aag gag gcg tcc ggg agc aag tac aaa gcc atc aag gag agc 163
Leu Gln Lys Glu Ala Ser Gly Ser Lys Tyr Lys Ala Ile Lys Glu Ser
10 15 20
tgc acc tgg gcc ctg gaa act cta ggt ggt ctg gat acc att gcc aag 211
Cys Thr Trp Ala Leu Glu Thr Leu Gly Gly Leu Asp Thr Ile Ala Lys
25 30 35
atc cct cca cat gta ctg agg gag aaa tgc ctg ctg cct ctc cag ttg 259
Ile Pro Pro His Val Leu Arg Glu Lys Cys Leu Leu Pro Leu Gln Leu
40 45 50 55
gct ttg gaa tcc aag aat gtg aag ctg gcc caa cat gct ttg gca ggg 307
Ala Leu Glu Ser Lys Asn Val Lys Leu Ala Gln His Ala Leu Ala Gly
60 65 70
atg cag aag ctt ctg tcg gaa gag agg ttt gta tcc atg gaa aca gat 355
Met Gln Lys Leu Leu Ser Glu Glu Arg Phe Val Ser Met Glu Thr Asp
75 80 85
tct gat gag aag cag ctg ctc aat cag ata ctg aat gcc gtg aaa gtg 403
Ser Asp Glu Lys Gln Leu Leu Asn Gln Ile Leu Asn Ala Val Lys Val
90 95 100
acg cct tcg ctc aac gag gac ctg cag gtg gaa gtg atg aag gtt tta 451
Thr Pro Ser Leu Asn Glu Asp Leu Gln Val Glu Val Met Lys Val Leu
105 110 115
cta tgc atc acc tac acg cca aca ttt gat ctg aat ggg agt gcc gtg 499
Leu Cys Ile Thr Tyr Thr Pro Thr Phe Asp Leu Asn Gly Ser Ala Val
120 125 130 135
ctg aag atc gcg gag gtg tgc att gag acg tac ata agc agc tgt cac 547
Leu Lys Ile Ala Glu Val Cys Ile Glu Thr Tyr Ile Ser Ser Cys His
140 145 150
cag cgt agc ata aac act gct gtg cgg gca act ctc agt caa atg ctg 595
Gln Arg Ser Ile Asn Thr Ala Val Arg Ala Thr Leu Ser Gln Met Leu
155 160 165
agt gac ttg act tta cag tta cga cag agg cag gag aat acg ata att 643
Ser Asp Leu Thr Leu Gln Leu Arg Gln Arg Gln Glu Asn Thr Ile Ile
170 175 180
gaa aac cca gat gtc cca cag gat ttc ggg aat caa ggg tca aca gta 691
Glu Asn Pro Asp Val Pro Gln Asp Phe Gly Asn Gln Gly Ser Thr Val
185 190 195
gag tcc ctc tgt gat gat gtt gtc tct gta ctc acc gtc ctg tgt gag 739
Glu Ser Leu Cys Asp Asp Val Val Ser Val Leu Thr Val Leu Cys Glu
200 205 210 215
aag ctg caa gcc gcc ata aag tgc cca tct ttc ctg acc atg gcg tgt 787
Lys Leu Gln Ala Ala Ile Lys Cys Pro Ser Phe Leu Thr Met Ala Cys
220 225 230
tgg aac agt gga gct ggc act cag att acc atc cta act gag ggc tct 835
Trp Asn Ser Gly Ala Gly Thr Gln Ile Thr Ile Leu Thr Glu Gly Ser
235 240 245
agc acc aac tgc agc gac ccc atc tgg gac acc aca gcc tcg ccg gtg 883
Ser Thr Asn Cys Ser Asp Pro Ile Trp Asp Thr Thr Ala Ser Pro Val
250 255 260
gca gcc agt gac agc cag cag ctg cag ctt ctc tac ctg gag tgc atc 931
Ala Ala Ser Asp Ser Gln Gln Leu Gln Leu Leu Tyr Leu Glu Cys Ile
265 270 275
ctg tct gtg ctc agc agc tcc tcc tcc tcc atg cac ctg cac agg cgc 979
Leu Ser Val Leu Ser Ser Ser Ser Ser Ser Met His Leu His Arg Arg
280 285 290 295
ttc acg gac ctg atc tgg aaa aac ctc tgc cct gct ctc atc gtg atc 1027
Phe Thr Asp Leu Ile Trp Lys Asn Leu Cys Pro Ala Leu Ile Val Ile
300 305 310
ttg ggg aat cca att cat gac aaa acc atc acc tct gct cac acc agc 1075
Leu Gly Asn Pro Ile His Asp Lys Thr Ile Thr Ser Ala His Thr Ser
315 320 325
agc acc agt acc agc ctg gag tcg gac tct gcg tct ccg gga gtg tct 1123
Ser Thr Ser Thr Ser Leu Glu Ser Asp Ser Ala Ser Pro Gly Val Ser
330 335 340
gac cac ggc cga gga tca ggc tgc tcc tgc act gcg ccg gcc ctg agc 1171
Asp His Gly Arg Gly Ser Gly Cys Ser Cys Thr Ala Pro Ala Leu Ser
345 350 355
gga cct gtg gct cgg act atc tat tac atc gca gcc gag ctg gtc cgg 1219
Gly Pro Val Ala Arg Thr Ile Tyr Tyr Ile Ala Ala Glu Leu Val Arg
360 365 370 375
ctg gtg ggg tct gtg gac tcc atg aag ccc gtg ctc cag tcc ctc tac 1267
Leu Val Gly Ser Val Asp Ser Met Lys Pro Val Leu Gln Ser Leu Tyr
380 385 390
cac cga gtg ctg ctc tac ccc cca ccc cag cac cgg gtg gaa gcc atc 1315
His Arg Val Leu Leu Tyr Pro Pro Pro Gln His Arg Val Glu Ala Ile
395 400 405
aaa ata atg aaa gag ata ctt ggg agc cca cag cgt ctc tgt gac ttg 1363
Lys Ile Met Lys Glu Ile Leu Gly Ser Pro Gln Arg Leu Cys Asp Leu
410 415 420
gca gga ccc agc tcc act gaa tca gag tcc aga aaa aga tca att tca 1411
Ala Gly Pro Ser Ser Thr Glu Ser Glu Ser Arg Lys Arg Ser Ile Ser
425 430 435
aaa aga aag tct cat ctg gat ctc ctc aaa ctc atc atg gat ggc atg 1459
Lys Arg Lys Ser His Leu Asp Leu Leu Lys Leu Ile Met Asp Gly Met
440 445 450 455
acc gaa gca tgc atc aag ggt ggc atc gaa gct tgc tat gca gcc gtg 1507
Thr Glu Ala Cys Ile Lys Gly Gly Ile Glu Ala Cys Tyr Ala Ala Val
460 465 470
tcc tgt gtc tgc acc ttg ctg ggt gcc ctg gat gag ctc agc cag ggg 1555
Ser Cys Val Cys Thr Leu Leu Gly Ala Leu Asp Glu Leu Ser Gln Gly
475 480 485
aag ggc ttg agc gaa ggt cag gtg caa ctg ctg ctt ctg cgc ctt gag 1603
Lys Gly Leu Ser Glu Gly Gln Val Gln Leu Leu Leu Leu Arg Leu Glu
490 495 500
gag ctg aag gat ggg gct gag tgg agc cga gat tcc atg gag atc aat 1651
Glu Leu Lys Asp Gly Ala Glu Trp Ser Arg Asp Ser Met Glu Ile Asn
505 510 515
gag gct gac ttc cgc tgg cag cgg cga gtg ctg tcc tca gaa cac acg 1699
Glu Ala Asp Phe Arg Trp Gln Arg Arg Val Leu Ser Ser Glu His Thr
520 525 530 535
ccg tgg gag tca ggg aac gag agg agc ctt gac atc agc atc agt gtc 1747
Pro Trp Glu Ser Gly Asn Glu Arg Ser Leu Asp Ile Ser Ile Ser Val
540 545 550
acc aca gac aca ggc cag acc act ctc gag gga gag ttg ggt cag act 1795
Thr Thr Asp Thr Gly Gln Thr Thr Leu Glu Gly Glu Leu Gly Gln Thr
555 560 565
aca ccc gag gac cat tcg gga aac cac aag aac agt ctc aag tcg cca 1843
Thr Pro Glu Asp His Ser Gly Asn His Lys Asn Ser Leu Lys Ser Pro
570 575 580
gcc atc cca gag ggt aag gag acg ctg agc aaa gta ttg gaa aca gag 1891
Ala Ile Pro Glu Gly Lys Glu Thr Leu Ser Lys Val Leu Glu Thr Glu
585 590 595
gcg gta gac cag cca gat gtc gtg cag aga agc cac acg gtc cct tac 1939
Ala Val Asp Gln Pro Asp Val Val Gln Arg Ser His Thr Val Pro Tyr
600 605 610 615
cct gac ata act aac ttc ctg tca gta gac tgc agg aca agg tcc tat 1987
Pro Asp Ile Thr Asn Phe Leu Ser Val Asp Cys Arg Thr Arg Ser Tyr
620 625 630
gga tct agg tat agt gag agc aat ttt agc gtt gat gac caa gac ctt 2035
Gly Ser Arg Tyr Ser Glu Ser Asn Phe Ser Val Asp Asp Gln Asp Leu
635 640 645
tct agg aca gag ttt gat tcc tgt gat cag tac tct atg gca gca gaa 2083
Ser Arg Thr Glu Phe Asp Ser Cys Asp Gln Tyr Ser Met Ala Ala Glu
650 655 660
aag gac tcg ggc agg tcc gac gtg tca gac att ggg tcg gac aac tgt 2131
Lys Asp Ser Gly Arg Ser Asp Val Ser Asp Ile Gly Ser Asp Asn Cys
665 670 675
tca cta gcc gat gaa gag cag aca ccc cgg gac tgc cta ggc cac cgg 2179
Ser Leu Ala Asp Glu Glu Gln Thr Pro Arg Asp Cys Leu Gly His Arg
680 685 690 695
tcc ctg cga act gcc gcc ctg tct cta aaa ctg ctg aag aac cag gag 2227
Ser Leu Arg Thr Ala Ala Leu Ser Leu Lys Leu Leu Lys Asn Gln Glu
700 705 710
gcg gat cag cac agc gcc agg ctg ttc ata cag tcc ctg gaa ggc ctc 2275
Ala Asp Gln His Ser Ala Arg Leu Phe Ile Gln Ser Leu Glu Gly Leu
715 720 725
ctc cct cgg ctc ctg tct ctc tcc aat gta gag gag gtg gac acc gct 2323
Leu Pro Arg Leu Leu Ser Leu Ser Asn Val Glu Glu Val Asp Thr Ala
730 735 740
ctg cag aac ttt gcc tct act ttc tgc tca ggc atg atg cac tct cct 2371
Leu Gln Asn Phe Ala Ser Thr Phe Cys Ser Gly Met Met His Ser Pro
745 750 755
ggc ttt gac ggg aat agc agc ctc agc ttc cag atg ctg atg aac gca 2419
Gly Phe Asp Gly Asn Ser Ser Leu Ser Phe Gln Met Leu Met Asn Ala
760 765 770 775
gac agc ctc tac aca gct gca cac tgc gcc ctg ctc ctc aac ctg aag 2467
Asp Ser Leu Tyr Thr Ala Ala His Cys Ala Leu Leu Leu Asn Leu Lys
780 785 790
ctc tcc cac ggt gac tac tac agg aag cgg ccg acc ctg gcg cca ggc 2515
Leu Ser His Gly Asp Tyr Tyr Arg Lys Arg Pro Thr Leu Ala Pro Gly
795 800 805
gtg atg aag gac ttc atg aag cag gtg cag acc agc ggc gtg ctg atg 2563
Val Met Lys Asp Phe Met Lys Gln Val Gln Thr Ser Gly Val Leu Met
810 815 820
gtc ttc tct cag gcc tgg att gag gag ctc tac cat cag gtg ctc gac 2611
Val Phe Ser Gln Ala Trp Ile Glu Glu Leu Tyr His Gln Val Leu Asp
825 830 835
agg aac atg ctt gga gag gct ggc tat tgg ggc agc cca gaa gat aac 2659
Arg Asn Met Leu Gly Glu Ala Gly Tyr Trp Gly Ser Pro Glu Asp Asn
840 845 850 855
agc ctt ccc ctc atc aca atg ctg acc gat att gac ggc tta gag agc 2707
Ser Leu Pro Leu Ile Thr Met Leu Thr Asp Ile Asp Gly Leu Glu Ser
860 865 870
agt gcc att ggt ggc cag ctg atg gcc tcg gct gct aca gag tct cct 2755
Ser Ala Ile Gly Gly Gln Leu Met Ala Ser Ala Ala Thr Glu Ser Pro
875 880 885
ttc gcc cag agc agg aga att gat gac tcc aca gtg gca ggc gtg gca 2803
Phe Ala Gln Ser Arg Arg Ile Asp Asp Ser Thr Val Ala Gly Val Ala
890 895 900
ttt gct cgc tat att ctg gtg ggc tgc tgg aag aac ttg atc gat act 2851
Phe Ala Arg Tyr Ile Leu Val Gly Cys Trp Lys Asn Leu Ile Asp Thr
905 910 915
tta tca acc cca ctg act ggt cga atg gcg ggg agc tcc aaa ggg ctg 2899
Leu Ser Thr Pro Leu Thr Gly Arg Met Ala Gly Ser Ser Lys Gly Leu
920 925 930 935
gcc ttc att ctg gga gct gaa ggc atc aaa gag cag aac cag aag gag 2947
Ala Phe Ile Leu Gly Ala Glu Gly Ile Lys Glu Gln Asn Gln Lys Glu
940 945 950
cgg gac gcc atc tgc atg agc ctc gac ggg ctg cgg aaa gcc gca cgg 2995
Arg Asp Ala Ile Cys Met Ser Leu Asp Gly Leu Arg Lys Ala Ala Arg
955 960 965
ctg agc tgc gct cta ggc gtt gct gct aac tgc gcc tca gcc ctt gcc 3043
Leu Ser Cys Ala Leu Gly Val Ala Ala Asn Cys Ala Ser Ala Leu Ala
970 975 980
cag atg gca gct gcc tcc tgt gtc caa gaa gaa aaa gaa gag agg gag 3091
Gln Met Ala Ala Ala Ser Cys Val Gln Glu Glu Lys Glu Glu Arg Glu
985 990 995
gcc caa gaa ccc agt gat gcc atc aca caa gtg aaa cta aaa gtg 3136
Ala Gln Glu Pro Ser Asp Ala Ile Thr Gln Val Lys Leu Lys Val
1000 1005 1010
gag cag aaa ctg gag cag att ggg aag gtg cag ggg gtg tgg ctg 3181
Glu Gln Lys Leu Glu Gln Ile Gly Lys Val Gln Gly Val Trp Leu
1015 1020 1025
cac act gcc cac gtc ttg tgc atg gag gcc atc ctc agc gta ggc 3226
His Thr Ala His Val Leu Cys Met Glu Ala Ile Leu Ser Val Gly
1030 1035 1040
ctg gag atg gga agc cac aac ccg gac tgc tgg cca cac gtg ttc 3271
Leu Glu Met Gly Ser His Asn Pro Asp Cys Trp Pro His Val Phe
1045 1050 1055
agg gtg tgt gaa tac gtg ggc acc ctg gag cac aac cac ttc agc 3316
Arg Val Cys Glu Tyr Val Gly Thr Leu Glu His Asn His Phe Ser
1060 1065 1070
gat ggt gcc tcg cag ccc cct ctg acc atc agc cag ccc cag aag 3361
Asp Gly Ala Ser Gln Pro Pro Leu Thr Ile Ser Gln Pro Gln Lys
1075 1080 1085
gcc act gga agc gct ggc ctc ctt ggg gac ccc gag tgt gag ggc 3406
Ala Thr Gly Ser Ala Gly Leu Leu Gly Asp Pro Glu Cys Glu Gly
1090 1095 1100
tcg ccc ccc gag cac agc ccg gag cag ggg cgc tcc ctg agc acg 3451
Ser Pro Pro Glu His Ser Pro Glu Gln Gly Arg Ser Leu Ser Thr
1105 1110 1115
gcc cct gtc gtc cag ccc ctg tcc atc cag gac ctc gtc cgg gaa 3496
Ala Pro Val Val Gln Pro Leu Ser Ile Gln Asp Leu Val Arg Glu
1120 1125 1130
ggc agc cgg ggt cgg gcc tcc gac ttc cgc ggc ggg agc ctc atg 3541
Gly Ser Arg Gly Arg Ala Ser Asp Phe Arg Gly Gly Ser Leu Met
1135 1140 1145
agc ggg agc agc gcg gcc aag gtg gtg ctc acc ctc tcc acg caa 3586
Ser Gly Ser Ser Ala Ala Lys Val Val Leu Thr Leu Ser Thr Gln
1150 1155 1160
gcc gac agg ctc ttt gaa gat gct acg gat aag ttg aac ctc atg 3631
Ala Asp Arg Leu Phe Glu Asp Ala Thr Asp Lys Leu Asn Leu Met
1165 1170 1175
gcc ttg gga ggt ttt ctt tac cag ctg aag aaa gca tcg cag tct 3676
Ala Leu Gly Gly Phe Leu Tyr Gln Leu Lys Lys Ala Ser Gln Ser
1180 1185 1190
cag ctt ttc cat tct gtt aca gat aca gtt gat tac tct ctg gca 3721
Gln Leu Phe His Ser Val Thr Asp Thr Val Asp Tyr Ser Leu Ala
1195 1200 1205
atg cca gga gaa gtt aaa tcc act caa gac cga aaa agc gcc ctc 3766
Met Pro Gly Glu Val Lys Ser Thr Gln Asp Arg Lys Ser Ala Leu
1210 1215 1220
cac ctg ttc cgc ctg ggg aat gcc atg ctg agg att gtg cgg agc 3811
His Leu Phe Arg Leu Gly Asn Ala Met Leu Arg Ile Val Arg Ser
1225 1230 1235
aaa gca cgg ccc ctg ctc cac gtg atg cgc tgc tgg agc ctt gtg 3856
Lys Ala Arg Pro Leu Leu His Val Met Arg Cys Trp Ser Leu Val
1240 1245 1250
gcc cca cac ctg gtg gag gct gct tgc cat aag gaa aga cat gtg 3901
Ala Pro His Leu Val Glu Ala Ala Cys His Lys Glu Arg His Val
1255 1260 1265
tct cag aag gct gtt tcc ttc atc cat gac ata ctg aca gaa gtc 3946
Ser Gln Lys Ala Val Ser Phe Ile His Asp Ile Leu Thr Glu Val
1270 1275 1280
ctc act gac tgg aat gag cca cct cat ttt cac ttc aat gaa gca 3991
Leu Thr Asp Trp Asn Glu Pro Pro His Phe His Phe Asn Glu Ala
1285 1290 1295
ctc ttc cga cct ttc gag cgc att atg cag ctg gaa ttg tgt gat 4036
Leu Phe Arg Pro Phe Glu Arg Ile Met Gln Leu Glu Leu Cys Asp
1300 1305 1310
gag gac gtc caa gac cag gtt gtc aca tcc att ggt gag ctg gtt 4081
Glu Asp Val Gln Asp Gln Val Val Thr Ser Ile Gly Glu Leu Val
1315 1320 1325
gaa gtg tgt tcc acg cag atc cag tcg gga tgg aga ccc ttg ttc 4126
Glu Val Cys Ser Thr Gln Ile Gln Ser Gly Trp Arg Pro Leu Phe
1330 1335 1340
agt gcc ctg gaa aca gtg cat ggc ggg aac aag tca gag atg aag 4171
Ser Ala Leu Glu Thr Val His Gly Gly Asn Lys Ser Glu Met Lys
1345 1350 1355
gag tac ctg gtt ggt gac tac tcc atg gga aaa ggc caa gct cca 4216
Glu Tyr Leu Val Gly Asp Tyr Ser Met Gly Lys Gly Gln Ala Pro
1360 1365 1370
gtg ttt gat gta ttt gaa gct ttt ctc aat act gac aac atc cag 4261
Val Phe Asp Val Phe Glu Ala Phe Leu Asn Thr Asp Asn Ile Gln
1375 1380 1385
gtc ttt gct aat gca gcc act agc tac atc atg tgc ctt atg aag 4306
Val Phe Ala Asn Ala Ala Thr Ser Tyr Ile Met Cys Leu Met Lys
1390 1395 1400
ttt gtc aaa gga ctg ggg gag gtg gac tgt aaa gag att gga gac 4351
Phe Val Lys Gly Leu Gly Glu Val Asp Cys Lys Glu Ile Gly Asp
1405 1410 1415
tgt gcc cca gca ccc gga gcc ccg tcc aca gac ctg tgc ctc ccg 4396
Cys Ala Pro Ala Pro Gly Ala Pro Ser Thr Asp Leu Cys Leu Pro
1420 1425 1430
gcc ctg gat tac ctc agg cgc tgc tct cag tta ttg gcc aaa atc 4441
Ala Leu Asp Tyr Leu Arg Arg Cys Ser Gln Leu Leu Ala Lys Ile
1435 1440 1445
tac aaa atg ccc ttg aag cca ata ttc ctt agt ggg aga ctt gcc 4486
Tyr Lys Met Pro Leu Lys Pro Ile Phe Leu Ser Gly Arg Leu Ala
1450 1455 1460
ggc ttg cct cga aga ctt cag gaa cag tca gcc agc agt gag gat 4531
Gly Leu Pro Arg Arg Leu Gln Glu Gln Ser Ala Ser Ser Glu Asp
1465 1470 1475
gga att gaa tca gtc ctg tct gat ttt gat gat gac acc ggt ctg 4576
Gly Ile Glu Ser Val Leu Ser Asp Phe Asp Asp Asp Thr Gly Leu
1480 1485 1490
ata gaa gtc tgg ata atc ctg ctg gag cag ctg aca gcg gct gtg 4621
Ile Glu Val Trp Ile Ile Leu Leu Glu Gln Leu Thr Ala Ala Val
1495 1500 1505
tcc aat tgt cca cgg cag cac caa cca cca act ctg gat tta ctc 4666
Ser Asn Cys Pro Arg Gln His Gln Pro Pro Thr Leu Asp Leu Leu
1510 1515 1520
ttt gag ctg ttg aga gat gtg acg aaa aca cca gga cca ggg ttt 4711
Phe Glu Leu Leu Arg Asp Val Thr Lys Thr Pro Gly Pro Gly Phe
1525 1530 1535
ggt atc tat gca gtg gtt cac ctc ctc ctt cct gtg atg tcc gtt 4756
Gly Ile Tyr Ala Val Val His Leu Leu Leu Pro Val Met Ser Val
1540 1545 1550
tgg ctc cgc cgg agc cat aaa gac cat tcc tac tgg gat atg gcc 4801
Trp Leu Arg Arg Ser His Lys Asp His Ser Tyr Trp Asp Met Ala
1555 1560 1565
tct gcc aat ttc aag cac gct att ggt ctg tcc tgt gag ctg gtg 4846
Ser Ala Asn Phe Lys His Ala Ile Gly Leu Ser Cys Glu Leu Val
1570 1575 1580
gtg gag cac att caa agc ttt cta cat tca gat atc agg tac gag 4891
Val Glu His Ile Gln Ser Phe Leu His Ser Asp Ile Arg Tyr Glu
1585 1590 1595
agc atg atc aat acc atg ctg aag gac ctc ttt gag ttg ctg gtc 4936
Ser Met Ile Asn Thr Met Leu Lys Asp Leu Phe Glu Leu Leu Val
1600 1605 1610
gcc tgt gtg gcc aag ccc act gaa acc atc tcc aga gtg ggc tgc 4981
Ala Cys Val Ala Lys Pro Thr Glu Thr Ile Ser Arg Val Gly Cys
1615 1620 1625
tcc tgt att aga tac gtc ctt gtg aca gcg ggc cct gtg ttc act 5026
Ser Cys Ile Arg Tyr Val Leu Val Thr Ala Gly Pro Val Phe Thr
1630 1635 1640
gag gag atg tgg agg ctt gcc tgc tgt gcc ctg caa gat gcg ttc 5071
Glu Glu Met Trp Arg Leu Ala Cys Cys Ala Leu Gln Asp Ala Phe
1645 1650 1655
tct gcc aca ctc aag cca gtg aag gac ctg ctg ggc tgc ttc cac 5116
Ser Ala Thr Leu Lys Pro Val Lys Asp Leu Leu Gly Cys Phe His
1660 1665 1670
agc ggc acg gag agc ttc agc ggg gaa ggc tgc cag gtg cga gtg 5161
Ser Gly Thr Glu Ser Phe Ser Gly Glu Gly Cys Gln Val Arg Val
1675 1680 1685
gcg gcc ccg tcc tcc tcc cca agt gcc gag gcc gag tac tgg cgc 5206
Ala Ala Pro Ser Ser Ser Pro Ser Ala Glu Ala Glu Tyr Trp Arg
1690 1695 1700
atc cga gcc atg gcc cag cag gtg ttt atg ctg gac acc cag tgc 5251
Ile Arg Ala Met Ala Gln Gln Val Phe Met Leu Asp Thr Gln Cys
1705 1710 1715
tca cca aag aca cca aac aac ttt gac cac gct cag tcc tgc cag 5296
Ser Pro Lys Thr Pro Asn Asn Phe Asp His Ala Gln Ser Cys Gln
1720 1725 1730
ctc att att gag ctg cct cct gat gaa aaa cca aat gga cac acc 5341
Leu Ile Ile Glu Leu Pro Pro Asp Glu Lys Pro Asn Gly His Thr
1735 1740 1745
aag aaa agc gtg tct ttc agg gaa att gtg gtg agc ctg ctg tct 5386
Lys Lys Ser Val Ser Phe Arg Glu Ile Val Val Ser Leu Leu Ser
1750 1755 1760
cat cag gtg tta ctc cag aac tta tat gac atc ttg tta gaa gag 5431
His Gln Val Leu Leu Gln Asn Leu Tyr Asp Ile Leu Leu Glu Glu
1765 1770 1775
ttt gtc aaa ggc ccc tct cct gga gag gaa aag acg ata caa gtg 5476
Phe Val Lys Gly Pro Ser Pro Gly Glu Glu Lys Thr Ile Gln Val
1780 1785 1790
cca gaa gcc aag ctg gct ggc ttc ctc aga tac atc tct atg cag 5521
Pro Glu Ala Lys Leu Ala Gly Phe Leu Arg Tyr Ile Ser Met Gln
1795 1800 1805
aac ttg gca gtc ata ttc gac ctg ctg ctg gac tct tat agg act 5566
Asn Leu Ala Val Ile Phe Asp Leu Leu Leu Asp Ser Tyr Arg Thr
1810 1815 1820
gcc agg gag ttt gac acc agc ccc ggg ctg aag tgc ctg ctg aag 5611
Ala Arg Glu Phe Asp Thr Ser Pro Gly Leu Lys Cys Leu Leu Lys
1825 1830 1835
aaa gtg tct ggc atc ggg ggc gcc gcc aac ctc tac cgc cag tct 5656
Lys Val Ser Gly Ile Gly Gly Ala Ala Asn Leu Tyr Arg Gln Ser
1840 1845 1850
gcg atg agc ttt aac att tat ttc cac gcc ctg gtg tgt gct gtt 5701
Ala Met Ser Phe Asn Ile Tyr Phe His Ala Leu Val Cys Ala Val
1855 1860 1865
ctc acc aat caa gaa acc atc acg gcc gag caa gtg aag aag gtc 5746
Leu Thr Asn Gln Glu Thr Ile Thr Ala Glu Gln Val Lys Lys Val
1870 1875 1880
ctt ttt gag gac gac gag aga agc acg gat tct tcc cag cag tgt 5791
Leu Phe Glu Asp Asp Glu Arg Ser Thr Asp Ser Ser Gln Gln Cys
1885 1890 1895
tca tct gag gat gaa gac atc ttt gag gaa acc gcc cag gtc agc 5836
Ser Ser Glu Asp Glu Asp Ile Phe Glu Glu Thr Ala Gln Val Ser
1900 1905 1910
ccc ccg aga ggc aag gag aag aga cag tgg cgg gca cgg atg ccc 5881
Pro Pro Arg Gly Lys Glu Lys Arg Gln Trp Arg Ala Arg Met Pro
1915 1920 1925
ttg ctc agc gtc cag cct gtc agc aac gca gat tgg gtg tgg ctg 5926
Leu Leu Ser Val Gln Pro Val Ser Asn Ala Asp Trp Val Trp Leu
1930 1935 1940
gtc aag agg ctg cac aag ctg tgc atg gaa ctg tgc aac aac tac 5971
Val Lys Arg Leu His Lys Leu Cys Met Glu Leu Cys Asn Asn Tyr
1945 1950 1955
atc cag atg cac ttg gac ctg gag aac tgt atg gag gag cct ccc 6016
Ile Gln Met His Leu Asp Leu Glu Asn Cys Met Glu Glu Pro Pro
1960 1965 1970
atc ttc aag ggc gac ccg ttc ttc atc ctg ccc tcc ttc cag tcc 6061
Ile Phe Lys Gly Asp Pro Phe Phe Ile Leu Pro Ser Phe Gln Ser
1975 1980 1985
gag tca tcc acc cca tcc acc ggg ggc ttc tct ggg aaa gaa acc 6106
Glu Ser Ser Thr Pro Ser Thr Gly Gly Phe Ser Gly Lys Glu Thr
1990 1995 2000
cct tcc gag gat gac aga agc cag tcc cgg gag cac atg ggc gag 6151
Pro Ser Glu Asp Asp Arg Ser Gln Ser Arg Glu His Met Gly Glu
2005 2010 2015
tcc ctg agc ctg aag gcc ggt ggt ggg gac ctg ctg ctg ccc ccc 6196
Ser Leu Ser Leu Lys Ala Gly Gly Gly Asp Leu Leu Leu Pro Pro
2020 2025 2030
agc ccc aaa gtg gag aag aag gat ccc agc cgg aag aag gag tgg 6241
Ser Pro Lys Val Glu Lys Lys Asp Pro Ser Arg Lys Lys Glu Trp
2035 2040 2045
tgg gag aat gcg ggg aac aaa atc tac acc atg gca gcc gac aag 6286
Trp Glu Asn Ala Gly Asn Lys Ile Tyr Thr Met Ala Ala Asp Lys
2050 2055 2060
acc att tca aag ttg atg acc gaa tac aaa aag agg aaa cag cag 6331
Thr Ile Ser Lys Leu Met Thr Glu Tyr Lys Lys Arg Lys Gln Gln
2065 2070 2075
cac aac ctg tcc gcg ttc ccc aaa gag gtc aaa gtg gag aag aaa 6376
His Asn Leu Ser Ala Phe Pro Lys Glu Val Lys Val Glu Lys Lys
2080 2085 2090
gga gag cca ctg ggt ccc agg ggc cag gac tcc ccg ctg ctt cag 6421
Gly Glu Pro Leu Gly Pro Arg Gly Gln Asp Ser Pro Leu Leu Gln
2095 2100 2105
cgt ccc cag cac ttg atg gac caa ggg caa atg cgg cat tcc ttc 6466
Arg Pro Gln His Leu Met Asp Gln Gly Gln Met Arg His Ser Phe
2110 2115 2120
agc gca ggc ccc gag ctg ctg cga cag gac aag agg ccc cgc tca 6511
Ser Ala Gly Pro Glu Leu Leu Arg Gln Asp Lys Arg Pro Arg Ser
2125 2130 2135
ggc tcc acc ggg agc tcc ctc agt gtc tcg gtg aga gac gca gaa 6556
Gly Ser Thr Gly Ser Ser Leu Ser Val Ser Val Arg Asp Ala Glu
2140 2145 2150
gca cag atc cag gca tgg acc aac atg gtg cta aca gtt ctc aat 6601
Ala Gln Ile Gln Ala Trp Thr Asn Met Val Leu Thr Val Leu Asn
2155 2160 2165
cag att cag att ctc cca gac cag acc ttc acg gcc ctc cag ccc 6646
Gln Ile Gln Ile Leu Pro Asp Gln Thr Phe Thr Ala Leu Gln Pro
2170 2175 2180
gca gtg ttc ccg tgc atc agt cag ctg acc tgt cac gtg acc gac 6691
Ala Val Phe Pro Cys Ile Ser Gln Leu Thr Cys His Val Thr Asp
2185 2190 2195
atc aga gtt cgc cag gct gtg agg gag tgg ctg ggc agg gtg ggc 6736
Ile Arg Val Arg Gln Ala Val Arg Glu Trp Leu Gly Arg Val Gly
2200 2205 2210
cgt gtc tat gac atc att gtg tag ccgactcctg ttctactctc 6780
Arg Val Tyr Asp Ile Ile Val
2215 2220
ccaccaaata acagtagtga gggttagagt cctgccaata cagctgttgc attttcccca 6840
ccactagccc cacttaaact actactactg tctcagagaa cagtgtttcc taatgtaaaa 6900
agcctttcca accactgatc agcattgggg ccatactaag gtttgtatct agatgacaca 6960
aacgatattc tgattttgca cattattata gaagaatcta taatccttga tatgtttcta 7020
actcttgaag tatatttccc agtgcttttg cttacagtgt tgtccccaaa tgggtcattt 7080
tcaaggatta ctcatttgaa aacactatat tgatccattt gatccatcat ttaaaaaata 7140
aatacaattc ctaaggcaat atctgctggt aagtcaagct gataaacact cagacatcta 7200
gtaccaggga ttattaattg gaggaagatt tatggttatg ggtctggctg ggaagaagac 7260
aactataaat acatattctt gggtgtcata atcaagaaag aggtgacttc tgttgtaaaa 7320
taatccagaa cacttcaaaa ttattcctaa atcattaaga ttttcaggta ttcaccaatt 7380
tccccatgta aggtactgtg ttgtaccttt atttctgtat ttctaaaaga agaaagttct 7440
ttcctagcag ggtttgaagt ctgtggctta tcagcctgtg acacagagta cccagtgaaa 7500
gtggctggta cgtagattgt caagagacat aagaccgacc agccaccctg gctgttcttg 7560
tggtgtttgt ttccatcccc aaggcaaaca aggaaaggaa aggaaagaag aaaaggtgcc 7620
ttagtccttt gttgcacttc catttccatg ccccacaatt gtctgaacat aaggtatagc 7680
atttggtttt taagaaaaca aaacattaag acgcaactca ttttatatca acacgcttgg 7740
aggaaaggga ctcagggaag ggagcaggga gtgtggggtg gggatggatt atgatgaaat 7800
cattttcaat cttaaaatat aatacaacaa tcttgcaaaa ttatggtgtc agttacacaa 7860
gctctagtct caaaatgaaa gtaatggaga aagacactga aatttagaaa attttgtcga 7920
tttaaaatat ttctcctatc taccaagtaa agttacccta tgtttgatgt ctttgcattc 7980
agaccaatat ttcaggtgga tatttctaag tattactaga aaatacgttt gaaagcttta 8040
tcttattatt tacagtattt ttatatttct tacattatcc taatgattga aaactcctca 8100
atcaagctta cttacacaca ttctacagag ttatttaagg catacattat aatctcccag 8160
ccccattcat aatgaataag tcacccttta aatataagac acaaattcta cagtattgaa 8220
ataaggattt aaaggggtat ttgtaaactt tgccctcctt gagaaatatg gaactacctt 8280
agaggttaag aggaaggcag tgttctgact tctttaggtg atctgaaaaa aacaccctta 8340
tcatccagtg taccatctag agatcaccac agaatccatt tttttcccag ttccacaaaa 8400
cactctgttt gccttcagtt tttactcact agacaataat tcaagtttag aaacaggtaa 8460
tcagctattt gatcttaaaa ggcaatgaat tgttgggata tcagtgaact atgttgtata 8520
cttttgaatt tttacatttt ataaatggaa ttgaaagttg gataactgct ttttttaaat 8580
tttccaacag aagtaacacc acagttgctt tgtttctttt tatagcttac ctgaggttca 8640
gttcttcttt gtgaacctgt gagtactcca cagtttactg ggggaaaagg cttcagtaaa 8700
gcagaggcta gaattacagt atttatacat agcaactttt cataaagtag aaaaattcaa 8760
aggaagctgt ctcaatttga gaataccagc tgggcacggt ggctcacgcc tgtaatccca 8820
gcacttactt tgggaggcca aggtgggcag ataacctgcg gtcaggagtt tgagaccagg 8880
ctggacaaca tggtgaaacc tcgtctctac taaaaataca aaaattagcc aggtgtggta 8940
ggatgcacct gtaatcccag ctacttagga ggccgagaca ggagaatcgc tcgaacccag 9000
gaggcggacg ttgcagtgag ccaagattgc accattgcac tccagactgg gtgacaagag 9060
tgaaactcca tctaaaaaaa aaaaaaaaaa aaagtgaata ctgtatccca aagtatgtta 9120
gttgtttgtt tggaaatcag cattctcccc gatgctctat tatgggatcc aaaattcttg 9180
aacataagtt taccctgtac tgtgtccaaa cactgttcta gttctagcct gattatgggt 9240
cccaagaata aaaggatgag taggtgtaca gagctcttga cctacaattt tttaagagtg 9300
ttttggtacc ttcccattgt cttctctata actcagtcct aacatactct gcactcgagt 9360
taccagccat ccacactgac atcagatttc aaccagaacc atcactgagt gacagcagta 9420
cttctcagag gtatttgcag cttgatgcaa agtagtctct aatgagtagg cattcaggtg 9480
gttcttccca gcaggtggag aagaaaggga ggagatgaag aacactgaga ggggagtggc 9540
accttcccag gctgcccagc tcagtctctt gccctgttcc tgtgactcag ctgcccactc 9600
ccccaacttt gtttccctcc ctcccagtct ctgaaagtgt caggtgtttc tctcctcaca 9660
gtctcttttg cagcaacagt aagacaaaat tcaaggcagc cttttaaagt tacgaacagt 9720
tattagcatg tatttacaga cctaagcaga atgagagttt atacattgtt tttagttgcc 9780
tgtatttata gccaaaagta tattacctta aagttgagat ctttctcttc ttttcctaaa 9840
ttttggtaaa gtgtgcttca tgaaacaaac atctggaaaa ctccaagtat aagagaccct 9900
ggactgatga tggcccagcc aagtatatgg agggacagag ttctctctgt cattaatgag 9960
gacatcggtt ttcacaattg aacctcatgc actgtccaca gcatctcacc tagctcctgt 10020
atctcctgat ctgcttttaa aaatagttag ttaggctgcc tttttacacc accttctctc 10080
tctccccttg tggtaatttt ccagccttcc ccatagatat aaaactagaa cacctttatg 10140
atttggggtc tatgtaatga ctgaccgata agaacccagg cagatgctaa catacttaac 10200
agctcgcatt aaaatacttt aaatcaggcg tgatggctca ttcctgtaat ctcaagcact 10260
ttgggaggct aaggtgggtg gatctcttga ggtcaggagt tcgagaccaa cctggccaac 10320
gtggtgaaac cccgtctcta ctaaaaatac aaaattagcc gggcatggtg gcagctgcct 10380
gtaatcccag ctactcggga agctgaggca ggagaattgc ttgaacctgg gaggtgggga 10440
ttgcagtcag ccaagattgt tctgcagcat gggtgacaaa gtgagacttc gtctcaagta 10500
aataaaacta aaatttttaa atcaaacatg acaaaaatgt taatataatt cagaagtacc 10560
ttgaaattga aacatatttg tgcaatgatc attaggcttt ttgtccttgt tgttttaaaa 10620
tgaggcttat acagagtgag ttgagagtca agtagccttc gctgtgagac ggtaatgcag 10680
ttatataata gatacccttg actttgccag attcatcaca atactgctta tacaggaaag 10740
ttttctcaga aaggaaaatc cattagtatc agtcccatca agccaaacag aatgaagacc 10800
tttgatagta atagcaagag gttacaaata gcagggagga ggcgagtagt gaatgtcact 10860
gtgattgcaa acccttacct gtattatcac acgtagtcct cacaacaacc ttgtgagaca 10920
agtgttgtgt tcctcatttt ttcagagggg aacacagacc cagagaggtt aagaaatttg 10980
cccaagataa caagtaaaag gcaaagttgg ttgcaaaaga ggtgtttctg aattcaaggg 11040
ccatactctc tctctgacaa catgctctaa gtccatagag taagcactct agtatgaaaa 11100
aaagtttcaa ggaacgaggc catgaaaatg agactatttg acatctcaga tctgtctggg 11160
atgttatgga ggtttttaaa aataaagttg aaaaaagaaa atgaatcatg tttatacata 11220
aaaaaatcac atgtaacaca tttcaagtgt ttgaaaataa aaccaaaatc taaactttag 11280
tcttcaagca gacattcagt gttactttag aaaactcact gaattaggtg gaaatgatgg 11340
aataatacta ttcatggcca gctattaaca cagaagaaca tggcagtgtg tgtctggaac 11400
ggcatgcaca atttgtaaac ctttttcaaa tatcatttaa tcaactcaga ataaagtgcc 11460
ctgtagccaa cagtgcctct ttacttgctt ctctgggaaa tacatggtac taaattagta 11520
gcacaaagtt tgggaatatg caaaataatg gataaccatt tttcaaaatg tacattctct 11580
gaagaggaag cagctggttg gacaggattt cttgaagagc caggtgctaa gggcatcagg 11640
tcgacatcca tagtaaccat gtgccataac atctacacat ttccacttgt tttacagaca 11700
aggtaacagg cagaaggaaa atccagagtc ttgcagtaag cagatgacaa aacttcaata 11760
tgcttgggca ccacttaggt gaccccaggg agatttagtg tggccttagg aaagcaaaag 11820
agcacttttt attggaaata tgagcttgtc actgggaaag atttgtaaaa ttgatcaaga 11880
acttgattta taattatgcc tcaaaaaaaa aagttctcat ttagtagtgg agcaatctag 11940
aaaacatacc ttttttgttt gtttggaaga tcctctttcc ctggctgtat tgtagtgttt 12000
gctatttgat gtggaaataa ctaataactt aagattttgg aacagaacac cctttagatt 12060
tccaaaacac aattcttatt tcagggaaga cagaccaaaa atatctcctg agatcattgg 12120
tttctttata aattgtggta ccactccatc attgaagaga aaccactacc acaccactag 12180
caccatacag aaccttttct ctgtatcttt gtacaatact acaaaggggt accagggagg 12240
agagagtggc tgaccacttt agtgacaaaa cagcactcca ctgctggtga atcccatcta 12300
attatggtcc ttccaccctt ttcaaccacc aacaactgtt cgtactgtta attcctatcc 12360
tgaaggttta accagtggtt gtctagtatc ttctgtcttt agaacagtgg ttctcaaact 12420
ttagtacaca tcagcatcac ctggagggcc tttttttaaa ataagacaca gattgctggg 12480
ctcatggtca gagttcccag ttaagtaaat caggaaattt gtatttctaa caagtttata 12540
ggtgaggcca atactgctgt tttgggaact atgctttgag aaccactgcc ttgaaaaaat 12600
ttccaacttc tacctttaag atcagcctga cttatcaaac gctagagaaa aactgaatct 12660
acccttgggc agatgacttg ggattggatt ctatacagca gtcttgctca atcttcccag 12720
tttccagttt tattatacca acaattggtt tttacaagct agaagacaat gaatgtataa 12780
gttctatgga acagtgagat aaatctaagc ttcttgtctt tgtatttaga aacattgatt 12840
ctatggatga tcatttgtat catgttgacc ctttgacttg tactgaaggt gattttaaat 12900
ttaagtatgt agtgtttgaa tttcttccat ccatgtcgtt ttaatgagat gtttccatgt 12960
cagctccttt acagccttgg ctcctggctt acagattttt gaatagttgt ttgcttgcca 13020
gttgttttac atctttcatt ggccaccaaa atattagcca tttgagatga gatgagacta 13080
cttgttgtac cttcatcttt catttaattt tctggcgtaa attaacattt taatttcata 13140
tatatctgta aagagtctac ccaaaggctt cacggaaatt tgcaaaatga actaattccc 13200
ttttaagcag caggtgtgcc tgtttttgac ttttcagtaa atatgttgtt tgtgcacata 13260
tctacatggt ggagaccata ttcattattt catcttccaa ataatgggaa aaatataaaa 13320
gtgaatcagt gtgctttggg aattcagtga aatcatgtta actcatatag agggggcctt 13380
agtttatctc ttctttactg aattaattag ttttggaaat tcttttacca ttaaaaaaaa 13440
ttaaggacca tacagagaat gatttaagaa aaaacaagtc acttaaaaat catcacctat 13500
ttataaactg tattaattac acataatgct tattgattca atgaggtttc tctaaagact 13560
tctgcttaat aaatatgctg acttcattta aattagttta gactattgta ggaatggaag 13620
gaaatgatta tatttactag aattagtgag atcagaaagc atatcagaat gttgatgata 13680
tcaaggagac aatctacaga gtttttgcct ctgtggatgg aaataagggt gttttttttt 13740
ggtttttttt ttactttagt ttcccataat ttttggaaat tatgtgtgca tttagttctt 13800
ttagtaacac tgattttaaa attaaatttc aaaagtcaat ctctaagagt aatttatttt 13860
tgttttacca accagtgcca aaaaggagag gagggaatcc aaaagccaat cttttgaacc 13920
aatgtgtaaa agattatgtt ttttcttaaa gttagggagg ctcgggccct gacactgcca 13980
gccccagtga gcatccctgg ctacctcggg attatgtgca agctgctttg tcctacattt 14040
ctttcatctg gttcttattg ggagtgcttc tctctaataa aaattgattt cccacaaaat 14100
aggcaaagct gaacaaagat gaatgctttt gataagttgg gtttcacttc agttgaaaca 14160
atgtgataga atatccaggt gtggcatgat ggggcaggag gaggtgccta gagggaaaag 14220
ttatttttgt ttcttagtgt tgtgttgtgg ggatgggaca gataagaata agatgtttat 14280
tgccctaatc atgctaagag actattattc aatatgcttt tcccgctttt ctaagaggaa 14340
taaacttaga caaattacat tataaacagt tcccctacta ctatctccca ctctagataa 14400
agccagtggg tggtatgggt ccttttattc cttatagtat tatgccaaag aatcaactta 14460
ttttcattga agattataaa taaatgaagc ttgttatagc cataatgatt tgagtcagta 14520
taccatttta cctataaaat gcaaaattca tccttgcaac cccattcacc aggagccttg 14580
aagcattttg tttactccaa aggccttgtc aaggaagcat aattttttgt tttgccttct 14640
tatttagtca gtttggtcat atttacttaa aaaaacaaac tgaaaatcac actcctttat 14700
atgttgatat aactgatttt atagaatctg tctgttcttt gtttaacagg tctctgtaag 14760
caagcttgca agtgtatttt gtgtacattt tatctgaggt ggaaatgaaa attctaaaga 14820
gaaaatattt taaaagatat tgtatttatg ttgcttgtgt tgtagaataa agattcaaat 14880
gcattaaaaa tctggtacat gaaacaattg tgtttactga ataaatatat ataaatatca 14940
aaaaagcact aaaaa 14955


30
2221
PRT
Homo sapiens

30
Met Glu Glu Ile Leu Arg Lys Leu Gln Lys Glu Ala Ser Gly Ser Lys
1 5 10 15
Tyr Lys Ala Ile Lys Glu Ser Cys Thr Trp Ala Leu Glu Thr Leu Gly
20 25 30
Gly Leu Asp Thr Ile Ala Lys Ile Pro Pro His Val Leu Arg Glu Lys
35 40 45
Cys Leu Leu Pro Leu Gln Leu Ala Leu Glu Ser Lys Asn Val Lys Leu
50 55 60
Ala Gln His Ala Leu Ala Gly Met Gln Lys Leu Leu Ser Glu Glu Arg
65 70 75 80
Phe Val Ser Met Glu Thr Asp Ser Asp Glu Lys Gln Leu Leu Asn Gln
85 90 95
Ile Leu Asn Ala Val Lys Val Thr Pro Ser Leu Asn Glu Asp Leu Gln
100 105 110
Val Glu Val Met Lys Val Leu Leu Cys Ile Thr Tyr Thr Pro Thr Phe
115 120 125
Asp Leu Asn Gly Ser Ala Val Leu Lys Ile Ala Glu Val Cys Ile Glu
130 135 140
Thr Tyr Ile Ser Ser Cys His Gln Arg Ser Ile Asn Thr Ala Val Arg
145 150 155 160
Ala Thr Leu Ser Gln Met Leu Ser Asp Leu Thr Leu Gln Leu Arg Gln
165 170 175
Arg Gln Glu Asn Thr Ile Ile Glu Asn Pro Asp Val Pro Gln Asp Phe
180 185 190
Gly Asn Gln Gly Ser Thr Val Glu Ser Leu Cys Asp Asp Val Val Ser
195 200 205
Val Leu Thr Val Leu Cys Glu Lys Leu Gln Ala Ala Ile Lys Cys Pro
210 215 220
Ser Phe Leu Thr Met Ala Cys Trp Asn Ser Gly Ala Gly Thr Gln Ile
225 230 235 240
Thr Ile Leu Thr Glu Gly Ser Ser Thr Asn Cys Ser Asp Pro Ile Trp
245 250 255
Asp Thr Thr Ala Ser Pro Val Ala Ala Ser Asp Ser Gln Gln Leu Gln
260 265 270
Leu Leu Tyr Leu Glu Cys Ile Leu Ser Val Leu Ser Ser Ser Ser Ser
275 280 285
Ser Met His Leu His Arg Arg Phe Thr Asp Leu Ile Trp Lys Asn Leu
290 295 300
Cys Pro Ala Leu Ile Val Ile Leu Gly Asn Pro Ile His Asp Lys Thr
305 310 315 320
Ile Thr Ser Ala His Thr Ser Ser Thr Ser Thr Ser Leu Glu Ser Asp
325 330 335
Ser Ala Ser Pro Gly Val Ser Asp His Gly Arg Gly Ser Gly Cys Ser
340 345 350
Cys Thr Ala Pro Ala Leu Ser Gly Pro Val Ala Arg Thr Ile Tyr Tyr
355 360 365
Ile Ala Ala Glu Leu Val Arg Leu Val Gly Ser Val Asp Ser Met Lys
370 375 380
Pro Val Leu Gln Ser Leu Tyr His Arg Val Leu Leu Tyr Pro Pro Pro
385 390 395 400
Gln His Arg Val Glu Ala Ile Lys Ile Met Lys Glu Ile Leu Gly Ser
405 410 415
Pro Gln Arg Leu Cys Asp Leu Ala Gly Pro Ser Ser Thr Glu Ser Glu
420 425 430
Ser Arg Lys Arg Ser Ile Ser Lys Arg Lys Ser His Leu Asp Leu Leu
435 440 445
Lys Leu Ile Met Asp Gly Met Thr Glu Ala Cys Ile Lys Gly Gly Ile
450 455 460
Glu Ala Cys Tyr Ala Ala Val Ser Cys Val Cys Thr Leu Leu Gly Ala
465 470 475 480
Leu Asp Glu Leu Ser Gln Gly Lys Gly Leu Ser Glu Gly Gln Val Gln
485 490 495
Leu Leu Leu Leu Arg Leu Glu Glu Leu Lys Asp Gly Ala Glu Trp Ser
500 505 510
Arg Asp Ser Met Glu Ile Asn Glu Ala Asp Phe Arg Trp Gln Arg Arg
515 520 525
Val Leu Ser Ser Glu His Thr Pro Trp Glu Ser Gly Asn Glu Arg Ser
530 535 540
Leu Asp Ile Ser Ile Ser Val Thr Thr Asp Thr Gly Gln Thr Thr Leu
545 550 555 560
Glu Gly Glu Leu Gly Gln Thr Thr Pro Glu Asp His Ser Gly Asn His
565 570 575
Lys Asn Ser Leu Lys Ser Pro Ala Ile Pro Glu Gly Lys Glu Thr Leu
580 585 590
Ser Lys Val Leu Glu Thr Glu Ala Val Asp Gln Pro Asp Val Val Gln
595 600 605
Arg Ser His Thr Val Pro Tyr Pro Asp Ile Thr Asn Phe Leu Ser Val
610 615 620
Asp Cys Arg Thr Arg Ser Tyr Gly Ser Arg Tyr Ser Glu Ser Asn Phe
625 630 635 640
Ser Val Asp Asp Gln Asp Leu Ser Arg Thr Glu Phe Asp Ser Cys Asp
645 650 655
Gln Tyr Ser Met Ala Ala Glu Lys Asp Ser Gly Arg Ser Asp Val Ser
660 665 670
Asp Ile Gly Ser Asp Asn Cys Ser Leu Ala Asp Glu Glu Gln Thr Pro
675 680 685
Arg Asp Cys Leu Gly His Arg Ser Leu Arg Thr Ala Ala Leu Ser Leu
690 695 700
Lys Leu Leu Lys Asn Gln Glu Ala Asp Gln His Ser Ala Arg Leu Phe
705 710 715 720
Ile Gln Ser Leu Glu Gly Leu Leu Pro Arg Leu Leu Ser Leu Ser Asn
725 730 735
Val Glu Glu Val Asp Thr Ala Leu Gln Asn Phe Ala Ser Thr Phe Cys
740 745 750
Ser Gly Met Met His Ser Pro Gly Phe Asp Gly Asn Ser Ser Leu Ser
755 760 765
Phe Gln Met Leu Met Asn Ala Asp Ser Leu Tyr Thr Ala Ala His Cys
770 775 780
Ala Leu Leu Leu Asn Leu Lys Leu Ser His Gly Asp Tyr Tyr Arg Lys
785 790 795 800
Arg Pro Thr Leu Ala Pro Gly Val Met Lys Asp Phe Met Lys Gln Val
805 810 815
Gln Thr Ser Gly Val Leu Met Val Phe Ser Gln Ala Trp Ile Glu Glu
820 825 830
Leu Tyr His Gln Val Leu Asp Arg Asn Met Leu Gly Glu Ala Gly Tyr
835 840 845
Trp Gly Ser Pro Glu Asp Asn Ser Leu Pro Leu Ile Thr Met Leu Thr
850 855 860
Asp Ile Asp Gly Leu Glu Ser Ser Ala Ile Gly Gly Gln Leu Met Ala
865 870 875 880
Ser Ala Ala Thr Glu Ser Pro Phe Ala Gln Ser Arg Arg Ile Asp Asp
885 890 895
Ser Thr Val Ala Gly Val Ala Phe Ala Arg Tyr Ile Leu Val Gly Cys
900 905 910
Trp Lys Asn Leu Ile Asp Thr Leu Ser Thr Pro Leu Thr Gly Arg Met
915 920 925
Ala Gly Ser Ser Lys Gly Leu Ala Phe Ile Leu Gly Ala Glu Gly Ile
930 935 940
Lys Glu Gln Asn Gln Lys Glu Arg Asp Ala Ile Cys Met Ser Leu Asp
945 950 955 960
Gly Leu Arg Lys Ala Ala Arg Leu Ser Cys Ala Leu Gly Val Ala Ala
965 970 975
Asn Cys Ala Ser Ala Leu Ala Gln Met Ala Ala Ala Ser Cys Val Gln
980 985 990
Glu Glu Lys Glu Glu Arg Glu Ala Gln Glu Pro Ser Asp Ala Ile Thr
995 1000 1005
Gln Val Lys Leu Lys Val Glu Gln Lys Leu Glu Gln Ile Gly Lys
1010 1015 1020
Val Gln Gly Val Trp Leu His Thr Ala His Val Leu Cys Met Glu
1025 1030 1035
Ala Ile Leu Ser Val Gly Leu Glu Met Gly Ser His Asn Pro Asp
1040 1045 1050
Cys Trp Pro His Val Phe Arg Val Cys Glu Tyr Val Gly Thr Leu
1055 1060 1065
Glu His Asn His Phe Ser Asp Gly Ala Ser Gln Pro Pro Leu Thr
1070 1075 1080
Ile Ser Gln Pro Gln Lys Ala Thr Gly Ser Ala Gly Leu Leu Gly
1085 1090 1095
Asp Pro Glu Cys Glu Gly Ser Pro Pro Glu His Ser Pro Glu Gln
1100 1105 1110
Gly Arg Ser Leu Ser Thr Ala Pro Val Val Gln Pro Leu Ser Ile
1115 1120 1125
Gln Asp Leu Val Arg Glu Gly Ser Arg Gly Arg Ala Ser Asp Phe
1130 1135 1140
Arg Gly Gly Ser Leu Met Ser Gly Ser Ser Ala Ala Lys Val Val
1145 1150 1155
Leu Thr Leu Ser Thr Gln Ala Asp Arg Leu Phe Glu Asp Ala Thr
1160 1165 1170
Asp Lys Leu Asn Leu Met Ala Leu Gly Gly Phe Leu Tyr Gln Leu
1175 1180 1185
Lys Lys Ala Ser Gln Ser Gln Leu Phe His Ser Val Thr Asp Thr
1190 1195 1200
Val Asp Tyr Ser Leu Ala Met Pro Gly Glu Val Lys Ser Thr Gln
1205 1210 1215
Asp Arg Lys Ser Ala Leu His Leu Phe Arg Leu Gly Asn Ala Met
1220 1225 1230
Leu Arg Ile Val Arg Ser Lys Ala Arg Pro Leu Leu His Val Met
1235 1240 1245
Arg Cys Trp Ser Leu Val Ala Pro His Leu Val Glu Ala Ala Cys
1250 1255 1260
His Lys Glu Arg His Val Ser Gln Lys Ala Val Ser Phe Ile His
1265 1270 1275
Asp Ile Leu Thr Glu Val Leu Thr Asp Trp Asn Glu Pro Pro His
1280 1285 1290
Phe His Phe Asn Glu Ala Leu Phe Arg Pro Phe Glu Arg Ile Met
1295 1300 1305
Gln Leu Glu Leu Cys Asp Glu Asp Val Gln Asp Gln Val Val Thr
1310 1315 1320
Ser Ile Gly Glu Leu Val Glu Val Cys Ser Thr Gln Ile Gln Ser
1325 1330 1335
Gly Trp Arg Pro Leu Phe Ser Ala Leu Glu Thr Val His Gly Gly
1340 1345 1350
Asn Lys Ser Glu Met Lys Glu Tyr Leu Val Gly Asp Tyr Ser Met
1355 1360 1365
Gly Lys Gly Gln Ala Pro Val Phe Asp Val Phe Glu Ala Phe Leu
1370 1375 1380
Asn Thr Asp Asn Ile Gln Val Phe Ala Asn Ala Ala Thr Ser Tyr
1385 1390 1395
Ile Met Cys Leu Met Lys Phe Val Lys Gly Leu Gly Glu Val Asp
1400 1405 1410
Cys Lys Glu Ile Gly Asp Cys Ala Pro Ala Pro Gly Ala Pro Ser
1415 1420 1425
Thr Asp Leu Cys Leu Pro Ala Leu Asp Tyr Leu Arg Arg Cys Ser
1430 1435 1440
Gln Leu Leu Ala Lys Ile Tyr Lys Met Pro Leu Lys Pro Ile Phe
1445 1450 1455
Leu Ser Gly Arg Leu Ala Gly Leu Pro Arg Arg Leu Gln Glu Gln
1460 1465 1470
Ser Ala Ser Ser Glu Asp Gly Ile Glu Ser Val Leu Ser Asp Phe
1475 1480 1485
Asp Asp Asp Thr Gly Leu Ile Glu Val Trp Ile Ile Leu Leu Glu
1490 1495 1500
Gln Leu Thr Ala Ala Val Ser Asn Cys Pro Arg Gln His Gln Pro
1505 1510 1515
Pro Thr Leu Asp Leu Leu Phe Glu Leu Leu Arg Asp Val Thr Lys
1520 1525 1530
Thr Pro Gly Pro Gly Phe Gly Ile Tyr Ala Val Val His Leu Leu
1535 1540 1545
Leu Pro Val Met Ser Val Trp Leu Arg Arg Ser His Lys Asp His
1550 1555 1560
Ser Tyr Trp Asp Met Ala Ser Ala Asn Phe Lys His Ala Ile Gly
1565 1570 1575
Leu Ser Cys Glu Leu Val Val Glu His Ile Gln Ser Phe Leu His
1580 1585 1590
Ser Asp Ile Arg Tyr Glu Ser Met Ile Asn Thr Met Leu Lys Asp
1595 1600 1605
Leu Phe Glu Leu Leu Val Ala Cys Val Ala Lys Pro Thr Glu Thr
1610 1615 1620
Ile Ser Arg Val Gly Cys Ser Cys Ile Arg Tyr Val Leu Val Thr
1625 1630 1635
Ala Gly Pro Val Phe Thr Glu Glu Met Trp Arg Leu Ala Cys Cys
1640 1645 1650
Ala Leu Gln Asp Ala Phe Ser Ala Thr Leu Lys Pro Val Lys Asp
1655 1660 1665
Leu Leu Gly Cys Phe His Ser Gly Thr Glu Ser Phe Ser Gly Glu
1670 1675 1680
Gly Cys Gln Val Arg Val Ala Ala Pro Ser Ser Ser Pro Ser Ala
1685 1690 1695
Glu Ala Glu Tyr Trp Arg Ile Arg Ala Met Ala Gln Gln Val Phe
1700 1705 1710
Met Leu Asp Thr Gln Cys Ser Pro Lys Thr Pro Asn Asn Phe Asp
1715 1720 1725
His Ala Gln Ser Cys Gln Leu Ile Ile Glu Leu Pro Pro Asp Glu
1730 1735 1740
Lys Pro Asn Gly His Thr Lys Lys Ser Val Ser Phe Arg Glu Ile
1745 1750 1755
Val Val Ser Leu Leu Ser His Gln Val Leu Leu Gln Asn Leu Tyr
1760 1765 1770
Asp Ile Leu Leu Glu Glu Phe Val Lys Gly Pro Ser Pro Gly Glu
1775 1780 1785
Glu Lys Thr Ile Gln Val Pro Glu Ala Lys Leu Ala Gly Phe Leu
1790 1795 1800
Arg Tyr Ile Ser Met Gln Asn Leu Ala Val Ile Phe Asp Leu Leu
1805 1810 1815
Leu Asp Ser Tyr Arg Thr Ala Arg Glu Phe Asp Thr Ser Pro Gly
1820 1825 1830
Leu Lys Cys Leu Leu Lys Lys Val Ser Gly Ile Gly Gly Ala Ala
1835 1840 1845
Asn Leu Tyr Arg Gln Ser Ala Met Ser Phe Asn Ile Tyr Phe His
1850 1855 1860
Ala Leu Val Cys Ala Val Leu Thr Asn Gln Glu Thr Ile Thr Ala
1865 1870 1875
Glu Gln Val Lys Lys Val Leu Phe Glu Asp Asp Glu Arg Ser Thr
1880 1885 1890
Asp Ser Ser Gln Gln Cys Ser Ser Glu Asp Glu Asp Ile Phe Glu
1895 1900 1905
Glu Thr Ala Gln Val Ser Pro Pro Arg Gly Lys Glu Lys Arg Gln
1910 1915 1920
Trp Arg Ala Arg Met Pro Leu Leu Ser Val Gln Pro Val Ser Asn
1925 1930 1935
Ala Asp Trp Val Trp Leu Val Lys Arg Leu His Lys Leu Cys Met
1940 1945 1950
Glu Leu Cys Asn Asn Tyr Ile Gln Met His Leu Asp Leu Glu Asn
1955 1960 1965
Cys Met Glu Glu Pro Pro Ile Phe Lys Gly Asp Pro Phe Phe Ile
1970 1975 1980
Leu Pro Ser Phe Gln Ser Glu Ser Ser Thr Pro Ser Thr Gly Gly
1985 1990 1995
Phe Ser Gly Lys Glu Thr Pro Ser Glu Asp Asp Arg Ser Gln Ser
2000 2005 2010
Arg Glu His Met Gly Glu Ser Leu Ser Leu Lys Ala Gly Gly Gly
2015 2020 2025
Asp Leu Leu Leu Pro Pro Ser Pro Lys Val Glu Lys Lys Asp Pro
2030 2035 2040
Ser Arg Lys Lys Glu Trp Trp Glu Asn Ala Gly Asn Lys Ile Tyr
2045 2050 2055
Thr Met Ala Ala Asp Lys Thr Ile Ser Lys Leu Met Thr Glu Tyr
2060 2065 2070
Lys Lys Arg Lys Gln Gln His Asn Leu Ser Ala Phe Pro Lys Glu
2075 2080 2085
Val Lys Val Glu Lys Lys Gly Glu Pro Leu Gly Pro Arg Gly Gln
2090 2095 2100
Asp Ser Pro Leu Leu Gln Arg Pro Gln His Leu Met Asp Gln Gly
2105 2110 2115
Gln Met Arg His Ser Phe Ser Ala Gly Pro Glu Leu Leu Arg Gln
2120 2125 2130
Asp Lys Arg Pro Arg Ser Gly Ser Thr Gly Ser Ser Leu Ser Val
2135 2140 2145
Ser Val Arg Asp Ala Glu Ala Gln Ile Gln Ala Trp Thr Asn Met
2150 2155 2160
Val Leu Thr Val Leu Asn Gln Ile Gln Ile Leu Pro Asp Gln Thr
2165 2170 2175
Phe Thr Ala Leu Gln Pro Ala Val Phe Pro Cys Ile Ser Gln Leu
2180 2185 2190
Thr Cys His Val Thr Asp Ile Arg Val Arg Gln Ala Val Arg Glu
2195 2200 2205
Trp Leu Gly Arg Val Gly Arg Val Tyr Asp Ile Ile Val
2210 2215 2220


31
1522
PRT
Homo sapiens

31
Met Ser Val Arg Leu Pro Gln Ser Ile Asp Arg Leu Ser Ser Leu Ser
1 5 10 15
Ser Leu Gly Asp Ser Ala Pro Glu Arg Lys Ser Pro Ser His His Arg
20 25 30
Gln Pro Ser Asp Ala Ser Glu Thr Thr Gly Leu Val Gln Arg Cys Val
35 40 45
Ile Ile Gln Lys Asp Gln His Gly Phe Gly Phe Thr Val Ser Gly Asp
50 55 60
Arg Ile Val Leu Val Gln Ser Val Arg Pro Gly Gly Ala Ala Met Lys
65 70 75 80
Ala Gly Val Lys Glu Gly Asp Arg Ile Ile Lys Val Asn Gly Thr Met
85 90 95
Val Thr Asn Ser Ser His Leu Glu Val Val Lys Leu Ile Lys Ser Gly
100 105 110
Ala Tyr Val Ala Leu Thr Leu Leu Gly Ser Ser Pro Ser Ser Met Gly
115 120 125
Ile Ser Gly Leu Gln Gln Asp Pro Ser Pro Ala Gly Ala Pro Arg Ile
130 135 140
Thr Ser Val Ile Pro Ser Pro Pro Pro Pro Pro Pro Leu Pro Pro Pro
145 150 155 160
Gln Arg Ile Thr Gly Pro Lys Pro Leu Gln Asp Pro Glu Val Gln Lys
165 170 175
His Ala Thr Gln Ile Leu Arg Asn Met Leu Arg Gln Glu Glu Lys Glu
180 185 190
Leu Gln Asp Ile Leu Pro Leu Tyr Gly Asp Thr Ser Gln Arg Pro Ser
195 200 205
Glu Gly Arg Leu Ser Leu Asp Ser Gln Glu Gly Asp Ser Gly Leu Asp
210 215 220
Ser Gly Thr Glu Arg Phe Pro Ser Leu Ser Glu Ser Leu Met Asn Arg
225 230 235 240
Asn Ser Val Leu Ser Asp Pro Gly Leu Asp Ser Pro Arg Thr Ser Pro
245 250 255
Val Ile Met Ala Arg Val Ala Gln His His Arg Arg Gln Gly Ser Asp
260 265 270
Ala Ala Val Pro Ser Thr Gly Asp Gln Gly Val Asp Gln Ser Pro Lys
275 280 285
Pro Leu Ile Ile Gly Pro Glu Glu Asp Tyr Asp Pro Gly Tyr Phe Asn
290 295 300
Asn Glu Ser Asp Ile Ile Phe Gln Asp Leu Glu Lys Leu Lys Ser Arg
305 310 315 320
Pro Ala His Leu Gly Val Phe Leu Arg Tyr Ile Phe Ser Gln Ala Asp
325 330 335
Pro Ser Pro Leu Leu Phe Tyr Leu Cys Ala Glu Val Tyr Gln Gln Ala
340 345 350
Ser Pro Lys Asp Ser Arg Ser Leu Gly Lys Asp Ile Trp Asn Ile Phe
355 360 365
Leu Glu Lys Asn Ala Pro Leu Arg Val Lys Ile Pro Glu Met Leu Gln
370 375 380
Ala Glu Ile Asp Ser Arg Leu Arg Asn Ser Glu Asp Ala Arg Gly Val
385 390 395 400
Leu Cys Glu Ala Gln Glu Ala Ala Met Pro Glu Ile Gln Glu Gln Ile
405 410 415
His Asp Tyr Arg Thr Lys Arg Thr Leu Gly Leu Gly Ser Leu Tyr Gly
420 425 430
Glu Asn Asp Leu Leu Asp Leu Asp Gly Asp Pro Leu Arg Glu Arg Gln
435 440 445
Val Ala Glu Lys Gln Leu Ala Ala Leu Gly Asp Ile Leu Ser Lys Tyr
450 455 460
Glu Glu Asp Arg Ser Ala Pro Met Asp Phe Ala Leu Asn Thr Tyr Met
465 470 475 480
Ser His Ala Gly Ile Arg Leu Arg Glu Ala Arg Pro Ser Asn Thr Ala
485 490 495
Glu Lys Ala Gln Ser Ala Pro Asp Lys Asp Lys Trp Leu Pro Phe Phe
500 505 510
Pro Lys Thr Lys Lys Ser Ser Asn Ser Lys Lys Glu Lys Asp Ala Leu
515 520 525
Glu Asp Lys Lys Arg Asn Pro Ile Leu Lys Tyr Ile Gly Lys Pro Lys
530 535 540
Ser Ser Ser Gln Ser Thr Phe His Ile Pro Leu Ser Pro Val Glu Val
545 550 555 560
Lys Pro Gly Asn Val Arg Asn Ile Ile Gln His Phe Glu Asn Asn Gln
565 570 575
Gln Tyr Asp Ala Pro Glu Pro Gly Thr Gln Arg Leu Ser Thr Gly Ser
580 585 590
Phe Pro Glu Asp Leu Leu Glu Ser Asp Ser Ser Arg Ser Glu Ile Arg
595 600 605
Leu Gly Arg Ser Glu Ser Leu Lys Gly Arg Glu Glu Met Lys Arg Ser
610 615 620
Arg Lys Ala Glu Asn Val Pro Arg Ser Arg Ser Asp Val Asp Met Asp
625 630 635 640
Ala Ala Ala Glu Ala Thr Arg Leu His Gln Ser Ala Ser Ser Ser Thr
645 650 655
Ser Ser Leu Ser Thr Arg Ser Leu Glu Asn Pro Thr Pro Pro Phe Thr
660 665 670
Pro Lys Met Gly Arg Arg Ser Ile Glu Ser Pro Ser Leu Gly Phe Cys
675 680 685
Thr Asp Thr Leu Leu Pro His Leu Leu Glu Asp Asp Leu Gly Gln Leu
690 695 700
Ser Asp Leu Glu Pro Glu Pro Asp Ala Gln Asn Trp Gln His Thr Val
705 710 715 720
Gly Lys Asp Val Val Ala Gly Leu Thr Gln Arg Glu Ile Asp Arg Gln
725 730 735
Glu Val Ile Asn Glu Leu Phe Val Thr Glu Ala Ser His Leu Arg Thr
740 745 750
Leu Arg Val Leu Asp Leu Ile Phe Tyr Gln Arg Met Lys Lys Glu Asn
755 760 765
Leu Met Pro Arg Glu Glu Leu Ala Arg Leu Phe Pro Asn Leu Pro Glu
770 775 780
Leu Ile Glu Ile His Asn Ser Trp Cys Glu Ala Met Lys Lys Leu Arg
785 790 795 800
Glu Glu Gly Pro Ile Ile Lys Glu Ile Ser Asp Leu Met Leu Ala Arg
805 810 815
Phe Asp Gly Pro Ala Arg Glu Glu Leu Gln Gln Val Ala Ala Gln Phe
820 825 830
Cys Ser Tyr Gln Ser Ile Ala Leu Glu Leu Ile Lys Thr Lys Gln Arg
835 840 845
Lys Glu Ser Arg Phe Gln Leu Phe Met Gln Glu Ala Glu Ser His Pro
850 855 860
Gln Cys Arg Arg Leu Gln Leu Arg Asp Leu Ile Ile Ser Glu Met Gln
865 870 875 880
Arg Leu Thr Lys Tyr Pro Leu Leu Leu Glu Ser Ile Ile Lys His Thr
885 890 895
Glu Gly Gly Thr Ser Glu His Glu Lys Leu Cys Arg Ala Arg Asp Gln
900 905 910
Cys Arg Glu Ile Leu Lys Tyr Val Asn Glu Ala Val Lys Gln Thr Glu
915 920 925
Asn Arg His Arg Leu Glu Gly Tyr Gln Lys Arg Leu Asp Ala Thr Ala
930 935 940
Leu Glu Arg Ala Ser Asn Pro Leu Ala Ala Glu Phe Lys Ser Leu Asp
945 950 955 960
Leu Thr Thr Arg Lys Met Ile His Glu Gly Pro Leu Thr Trp Arg Ile
965 970 975
Ser Lys Asp Lys Thr Leu Asp Leu His Val Leu Leu Leu Glu Asp Leu
980 985 990
Leu Val Leu Leu Gln Lys Gln Asp Glu Lys Leu Leu Leu Lys Cys His
995 1000 1005
Ser Lys Thr Ala Val Gly Ser Ser Asp Ser Lys Gln Thr Phe Ser
1010 1015 1020
Pro Val Leu Lys Leu Asn Ala Val Leu Ile Arg Ser Val Ala Thr
1025 1030 1035
Asp Lys Arg Ala Phe Phe Ile Ile Cys Thr Ser Lys Leu Gly Pro
1040 1045 1050
Pro Gln Ile Tyr Glu Leu Val Ala Leu Thr Ser Ser Asp Lys Asn
1055 1060 1065
Thr Trp Met Glu Leu Leu Glu Glu Ala Val Arg Asn Ala Thr Arg
1070 1075 1080
His Pro Gly Ala Ala Pro Met Pro Val His Pro Pro Pro Pro Gly
1085 1090 1095
Pro Arg Glu Pro Ala Gln Gln Gly Pro Thr Pro Ser Arg Val Glu
1100 1105 1110
Leu Asp Asp Ser Asp Val Phe His Gly Glu Pro Glu Pro Glu Glu
1115 1120 1125
Leu Pro Gly Gly Thr Gly Ser Gln Gln Arg Val Gln Gly Lys His
1130 1135 1140
Gln Val Leu Leu Glu Asp Pro Glu Gln Glu Gly Ser Ala Glu Glu
1145 1150 1155
Glu Glu Leu Gly Val Leu Pro Cys Pro Ser Thr Ser Leu Asp Gly
1160 1165 1170
Glu Asn Arg Gly Ile Arg Thr Arg Asn Pro Ile His Leu Ala Phe
1175 1180 1185
Pro Gly Pro Leu Phe Met Glu Gly Leu Ala Asp Ser Ala Leu Glu
1190 1195 1200
Asp Val Glu Asn Leu Arg His Leu Ile Leu Trp Ser Leu Leu Pro
1205 1210 1215
Gly His Thr Met Glu Thr Gln Ala Ala Gln Glu Pro Glu Asp Asp
1220 1225 1230
Leu Thr Pro Thr Pro Ser Val Ile Ser Val Thr Ser His Pro Trp
1235 1240 1245
Asp Pro Gly Ser Pro Gly Gln Ala Pro Pro Gly Gly Glu Gly Asp
1250 1255 1260
Asn Thr Gln Leu Ala Gly Leu Glu Gly Glu Arg Pro Glu Gln Glu
1265 1270 1275
Asp Met Gly Leu Cys Ser Leu Glu His Leu Pro Pro Arg Thr Arg
1280 1285 1290
Asn Ser Gly Ile Trp Glu Ser Pro Glu Leu Asp Arg Asn Leu Ala
1295 1300 1305
Glu Asp Ala Ser Ser Thr Glu Ala Ala Gly Gly Tyr Lys Val Val
1310 1315 1320
Arg Lys Ala Glu Val Ala Gly Ser Lys Val Val Pro Ala Leu Pro
1325 1330 1335
Glu Ser Gly Gln Ser Glu Pro Gly Pro Pro Glu Val Glu Gly Gly
1340 1345 1350
Thr Lys Ala Thr Gly Asn Cys Phe Tyr Val Ser Met Pro Ser Gly
1355 1360 1365
Pro Pro Asp Ser Ser Thr Asp His Ser Glu Ala Pro Met Ser Pro
1370 1375 1380
Pro Gln Pro Asp Ser Leu Pro Ala Gly Gln Thr Glu Pro Gln Pro
1385 1390 1395
Gln Leu Gln Gly Gly Asn Asp Asp Pro Arg Arg Pro Ser Arg Ser
1400 1405 1410
Pro Pro Ser Leu Ala Leu Arg Asp Val Gly Met Ile Phe His Thr
1415 1420 1425
Ile Glu Gln Leu Thr Leu Lys Leu Asn Arg Leu Lys Asp Met Glu
1430 1435 1440
Leu Ala His Arg Glu Leu Leu Lys Ser Leu Gly Gly Glu Ser Ser
1445 1450 1455
Gly Gly Thr Thr Pro Val Gly Ser Phe His Thr Glu Ala Ala Arg
1460 1465 1470
Trp Thr Asp Gly Ser Leu Ser Pro Pro Ala Lys Glu Pro Leu Ala
1475 1480 1485
Ser Asp Ser Arg Asn Ser His Glu Leu Gly Pro Cys Pro Glu Asp
1490 1495 1500
Gly Ser Asp Ala Pro Leu Glu Asp Ser Thr Ala Asp Ala Ala Ala
1505 1510 1515
Ser Pro Gly Pro
1520


32
577
PRT
Homo sapiens

32
Met Cys Lys Glu Gln Lys Ala Thr Lys Lys Ser Lys Val Gly Phe Leu
1 5 10 15
Asp Pro Leu Ala Thr Asp Asn Gln Lys Glu Cys Glu Ala Trp Pro Asp
20 25 30
Leu Arg Thr Ser Glu Glu Asp Ser Lys Ser Cys Ser Gly Ala Leu Ser
35 40 45
Thr Ala Leu Glu Glu Leu Ala Lys Val Ser Glu Glu Leu Cys Ser Phe
50 55 60
Gln Glu Glu Ile Arg Lys Arg Ser Asn His Arg Arg Met Lys Ser Asp
65 70 75 80
Ser Phe Leu Gln Glu Met Pro Asn Val Thr Asn Ile Pro His Gly Asp
85 90 95
Pro Met Ile Asn Asn Asp Gln Cys Ile Leu Pro Ile Ser Leu Glu Lys
100 105 110
Glu Lys Gln Lys Asn Arg Lys Asn Leu Ser Cys Thr Asn Val Leu Gln
115 120 125
Ser Asn Ser Thr Lys Lys Cys Gly Ile Asp Thr Ile Asp Leu Lys Arg
130 135 140
Asn Glu Thr Pro Pro Val Pro Pro Pro Arg Ser Thr Ser Arg Asn Phe
145 150 155 160
Pro Ser Ser Asp Ser Glu Gln Ala Tyr Glu Arg Trp Lys Glu Arg Leu
165 170 175
Asp His Asn Ser Trp Val Pro His Glu Gly Arg Ser Lys Arg Asn Tyr
180 185 190
Asn Pro His Phe Pro Leu Arg Gln Gln Glu Met Ser Met Leu Tyr Pro
195 200 205
Asn Glu Gly Lys Thr Ser Lys Asp Gly Ile Ile Phe Ser Ser Leu Val
210 215 220
Pro Glu Val Lys Ile Asp Ser Lys Pro Pro Ser Asn Glu Asp Val Gly
225 230 235 240
Leu Ser Met Trp Ser Cys Asp Ile Gly Ile Gly Ala Lys Arg Ser Pro
245 250 255
Ser Thr Ser Trp Phe Gln Lys Thr Cys Ser Thr Pro Ser Asn Pro Lys
260 265 270
Tyr Glu Met Val Ile Pro Asp His Pro Ala Lys Ser His Pro Asp Leu
275 280 285
His Val Ser Asn Asp Cys Ser Ser Ser Val Ala Glu Ser Ser Ser Pro
290 295 300
Leu Arg Asn Phe Ser Cys Gly Phe Glu Arg Thr Thr Arg Asn Glu Lys
305 310 315 320
Leu Ala Ala Lys Thr Asp Glu Phe Asn Arg Thr Val Phe Arg Thr Asp
325 330 335
Arg Asn Cys Gln Ala Ile Gln Gln Asn His Ser Cys Ser Lys Ser Ser
340 345 350
Glu Asp Leu Lys Pro Cys Asp Thr Ser Ser Thr His Thr Gly Ser Ile
355 360 365
Ser Gln Ser Asn Asp Val Ser Gly Ile Trp Lys Thr Asn Ala His Met
370 375 380
Pro Val Pro Met Glu Asn Val Pro Asp Asn Pro Thr Lys Lys Ser Thr
385 390 395 400
Thr Gly Leu Val Arg Gln Met Gln Gly His Leu Ser Pro Arg Ser Tyr
405 410 415
Arg Asn Met Leu His Glu His Asp Trp Arg Pro Ser Asn Leu Ser Gly
420 425 430
Arg Pro Arg Ser Ala Asp Pro Arg Ser Asn Tyr Gly Val Val Glu Lys
435 440 445
Leu Leu Lys Thr Tyr Glu Thr Ala Thr Glu Ser Ala Leu Gln Asn Ser
450 455 460
Lys Cys Phe Gln Asp Asn Trp Thr Lys Cys Asn Ser Asp Val Ser Gly
465 470 475 480
Gly Ala Thr Leu Ser Gln His Leu Glu Met Leu Gln Met Glu Gln Gln
485 490 495
Phe Gln Gln Lys Thr Ala Val Trp Gly Gly Gln Glu Val Lys Gln Gly
500 505 510
Ile Asp Pro Lys Lys Ile Thr Glu Glu Ser Met Ser Val Asn Ala Ser
515 520 525
His Gly Lys Gly Phe Ser Arg Pro Ala Arg Pro Ala Asn Arg Arg Leu
530 535 540
Pro Ser Arg Trp Ala Ser Arg Ser Pro Ser Ala Pro Pro Ala Leu Arg
545 550 555 560
Arg Thr Thr His Asn Tyr Thr Ile Ser Leu Arg Ser Glu Ala Leu Met
565 570 575
Val


33
248
PRT
Homo sapiens

33
Met Gly Met Glu Arg Pro Ala Ala Arg Glu Pro His Gly Pro Asp Ala
1 5 10 15
Leu Arg Arg Phe Gln Gly Leu Leu Leu Asp Arg Arg Gly Arg Leu His
20 25 30
Arg Gln Val Leu Arg Leu Arg Glu Val Ala Arg Arg Leu Glu Arg Leu
35 40 45
Arg Arg Arg Ser Leu Val Ala Asn Val Ala Gly Ser Ser Leu Ser Ala
50 55 60
Thr Gly Ala Leu Ala Ala Ile Val Gly Leu Ser Leu Ser Pro Val Thr
65 70 75 80
Leu Gly Thr Ser Leu Leu Val Ser Ala Val Gly Leu Gly Val Ala Thr
85 90 95
Ala Gly Gly Ala Val Thr Ile Thr Ser Asp Leu Ser Leu Ile Phe Cys
100 105 110
Asn Ser Arg Glu Leu Arg Arg Val Gln Glu Ile Ala Ala Thr Cys Gln
115 120 125
Asp Gln Met Arg Glu Ile Leu Ser Cys Leu Glu Phe Phe Cys Arg Trp
130 135 140
Gln Gly Cys Gly Asp Arg Gln Leu Leu Gln Cys Gly Arg Asn Ala Ser
145 150 155 160
Ile Ala Leu Tyr Asn Ser Val Tyr Phe Ile Val Phe Phe Gly Ser Arg
165 170 175
Gly Phe Leu Ile Pro Arg Arg Ala Glu Gly Asp Thr Lys Val Ser Gln
180 185 190
Ala Val Leu Lys Ala Lys Ile Gln Lys Leu Ala Glu Ser Leu Glu Ser
195 200 205
Cys Thr Gly Ala Leu Asp Glu Leu Ser Glu Gln Leu Glu Ser Arg Val
210 215 220
Gln Leu Cys Thr Lys Ser Ser Arg Gly His Asp Leu Lys Ile Ser Ala
225 230 235 240
Asp Gln Arg Ala Gly Leu Phe Phe
245


34
2158
PRT
Homo sapiens

34
Met Val Ser Ile Asp Leu His Gln Ala Gly Arg Val Asp Ser Gln Ala
1 5 10 15
Ser Ile Thr Gln Asp Ser Asp Ser Ile Lys Lys Pro Glu Glu Ile Lys
20 25 30
Gln Cys Asn Asp Ala Pro Val Ser Val Leu Gln Glu Asp Ile Val Gly
35 40 45
Ser Leu Lys Ser Thr Pro Glu Asn His Pro Glu Thr Pro Lys Lys Lys
50 55 60
Ser Asp Pro Glu Leu Ser Lys Ser Glu Met Lys Gln Ser Glu Ser Arg
65 70 75 80
Leu Ala Glu Ser Lys Pro Asn Glu Asn Arg Leu Val Glu Thr Lys Ser
85 90 95
Ser Glu Asn Lys Leu Glu Thr Lys Val Glu Thr Gln Thr Glu Glu Leu
100 105 110
Lys Gln Asn Glu Ser Arg Thr Thr Glu Cys Lys Gln Asn Glu Ser Thr
115 120 125
Ile Val Glu Pro Lys Gln Asn Glu Asn Arg Leu Ser Asp Thr Lys Pro
130 135 140
Asn Asp Asn Lys Gln Asn Asn Gly Arg Ser Glu Thr Thr Lys Ser Arg
145 150 155 160
Pro Glu Thr Pro Lys Gln Lys Gly Glu Ser Arg Pro Glu Thr Pro Lys
165 170 175
Gln Lys Ser Asp Gly His Pro Glu Thr Pro Lys Gln Lys Gly Asp Gly
180 185 190
Arg Pro Glu Thr Pro Lys Gln Lys Gly Glu Ser Arg Pro Glu Thr Pro
195 200 205
Lys Gln Lys Asn Glu Gly Arg Pro Glu Thr Pro Lys His Arg His Asp
210 215 220
Asn Arg Arg Asp Ser Gly Lys Pro Ser Thr Glu Lys Lys Pro Glu Val
225 230 235 240
Ser Lys His Lys Gln Asp Thr Lys Ser Asp Ser Pro Arg Leu Lys Ser
245 250 255
Glu Arg Ala Glu Ala Leu Lys Gln Arg Pro Asp Gly Arg Ser Val Ser
260 265 270
Glu Ser Leu Arg Arg Asp His Asp Asn Lys Gln Lys Ser Asp Asp Arg
275 280 285
Gly Glu Ser Glu Arg His Arg Gly Asp Gln Ser Arg Val Arg Arg Pro
290 295 300
Glu Thr Leu Arg Ser Ser Ser Arg Asn Glu His Gly Ile Lys Ser Asp
305 310 315 320
Ser Ser Lys Thr Asp Lys Leu Glu Arg Lys His Arg His Glu Ser Gly
325 330 335
Asp Ser Arg Glu Arg Pro Ser Ser Gly Glu Gln Lys Ser Arg Pro Asp
340 345 350
Ser Pro Arg Val Lys Gln Gly Asp Ser Asn Lys Ser Arg Ser Asp Lys
355 360 365
Leu Gly Phe Lys Ser Pro Thr Ser Lys Asp Asp Lys Arg Thr Glu Gly
370 375 380
Asn Lys Ser Lys Val Asp Thr Asn Lys Ala His Pro Asp Asn Lys Ala
385 390 395 400
Glu Phe Pro Ser Tyr Leu Leu Gly Gly Arg Ser Gly Ala Leu Lys Asn
405 410 415
Phe Val Ile Pro Lys Ile Lys Arg Asp Lys Asp Gly Asn Val Thr Gln
420 425 430
Glu Thr Lys Lys Met Glu Met Lys Gly Glu Pro Lys Asp Lys Val Glu
435 440 445
Lys Ile Gly Leu Val Glu Asp Leu Asn Lys Gly Ala Lys Pro Val Val
450 455 460
Val Leu Gln Lys Leu Ser Leu Asp Asp Val Gln Lys Leu Ile Lys Asp
465 470 475 480
Arg Glu Asp Lys Ser Arg Ser Ser Leu Lys Pro Ile Lys Asn Lys Pro
485 490 495
Ser Lys Ser Asn Lys Gly Ser Ile Asp Gln Ser Val Leu Lys Glu Leu
500 505 510
Pro Pro Glu Leu Leu Ala Glu Ile Glu Ser Thr Met Pro Leu Cys Glu
515 520 525
Arg Val Lys Met Asn Lys Arg Lys Arg Ser Thr Val Asn Glu Lys Pro
530 535 540
Lys Tyr Ala Glu Ile Ser Ser Asp Glu Asp Asn Asp Ser Asp Glu Ala
545 550 555 560
Phe Glu Ser Ser Arg Lys Arg His Lys Lys Asp Asp Asp Lys Ala Trp
565 570 575
Glu Tyr Glu Glu Arg Asp Arg Arg Ser Ser Gly Asp His Arg Arg Ser
580 585 590
Gly His Ser His Glu Gly Arg Arg Ser Ser Gly Gly Gly Arg Tyr Arg
595 600 605
Asn Arg Ser Pro Ser Asp Ser Asp Met Glu Asp Tyr Ser Pro Pro Pro
610 615 620
Ser Leu Ser Glu Val Ala Arg Lys Met Lys Lys Lys Glu Lys Gln Lys
625 630 635 640
Lys Arg Lys Ala Tyr Glu Pro Lys Leu Thr Pro Glu Glu Met Met Asp
645 650 655
Ser Ser Thr Phe Lys Arg Phe Thr Ala Ser Ile Glu Asn Ile Leu Asp
660 665 670
Asn Leu Glu Asp Met Asp Phe Thr Ala Phe Gly Asp Asp Asp Glu Ile
675 680 685
Pro Gln Glu Leu Leu Leu Gly Lys His Gln Leu Asn Glu Leu Gly Ser
690 695 700
Glu Ser Ala Lys Ile Lys Ala Met Gly Ile Met Asp Lys Leu Ser Thr
705 710 715 720
Asp Lys Thr Val Lys Val Leu Asn Ile Leu Glu Lys Asn Ile Gln Asp
725 730 735
Gly Ser Lys Leu Ser Thr Leu Leu Asn His Asn Asn Asp Thr Glu Glu
740 745 750
Glu Glu Arg Leu Trp Arg Asp Leu Ile Met Glu Arg Val Thr Lys Ser
755 760 765
Ala Asp Ala Cys Leu Thr Thr Ile Asn Ile Met Thr Ser Pro Asn Met
770 775 780
Pro Lys Ala Val Tyr Ile Glu Asp Val Ile Glu Arg Val Ile Gln Tyr
785 790 795 800
Thr Lys Phe His Leu Gln Asn Thr Leu Tyr Pro Gln Tyr Asp Pro Val
805 810 815
Tyr Arg Leu Asp Pro His Gly Gly Gly Leu Leu Ser Ser Lys Ala Lys
820 825 830
Arg Ala Lys Cys Ser Thr His Lys Gln Arg Val Ile Val Met Leu Tyr
835 840 845
Asn Lys Val Cys Asp Ile Val Ser Ser Leu Ser Glu Leu Leu Glu Ile
850 855 860
Gln Leu Leu Thr Asp Thr Thr Ile Leu Gln Val Ser Ser Met Gly Ile
865 870 875 880
Thr Pro Phe Phe Val Glu Asn Val Ser Glu Leu Gln Leu Cys Ala Ile
885 890 895
Lys Leu Val Thr Ala Val Phe Ser Arg Tyr Glu Lys His Arg Gln Leu
900 905 910
Ile Leu Glu Glu Ile Phe Thr Ser Leu Ala Arg Leu Pro Thr Ser Lys
915 920 925
Arg Ser Leu Arg Asn Phe Arg Leu Asn Ser Ser Asp Met Asp Gly Glu
930 935 940
Pro Met Tyr Ile Gln Met Val Thr Ala Leu Val Leu Gln Leu Ile Gln
945 950 955 960
Cys Val Val His Leu Pro Ser Ser Glu Lys Asp Ser Asn Ala Glu Glu
965 970 975
Asp Ser Asn Lys Lys Ile Asp Gln Asp Val Val Ile Thr Asn Ser Tyr
980 985 990
Glu Thr Ala Met Arg Thr Ala Gln Asn Phe Leu Ser Ile Phe Leu Lys
995 1000 1005
Lys Cys Gly Ser Lys Gln Gly Glu Glu Asp Tyr Arg Pro Leu Phe
1010 1015 1020
Glu Asn Phe Val Gln Asp Leu Leu Ser Thr Val Asn Lys Pro Glu
1025 1030 1035
Trp Pro Ala Ala Glu Leu Leu Leu Ser Leu Leu Gly Arg Leu Leu
1040 1045 1050
Val His Gln Phe Ser Asn Lys Ser Thr Glu Met Ala Leu Arg Val
1055 1060 1065
Ala Ser Leu Asp Tyr Leu Gly Thr Val Ala Ala Arg Leu Arg Lys
1070 1075 1080
Asp Ala Val Thr Ser Lys Met Asp Gln Gly Ser Ile Glu Arg Ile
1085 1090 1095
Leu Lys Gln Val Ser Gly Gly Glu Asp Glu Ile Gln Gln Leu Gln
1100 1105 1110
Lys Ala Leu Leu Asp Tyr Leu Asp Glu Asn Thr Glu Thr Asp Pro
1115 1120 1125
Ser Leu Val Phe Ser Arg Lys Phe Tyr Ile Ala Gln Trp Phe Arg
1130 1135 1140
Asp Thr Thr Leu Glu Thr Glu Lys Ala Met Lys Ser Gln Lys Asp
1145 1150 1155
Glu Glu Ser Ser Glu Gly Thr His His Ala Lys Glu Ile Glu Thr
1160 1165 1170
Thr Gly Gln Ile Met His Arg Ala Glu Asn Arg Lys Lys Phe Leu
1175 1180 1185
Arg Ser Ile Ile Lys Thr Thr Pro Ser Gln Phe Ser Thr Leu Lys
1190 1195 1200
Met Asn Ser Asp Thr Val Asp Tyr Asp Asp Ala Cys Leu Ile Val
1205 1210 1215
Arg Tyr Leu Ala Ser Met Arg Pro Phe Ala Gln Ser Phe Asp Ile
1220 1225 1230
Tyr Leu Thr Gln Ile Leu Arg Val Leu Gly Glu Asn Ala Ile Ala
1235 1240 1245
Val Arg Thr Lys Ala Met Lys Cys Leu Ser Glu Val Val Ala Val
1250 1255 1260
Asp Pro Ser Ile Leu Ala Arg Leu Asp Met Gln Arg Gly Val His
1265 1270 1275
Gly Arg Leu Met Asp Asn Ser Thr Ser Val Arg Glu Ala Ala Val
1280 1285 1290
Glu Leu Leu Gly Arg Phe Val Leu Cys Arg Pro Gln Leu Ala Glu
1295 1300 1305
Gln Tyr Tyr Asp Met Leu Ile Glu Arg Ile Leu Asp Thr Gly Ile
1310 1315 1320
Ser Val Arg Lys Arg Val Ile Lys Ile Leu Arg Asp Ile Cys Ile
1325 1330 1335
Glu Gln Pro Thr Phe Pro Lys Ile Thr Glu Met Cys Val Lys Met
1340 1345 1350
Ile Arg Arg Val Asn Asp Glu Glu Gly Ile Lys Lys Leu Val Asn
1355 1360 1365
Glu Thr Phe Gln Lys Leu Trp Phe Thr Pro Thr Pro His Asn Asp
1370 1375 1380
Lys Glu Ala Met Thr Arg Lys Ile Leu Asn Ile Thr Asp Val Val
1385 1390 1395
Ala Ala Cys Arg Asp Thr Gly Tyr Asp Trp Phe Glu Gln Leu Leu
1400 1405 1410
Gln Asn Leu Leu Lys Ser Glu Glu Asp Ser Ser Tyr Lys Pro Val
1415 1420 1425
Lys Lys Ala Cys Thr Gln Leu Val Asp Asn Leu Val Glu His Ile
1430 1435 1440
Leu Lys Tyr Glu Glu Ser Leu Ala Asp Ser Asp Asn Lys Gly Val
1445 1450 1455
Asn Ser Gly Arg Leu Val Ala Cys Ile Thr Thr Leu Phe Leu Phe
1460 1465 1470
Ser Lys Ile Arg Pro Gln Leu Met Val Lys His Ala Met Thr Met
1475 1480 1485
Gln Pro Tyr Leu Thr Thr Lys Cys Ser Thr Gln Asn Asp Phe Met
1490 1495 1500
Val Ile Cys Asn Val Ala Lys Ile Leu Glu Leu Val Val Pro Leu
1505 1510 1515
Met Glu His Pro Ser Glu Thr Phe Leu Ala Thr Ile Glu Glu Asp
1520 1525 1530
Leu Met Lys Leu Ile Ile Lys Tyr Gly Met Thr Val Val Gln His
1535 1540 1545
Cys Val Ser Cys Leu Gly Ala Val Val Asn Lys Val Thr Gln Asn
1550 1555 1560
Phe Lys Phe Val Trp Ala Cys Phe Asn Arg Tyr Tyr Gly Ala Ile
1565 1570 1575
Ser Lys Leu Lys Ser Gln His Gln Glu Asp Pro Asn Asn Thr Ser
1580 1585 1590
Leu Leu Thr Asn Lys Pro Ala Leu Leu Arg Ser Leu Phe Thr Val
1595 1600 1605
Gly Ala Leu Cys Arg His Phe Asp Phe Asp Leu Glu Asp Phe Lys
1610 1615 1620
Gly Asn Ser Lys Val Asn Ile Lys Asp Lys Val Leu Glu Leu Leu
1625 1630 1635
Met Tyr Phe Thr Lys His Ser Asp Glu Glu Val Gln Thr Lys Ala
1640 1645 1650
Ile Ile Gly Leu Gly Phe Ala Phe Ile Gln His Pro Ser Leu Met
1655 1660 1665
Phe Glu Gln Glu Val Lys Asn Leu Tyr Asn Asn Ile Leu Ser Asp
1670 1675 1680
Lys Asn Ser Ser Val Asn Leu Lys Ile Gln Val Leu Lys Asn Leu
1685 1690 1695
Gln Thr Tyr Leu Gln Glu Glu Asp Thr Arg Met Gln Gln Ala Asp
1700 1705 1710
Arg Asp Trp Lys Lys Val Ala Lys Gln Glu Asp Leu Lys Glu Met
1715 1720 1725
Gly Asp Val Ser Ser Gly Met Ser Ser Ser Ile Met Gln Leu Tyr
1730 1735 1740
Leu Lys Gln Val Leu Glu Ala Phe Phe His Thr Gln Ser Ser Val
1745 1750 1755
Arg His Phe Ala Leu Asn Val Ile Ala Leu Thr Leu Asn Gln Gly
1760 1765 1770
Leu Ile His Pro Val Gln Cys Val Pro Tyr Leu Ile Ala Met Gly
1775 1780 1785
Thr Asp Pro Glu Pro Ala Met Arg Asn Lys Ala Asp Gln Gln Leu
1790 1795 1800
Val Glu Ile Asp Lys Lys Tyr Ala Gly Phe Ile His Met Lys Ala
1805 1810 1815
Val Ala Gly Met Lys Met Ser Tyr Gln Val Gln Gln Ala Ile Asn
1820 1825 1830
Thr Cys Leu Lys Asp Pro Val Arg Gly Phe Arg Gln Asp Glu Ser
1835 1840 1845
Ser Ser Ala Leu Cys Ser His Leu Tyr Ser Met Ile Arg Gly Asn
1850 1855 1860
Arg Gln His Arg Arg Ala Phe Leu Ile Ser Leu Leu Asn Leu Phe
1865 1870 1875
Asp Asp Thr Ala Lys Thr Asp Val Thr Met Leu Leu Tyr Ile Ala
1880 1885 1890
Asp Asn Leu Ala Cys Phe Pro Tyr Gln Thr Gln Glu Glu Pro Leu
1895 1900 1905
Phe Ile Met His His Ile Asp Ile Thr Leu Ser Val Ser Gly Ser
1910 1915 1920
Asn Leu Leu Gln Ser Phe Lys Glu Ser Met Val Lys Asp Lys Arg
1925 1930 1935
Lys Glu Arg Lys Ser Ser Pro Ser Lys Glu Asn Glu Ser Ser Asp
1940 1945 1950
Ser Glu Glu Glu Val Ser Arg Pro Arg Lys Ser Arg Lys Arg Val
1955 1960 1965
Asp Ser Asp Ser Asp Ser Asp Ser Glu Asp Asp Ile Asn Ser Val
1970 1975 1980
Met Lys Cys Leu Pro Glu Asn Ser Ala Pro Leu Ile Glu Phe Ala
1985 1990 1995
Asn Val Ser Gln Gly Ile Leu Leu Leu Leu Met Leu Lys Gln His
2000 2005 2010
Leu Lys Asn Leu Cys Gly Phe Ser Asp Ser Lys Ile Gln Lys Tyr
2015 2020 2025
Ser Pro Ser Glu Ser Ala Lys Val Tyr Asp Lys Ala Ile Asn Arg
2030 2035 2040
Lys Thr Gly Val His Phe His Pro Lys Gln Thr Leu Asp Phe Leu
2045 2050 2055
Arg Ser Asp Met Ala Asn Ser Lys Ile Thr Glu Glu Val Lys Arg
2060 2065 2070
Ser Ile Val Lys Gln Tyr Leu Asp Phe Lys Leu Leu Met Glu His
2075 2080 2085
Leu Asp Pro Asp Glu Glu Glu Glu Glu Gly Glu Val Ser Ala Ser
2090 2095 2100
Thr Asn Ala Arg Asn Lys Ala Ile Thr Ser Leu Leu Gly Gly Gly
2105 2110 2115
Ser Pro Lys Asn Asn Thr Ala Ala Glu Thr Glu Asp Asp Glu Ser
2120 2125 2130
Asp Gly Glu Asp Arg Gly Gly Gly Thr Ser Gly Val Arg Arg Arg
2135 2140 2145
Arg Ser Gln Arg Ile Ser Gln Arg Ile Thr
2150 2155


35
2265
PRT
Homo sapiens

35
Met Val Ser Ile Asp Leu His Gln Ala Gly Arg Val Asp Ser Gln Ala
1 5 10 15
Ser Ile Thr Gln Asp Ser Asp Ser Ile Lys Lys Pro Glu Glu Ile Lys
20 25 30
Gln Cys Asn Asp Ala Pro Val Ser Val Leu Gln Glu Asp Ile Val Gly
35 40 45
Ser Leu Lys Ser Thr Pro Glu Asn His Pro Glu Thr Pro Lys Lys Lys
50 55 60
Ser Asp Pro Glu Leu Ser Lys Ser Glu Met Lys Gln Ser Glu Ser Arg
65 70 75 80
Leu Ala Glu Ser Lys Pro Asn Glu Asn Arg Leu Val Glu Thr Lys Ser
85 90 95
Ser Glu Asn Lys Leu Glu Thr Lys Val Glu Thr Gln Thr Glu Glu Leu
100 105 110
Lys Gln Asn Glu Ser Arg Thr Thr Glu Cys Lys Gln Asn Glu Ser Thr
115 120 125
Ile Val Glu Pro Lys Gln Asn Glu Asn Arg Leu Ser Asp Thr Lys Pro
130 135 140
Asn Asp Asn Lys Gln Asn Asn Gly Arg Ser Glu Thr Thr Lys Ser Arg
145 150 155 160
Pro Glu Thr Pro Lys Gln Lys Gly Glu Ser Arg Pro Glu Thr Pro Lys
165 170 175
Gln Lys Ser Asp Gly His Pro Glu Thr Pro Lys Gln Lys Gly Asp Gly
180 185 190
Arg Pro Glu Thr Pro Lys Gln Lys Gly Glu Ser Arg Pro Glu Thr Pro
195 200 205
Lys Gln Lys Asn Glu Gly Arg Pro Glu Thr Pro Lys His Arg His Asp
210 215 220
Asn Arg Arg Asp Ser Gly Lys Pro Ser Thr Glu Lys Lys Pro Glu Val
225 230 235 240
Ser Lys His Lys Gln Asp Thr Lys Ser Asp Ser Pro Arg Leu Lys Ser
245 250 255
Glu Arg Ala Glu Ala Leu Lys Gln Arg Pro Asp Gly Arg Ser Val Ser
260 265 270
Glu Ser Leu Arg Arg Asp His Asp Asn Lys Gln Lys Ser Asp Asp Arg
275 280 285
Gly Glu Ser Glu Arg His Arg Gly Asp Gln Ser Arg Val Arg Arg Pro
290 295 300
Glu Thr Leu Arg Ser Ser Ser Arg Asn Glu His Gly Ile Lys Ser Asp
305 310 315 320
Ser Ser Lys Thr Asp Lys Leu Glu Arg Lys His Arg His Glu Ser Gly
325 330 335
Asp Ser Arg Glu Arg Pro Ser Ser Gly Glu Gln Lys Ser Arg Pro Asp
340 345 350
Ser Pro Arg Val Lys Gln Gly Asp Ser Asn Lys Ser Arg Ser Asp Lys
355 360 365
Leu Gly Phe Lys Ser Pro Thr Ser Lys Asp Asp Lys Arg Thr Glu Gly
370 375 380
Asn Lys Ser Lys Val Asp Thr Asn Lys Ala His Pro Asp Asn Lys Ala
385 390 395 400
Glu Phe Pro Ser Tyr Leu Leu Gly Gly Arg Ser Gly Ala Leu Lys Asn
405 410 415
Phe Val Ile Pro Lys Ile Lys Arg Asp Lys Asp Gly Asn Val Thr Gln
420 425 430
Glu Thr Lys Lys Met Glu Met Lys Gly Glu Pro Lys Asp Lys Val Glu
435 440 445
Lys Ile Gly Leu Val Glu Asp Leu Asn Lys Gly Ala Lys Pro Val Val
450 455 460
Val Leu Gln Lys Leu Ser Leu Asp Asp Val Gln Lys Leu Ile Lys Asp
465 470 475 480
Arg Glu Asp Lys Ser Arg Ser Ser Leu Lys Pro Ile Lys Asn Lys Pro
485 490 495
Ser Lys Ser Asn Lys Gly Ser Ile Asp Gln Ser Val Leu Lys Glu Leu
500 505 510
Pro Pro Glu Leu Leu Ala Glu Ile Glu Ser Thr Met Pro Leu Cys Glu
515 520 525
Arg Val Lys Met Asn Lys Arg Lys Arg Ser Thr Val Asn Glu Lys Pro
530 535 540
Lys Tyr Ala Glu Ile Ser Ser Asp Glu Asp Asn Asp Ser Asp Glu Ala
545 550 555 560
Phe Glu Ser Ser Arg Lys Arg His Lys Lys Asp Asp Asp Lys Ala Trp
565 570 575
Glu Tyr Glu Glu Arg Asp Arg Arg Ser Ser Gly Asp His Arg Arg Ser
580 585 590
Gly His Ser His Glu Gly Arg Arg Ser Ser Gly Gly Gly Arg Tyr Arg
595 600 605
Asn Arg Ser Pro Ser Asp Ser Asp Met Glu Asp Tyr Ser Pro Pro Pro
610 615 620
Ser Leu Ser Glu Val Ala Arg Lys Met Lys Lys Lys Glu Lys Gln Lys
625 630 635 640
Lys Arg Lys Ala Tyr Glu Pro Lys Leu Thr Pro Glu Glu Met Met Asp
645 650 655
Ser Ser Thr Phe Lys Arg Phe Thr Ala Ser Ile Glu Asn Ile Leu Asp
660 665 670
Asn Leu Glu Asp Met Asp Phe Thr Ala Phe Gly Asp Asp Asp Glu Ile
675 680 685
Pro Gln Glu Leu Leu Leu Gly Lys His Gln Leu Asn Glu Leu Gly Ser
690 695 700
Glu Ser Ala Lys Ile Lys Ala Met Gly Ile Met Asp Lys Leu Ser Thr
705 710 715 720
Asp Lys Thr Val Lys Val Leu Asn Ile Leu Glu Lys Asn Ile Gln Asp
725 730 735
Gly Ser Lys Leu Ser Thr Leu Leu Asn His Asn Asn Asp Thr Glu Glu
740 745 750
Glu Glu Arg Leu Trp Arg Asp Leu Ile Met Glu Arg Val Thr Lys Ser
755 760 765
Ala Asp Ala Cys Leu Thr Thr Ile Asn Ile Met Thr Ser Pro Asn Met
770 775 780
Pro Lys Ala Val Tyr Ile Glu Asp Val Ile Glu Arg Val Ile Gln Tyr
785 790 795 800
Thr Lys Phe His Leu Gln Asn Thr Leu Tyr Pro Gln Tyr Asp Pro Val
805 810 815
Tyr Arg Leu Asp Pro His Gly Gly Gly Leu Leu Ser Ser Lys Ala Lys
820 825 830
Arg Ala Lys Cys Ser Thr His Lys Gln Arg Val Ile Val Met Leu Tyr
835 840 845
Asn Lys Val Cys Asp Ile Val Ser Ser Leu Ser Glu Leu Leu Glu Ile
850 855 860
Gln Leu Leu Thr Asp Thr Thr Ile Leu Gln Val Ser Ser Met Gly Ile
865 870 875 880
Thr Pro Phe Phe Val Glu Asn Val Ser Glu Leu Gln Leu Cys Ala Ile
885 890 895
Lys Leu Val Thr Ala Val Phe Ser Arg Tyr Glu Lys His Arg Gln Leu
900 905 910
Ile Leu Glu Glu Ile Phe Thr Ser Leu Ala Arg Leu Pro Thr Ser Lys
915 920 925
Arg Ser Leu Arg Asn Phe Arg Leu Asn Ser Ser Asp Met Asp Gly Glu
930 935 940
Pro Met Tyr Ile Gln Met Val Thr Ala Leu Val Leu Gln Leu Ile Gln
945 950 955 960
Cys Val Val His Leu Pro Ser Ser Glu Lys Asp Ser Asn Ala Glu Glu
965 970 975
Asp Ser Asn Lys Lys Ile Asp Gln Asp Val Val Ile Thr Asn Ser Tyr
980 985 990
Glu Thr Ala Met Arg Thr Ala Gln Asn Phe Leu Ser Ile Phe Leu Lys
995 1000 1005
Lys Cys Gly Ser Lys Gln Gly Glu Glu Asp Tyr Arg Pro Leu Phe
1010 1015 1020
Glu Asn Phe Val Gln Asp Leu Leu Ser Thr Val Asn Lys Pro Glu
1025 1030 1035
Trp Pro Ala Ala Glu Leu Leu Leu Ser Leu Leu Gly Arg Leu Leu
1040 1045 1050
Val His Gln Phe Ser Asn Lys Ser Thr Glu Met Ala Leu Arg Val
1055 1060 1065
Ala Ser Leu Asp Tyr Leu Gly Thr Val Ala Ala Arg Leu Arg Lys
1070 1075 1080
Asp Ala Val Thr Ser Lys Met Asp Gln Gly Ser Ile Glu Arg Ile
1085 1090 1095
Leu Lys Gln Val Ser Gly Gly Glu Asp Glu Ile Gln Gln Leu Gln
1100 1105 1110
Lys Ala Leu Leu Asp Tyr Leu Asp Glu Asn Thr Glu Thr Asp Pro
1115 1120 1125
Ser Leu Val Phe Ser Arg Lys Phe Tyr Ile Ala Gln Trp Phe Arg
1130 1135 1140
Asp Thr Thr Leu Glu Thr Glu Lys Ala Met Lys Ser Gln Lys Asp
1145 1150 1155
Glu Glu Ser Ser Glu Gly Thr His His Ala Lys Glu Ile Glu Thr
1160 1165 1170
Thr Gly Gln Ile Met His Arg Ala Glu Asn Arg Lys Lys Phe Leu
1175 1180 1185
Arg Ser Ile Ile Lys Thr Thr Pro Ser Gln Phe Ser Thr Leu Lys
1190 1195 1200
Met Asn Ser Asp Thr Val Asp Tyr Asp Asp Ala Cys Leu Ile Val
1205 1210 1215
Arg Tyr Leu Ala Ser Met Arg Pro Phe Ala Gln Ser Phe Asp Ile
1220 1225 1230
Tyr Leu Thr Gln Ile Leu Arg Val Leu Gly Glu Asn Ala Ile Ala
1235 1240 1245
Val Arg Thr Lys Ala Met Lys Cys Leu Ser Glu Val Val Ala Val
1250 1255 1260
Asp Pro Ser Ile Leu Ala Arg Leu Asp Met Gln Arg Gly Val His
1265 1270 1275
Gly Arg Leu Met Asp Asn Ser Thr Ser Val Arg Glu Ala Ala Val
1280 1285 1290
Glu Leu Leu Gly Arg Phe Val Leu Cys Arg Pro Gln Leu Ala Glu
1295 1300 1305
Gln Tyr Tyr Asp Met Leu Ile Glu Arg Ile Leu Asp Thr Gly Ile
1310 1315 1320
Ser Val Arg Lys Arg Val Ile Lys Ile Leu Arg Asp Ile Cys Ile
1325 1330 1335
Glu Gln Pro Thr Phe Pro Lys Ile Thr Glu Met Cys Val Lys Met
1340 1345 1350
Ile Arg Arg Val Asn Asp Glu Glu Gly Ile Lys Lys Leu Val Asn
1355 1360 1365
Glu Thr Phe Gln Lys Leu Trp Phe Thr Pro Thr Pro His Asn Asp
1370 1375 1380
Lys Glu Ala Met Thr Arg Lys Ile Leu Asn Ile Thr Asp Val Val
1385 1390 1395
Ala Ala Cys Arg Asp Thr Gly Tyr Asp Trp Phe Glu Gln Leu Leu
1400 1405 1410
Gln Asn Leu Leu Lys Ser Glu Glu Asp Ser Ser Tyr Lys Pro Val
1415 1420 1425
Lys Lys Ala Cys Thr Gln Leu Val Asp Asn Leu Val Glu His Ile
1430 1435 1440
Leu Lys Tyr Glu Glu Ser Leu Ala Asp Ser Asp Asn Lys Gly Val
1445 1450 1455
Asn Ser Gly Arg Leu Val Ala Cys Ile Thr Thr Leu Phe Leu Phe
1460 1465 1470
Ser Lys Ile Arg Pro Gln Leu Met Val Lys His Ala Met Thr Met
1475 1480 1485
Gln Pro Tyr Leu Thr Thr Lys Cys Ser Thr Gln Asn Asp Phe Met
1490 1495 1500
Val Ile Cys Asn Val Ala Lys Ile Leu Glu Leu Val Val Pro Leu
1505 1510 1515
Met Glu His Pro Ser Glu Thr Phe Leu Ala Thr Ile Glu Glu Asp
1520 1525 1530
Leu Met Lys Leu Ile Ile Lys Tyr Gly Met Thr Val Val Gln His
1535 1540 1545
Cys Val Ser Cys Leu Gly Ala Val Val Asn Lys Val Thr Gln Asn
1550 1555 1560
Phe Lys Phe Val Trp Ala Cys Phe Asn Arg Tyr Tyr Gly Ala Ile
1565 1570 1575
Ser Lys Leu Lys Ser Gln His Gln Glu Asp Pro Asn Asn Thr Ser
1580 1585 1590
Leu Leu Thr Asn Lys Pro Ala Leu Leu Arg Ser Leu Phe Thr Val
1595 1600 1605
Gly Ala Leu Cys Arg His Phe Asp Phe Asp Leu Glu Asp Phe Lys
1610 1615 1620
Gly Asn Ser Lys Val Asn Ile Lys Asp Lys Val Leu Glu Leu Leu
1625 1630 1635
Met Tyr Phe Thr Lys His Ser Asp Glu Glu Val Gln Thr Lys Ala
1640 1645 1650
Ile Ile Gly Leu Gly Phe Ala Phe Ile Gln His Pro Ser Leu Met
1655 1660 1665
Phe Glu Gln Glu Val Lys Asn Leu Tyr Asn Asn Ile Leu Ser Asp
1670 1675 1680
Lys Asn Ser Ser Val Asn Leu Lys Ile Gln Val Leu Lys Asn Leu
1685 1690 1695
Gln Thr Tyr Leu Gln Glu Glu Asp Thr Arg Met Gln Gln Ala Asp
1700 1705 1710
Arg Asp Trp Lys Lys Val Ala Lys Gln Glu Asp Leu Lys Glu Met
1715 1720 1725
Gly Asp Val Ser Ser Gly Met Ser Ser Ser Ile Met Gln Leu Tyr
1730 1735 1740
Leu Lys Gln Val Leu Glu Ala Phe Phe His Thr Gln Ser Ser Val
1745 1750 1755
Arg His Phe Ala Leu Asn Val Ile Ala Leu Thr Leu Asn Gln Gly
1760 1765 1770
Leu Ile His Pro Val Gln Cys Val Pro Tyr Leu Ile Ala Met Gly
1775 1780 1785
Thr Asp Pro Glu Pro Ala Met Arg Asn Lys Ala Asp Gln Gln Leu
1790 1795 1800
Val Glu Ile Asp Lys Lys Tyr Ala Gly Phe Ile His Met Lys Ala
1805 1810 1815
Val Ala Gly Met Lys Met Ser Tyr Gln Val Gln Gln Ala Ile Asn
1820 1825 1830
Thr Cys Leu Lys Asp Pro Val Arg Gly Phe Arg Gln Asp Glu Ser
1835 1840 1845
Ser Ser Ala Leu Cys Ser His Leu Tyr Ser Met Ile Arg Gly Asn
1850 1855 1860
Arg Gln His Arg Arg Ala Phe Leu Ile Ser Leu Leu Asn Leu Phe
1865 1870 1875
Asp Asp Thr Ala Lys Thr Asp Val Thr Met Leu Leu Tyr Ile Ala
1880 1885 1890
Asp Asn Leu Ala Cys Phe Pro Tyr Gln Thr Gln Glu Glu Pro Leu
1895 1900 1905
Phe Ile Met His His Ile Asp Ile Thr Leu Ser Val Ser Gly Ser
1910 1915 1920
Asn Leu Leu Gln Ser Phe Lys Glu Ser Met Val Lys Asp Lys Arg
1925 1930 1935
Lys Glu Arg Lys Ser Ser Pro Ser Lys Glu Asn Glu Ser Ser Asp
1940 1945 1950
Ser Glu Glu Glu Val Ser Arg Pro Arg Lys Ser Arg Lys Arg Val
1955 1960 1965
Asp Ser Asp Ser Asp Ser Asp Ser Glu Asp Asp Ile Asn Ser Val
1970 1975 1980
Met Lys Cys Leu Pro Glu Asn Ser Ala Pro Leu Ile Glu Phe Ala
1985 1990 1995
Asn Val Ser Gln Gly Ile Leu Leu Leu Leu Met Leu Lys Gln His
2000 2005 2010
Leu Lys Asn Leu Cys Gly Phe Ser Asp Ser Lys Ile Gln Lys Tyr
2015 2020 2025
Ser Pro Ser Glu Ser Ala Lys Val Tyr Asp Lys Ala Ile Asn Arg
2030 2035 2040
Lys Thr Gly Val His Phe His Pro Lys Gln Thr Leu Asp Phe Leu
2045 2050 2055
Arg Ser Asp Met Ala Asn Ser Lys Ile Thr Glu Glu Val Lys Arg
2060 2065 2070
Ser Ile Val Lys Gln Tyr Leu Asp Phe Lys Leu Leu Met Glu His
2075 2080 2085
Leu Asp Pro Asp Glu Glu Glu Glu Glu Gly Glu Val Ser Ala Ser
2090 2095 2100
Thr Asn Ala Arg Asn Lys Ala Ile Thr Ser Leu Leu Gly Gly Gly
2105 2110 2115
Ser Pro Lys Asn Asn Thr Ala Ala Glu Thr Glu Asp Asp Glu Ser
2120 2125 2130
Asp Gly Glu Asp Arg Gly Gly Gly Thr Ser Gly Ser Leu Arg Arg
2135 2140 2145
Ser Lys Arg Asn Ser Asp Ser Thr Glu Leu Ala Ala Gln Met Asn
2150 2155 2160
Glu Ser Val Asp Val Met Asp Val Ile Ala Ile Cys Cys Pro Lys
2165 2170 2175
Tyr Lys Asp Arg Pro Gln Ile Ala Arg Val Val Gln Lys Thr Ser
2180 2185 2190
Ser Gly Phe Ser Val Gln Trp Met Ala Gly Ser Tyr Ser Gly Ser
2195 2200 2205
Trp Thr Glu Ala Lys Arg Arg Asp Gly Arg Lys Leu Val Pro Trp
2210 2215 2220
Val Asp Thr Ile Lys Glu Ser Asp Ile Ile Tyr Lys Lys Ile Ala
2225 2230 2235
Leu Thr Ser Ala Asn Lys Leu Thr Asn Lys Val Val Gln Thr Leu
2240 2245 2250
Arg Ser Leu Tyr Ala Ala Lys Asp Gly Thr Ser Ser
2255 2260 2265


36
1007
PRT
Homo sapiens

36
Met Ser Arg Arg Lys Gln Arg Lys Pro Gln Gln Leu Ile Ser Asp Cys
1 5 10 15
Glu Gly Pro Ser Ala Ser Glu Asn Gly Asp Ala Ser Glu Glu Asp His
20 25 30
Pro Gln Val Cys Ala Lys Cys Cys Ala Gln Phe Thr Asp Pro Thr Glu
35 40 45
Phe Leu Ala His Gln Asn Ala Cys Ser Thr Asp Pro Pro Val Met Val
50 55 60
Ile Ile Gly Gly Gln Glu Asn Pro Asn Asn Ser Ser Ala Ser Ser Glu
65 70 75 80
Pro Arg Pro Glu Gly His Asn Asn Pro Gln Val Met Asp Thr Glu His
85 90 95
Ser Asn Pro Pro Asp Ser Gly Ser Ser Val Pro Thr Asp Pro Thr Trp
100 105 110
Gly Pro Glu Arg Arg Gly Glu Glu Ser Pro Gly His Phe Leu Val Ala
115 120 125
Ala Thr Gly Thr Ala Ala Gly Gly Gly Gly Gly Leu Ile Leu Ala Ser
130 135 140
Pro Lys Leu Gly Ala Thr Pro Leu Pro Pro Glu Ser Thr Pro Ala Pro
145 150 155 160
Pro Pro Pro Pro Pro Pro Pro Pro Pro Pro Gly Val Gly Ser Gly His
165 170 175
Leu Asn Ile Pro Leu Ile Leu Glu Glu Leu Arg Val Leu Gln Gln Arg
180 185 190
Gln Ile His Gln Met Gln Met Thr Glu Gln Ile Cys Arg Gln Val Leu
195 200 205
Leu Leu Gly Ser Leu Gly Gln Thr Val Gly Ala Pro Ala Ser Pro Ser
210 215 220
Glu Leu Pro Gly Thr Gly Thr Ala Ser Ser Thr Lys Pro Leu Leu Pro
225 230 235 240
Leu Phe Ser Pro Ile Lys Pro Val Gln Thr Ser Lys Thr Leu Ala Ser
245 250 255
Ser Ser Ser Ser Ser Ser Ser Ser Ser Gly Ala Glu Thr Pro Lys Gln
260 265 270
Ala Phe Phe His Leu Tyr His Pro Leu Gly Ser Gln His Pro Phe Ser
275 280 285
Ala Gly Gly Val Gly Arg Ser His Lys Pro Thr Pro Ala Pro Ser Pro
290 295 300
Ala Leu Pro Gly Ser Thr Asp Gln Leu Ile Ala Ser Pro His Leu Ala
305 310 315 320
Phe Pro Ser Thr Thr Gly Leu Leu Ala Ala Gln Cys Leu Gly Ala Ala
325 330 335
Arg Gly Leu Glu Ala Thr Ala Ser Pro Gly Leu Leu Lys Pro Lys Asn
340 345 350
Gly Ser Gly Glu Leu Ser Tyr Gly Glu Val Met Gly Pro Leu Glu Lys
355 360 365
Pro Gly Gly Arg His Lys Cys Arg Phe Cys Ala Lys Val Phe Gly Ser
370 375 380
Asp Ser Ala Leu Gln Ile His Leu Arg Ser His Thr Gly Glu Arg Pro
385 390 395 400
Tyr Lys Cys Asn Val Cys Gly Asn Arg Phe Thr Thr Arg Gly Asn Leu
405 410 415
Lys Val His Phe His Arg His Arg Glu Lys Tyr Pro His Val Gln Met
420 425 430
Asn Pro His Pro Val Pro Glu His Leu Asp Tyr Val Ile Thr Ser Ser
435 440 445
Gly Leu Pro Tyr Gly Met Ser Val Pro Pro Glu Lys Ala Glu Glu Glu
450 455 460
Ala Ala Thr Pro Gly Gly Gly Val Glu Arg Lys Pro Leu Val Ala Ser
465 470 475 480
Thr Thr Ala Leu Ser Ala Thr Glu Ser Leu Thr Leu Leu Ser Thr Ser
485 490 495
Ala Gly Thr Ala Thr Ala Pro Gly Leu Pro Ala Phe Asn Lys Phe Val
500 505 510
Leu Met Lys Ala Val Glu Pro Lys Asn Lys Ala Asp Glu Asn Thr Pro
515 520 525
Pro Gly Ser Glu Gly Ser Ala Ile Ser Gly Val Ala Glu Ser Ser Thr
530 535 540
Ala Thr Arg Met Gln Leu Ser Lys Leu Val Thr Ser Leu Pro Ser Trp
545 550 555 560
Ala Leu Leu Thr Asn His Phe Lys Ser Thr Gly Ser Phe Pro Phe Pro
565 570 575
Tyr Val Leu Glu Pro Leu Gly Ala Ser Pro Ser Glu Thr Ser Lys Leu
580 585 590
Gln Gln Leu Val Glu Lys Ile Asp Arg Gln Gly Ala Val Ala Val Thr
595 600 605
Ser Ala Ala Ser Gly Ala Pro Thr Thr Ser Ala Pro Ala Pro Ser Ser
610 615 620
Ser Ala Ser Ser Gly Pro Asn Gln Cys Val Ile Cys Leu Arg Val Leu
625 630 635 640
Ser Cys Pro Arg Ala Leu Arg Leu His Tyr Gly Gln His Gly Gly Glu
645 650 655
Arg Pro Phe Lys Cys Lys Val Cys Gly Arg Ala Phe Ser Thr Arg Gly
660 665 670
Asn Leu Arg Ala His Phe Val Gly His Lys Ala Ser Pro Ala Ala Arg
675 680 685
Ala Gln Asn Ser Cys Pro Ile Cys Gln Lys Lys Phe Thr Asn Ala Val
690 695 700
Thr Leu Gln Gln His Val Arg Met His Leu Gly Gly Gln Ile Pro Asn
705 710 715 720
Gly Gly Thr Ala Leu Pro Glu Gly Gly Gly Ala Ala Gln Glu Asn Gly
725 730 735
Ser Glu Gln Ser Thr Val Ser Gly Ala Gly Ser Phe Pro Gln Gln Gln
740 745 750
Ser Gln Gln Pro Ser Pro Glu Glu Glu Leu Ser Glu Glu Glu Glu Glu
755 760 765
Glu Asp Glu Glu Glu Glu Glu Asp Val Thr Asp Glu Asp Ser Leu Ala
770 775 780
Gly Arg Gly Ser Glu Ser Gly Gly Glu Lys Ala Ile Ser Val Arg Gly
785 790 795 800
Asp Ser Glu Glu Ala Ser Gly Ala Glu Glu Glu Val Gly Thr Val Ala
805 810 815
Ala Ala Ala Thr Ala Gly Lys Glu Met Asp Ser Asn Glu Lys Thr Thr
820 825 830
Gln Gln Ser Ser Leu Pro Pro Pro Pro Pro Pro Asp Ser Leu Asp Gln
835 840 845
Pro Gln Pro Met Glu Gln Gly Ser Ser Gly Val Leu Gly Gly Lys Glu
850 855 860
Glu Gly Gly Lys Pro Glu Arg Ser Ser Ser Pro Ala Ser Ala Leu Thr
865 870 875 880
Pro Glu Gly Glu Ala Thr Ser Val Thr Leu Val Glu Glu Leu Ser Leu
885 890 895
Gln Glu Ala Met Arg Lys Glu Pro Gly Glu Ser Ser Ser Arg Lys Ala
900 905 910
Cys Glu Val Cys Gly Gln Ala Phe Pro Ser Gln Ala Ala Leu Glu Glu
915 920 925
His Gln Lys Thr His Pro Lys Glu Gly Pro Leu Phe Thr Cys Val Phe
930 935 940
Cys Arg Gln Gly Phe Leu Glu Arg Ala Thr Leu Lys Lys His Met Leu
945 950 955 960
Leu Ala His His Gln Val Gln Pro Phe Ala Pro His Gly Pro Gln Asn
965 970 975
Ile Ala Ala Leu Ser Leu Val Pro Gly Cys Ser Pro Ser Ile Thr Ser
980 985 990
Thr Gly Leu Ser Pro Phe Pro Arg Lys Asp Asp Pro Thr Ile Pro
995 1000 1005


37
121
PRT
Homo sapiens

37
Met Asn Ala Pro Arg Ile Cys Ser Glu Tyr Asp Glu Glu Glu Val Asp
1 5 10 15
Tyr Glu Glu Ser Asp Ser Asp Glu Ser Trp Thr Thr Glu Ser Ala Ile
20 25 30
Ser Ser Glu Ala Ile Leu Ser Ser Met Cys Met Asn Gly Gly Glu Glu
35 40 45
Lys Pro Phe Ala Cys Pro Val Pro Gly Cys Lys Lys Arg Tyr Lys Asn
50 55 60
Val Asn Gly Ile Lys Tyr His Ala Lys Asn Gly His Arg Thr Gln Ile
65 70 75 80
Arg Val Arg Lys Pro Phe Lys Cys Arg Cys Gly Lys Ser Tyr Lys Thr
85 90 95
Ala Gln Gly Leu Arg His His Thr Ile Asn Phe His Pro Pro Val Ser
100 105 110
Ala Glu Ile Ile Arg Lys Met Gln Gln
115 120


38
736
PRT
Homo sapiens

38
Met Glu Ala Leu Ile Pro Val Ile Asn Lys Leu Gln Asp Val Phe Asn
1 5 10 15
Thr Val Gly Ala Asp Ile Ile Gln Leu Pro Gln Ile Val Val Val Gly
20 25 30
Thr Gln Ser Ser Gly Lys Ser Ser Val Leu Glu Ser Leu Val Gly Arg
35 40 45
Asp Leu Leu Pro Arg Gly Thr Gly Ile Val Thr Arg Arg Pro Leu Ile
50 55 60
Leu Gln Leu Val His Val Thr Gln Glu Asp Lys Arg Lys Thr Thr Gly
65 70 75 80
Glu Glu Asn Gly Val Glu Ala Glu Glu Trp Gly Lys Phe Leu His Thr
85 90 95
Lys Asn Lys Leu Tyr Thr Asp Phe Asp Glu Ile Arg Gln Glu Ile Glu
100 105 110
Asn Glu Thr Glu Arg Ile Ser Gly Asn Asn Lys Gly Val Ser Pro Glu
115 120 125
Pro Ile His Leu Lys Ile Phe Ser Pro Asn Val Val Asn Leu Thr Leu
130 135 140
Val Asp Leu Pro Gly Met Thr Lys Val Pro Val Gly Asp Gln Pro Lys
145 150 155 160
Asp Ile Glu Leu Gln Ile Arg Glu Leu Ile Leu Arg Phe Ile Ser Asn
165 170 175
Pro Asn Ser Ile Ile Leu Ala Val Thr Ala Ala Asn Thr Asp Met Ala
180 185 190
Thr Ser Glu Ala Leu Lys Ile Ser Arg Glu Val Asp Pro Asp Gly Arg
195 200 205
Arg Thr Leu Ala Val Ile Thr Lys Leu Asp Leu Met Asp Ala Gly Thr
210 215 220
Asp Ala Met Asp Val Leu Met Gly Arg Val Ile Pro Val Lys Leu Gly
225 230 235 240
Ile Ile Gly Val Val Asn Arg Ser Gln Leu Asp Ile Asn Asn Lys Lys
245 250 255
Ser Val Thr Asp Ser Ile Arg Asp Glu Tyr Ala Phe Leu Gln Lys Lys
260 265 270
Tyr Pro Ser Leu Ala Asn Arg Asn Gly Thr Lys Tyr Leu Ala Arg Thr
275 280 285
Leu Asn Arg Leu Leu Met His His Ile Arg Asp Cys Leu Pro Glu Leu
290 295 300
Lys Thr Arg Ile Asn Val Leu Ala Ala Gln Tyr Gln Ser Leu Leu Asn
305 310 315 320
Ser Tyr Gly Glu Pro Val Asp Asp Lys Ser Ala Thr Leu Leu Gln Leu
325 330 335
Ile Thr Lys Phe Ala Thr Glu Tyr Cys Asn Thr Ile Glu Gly Thr Ala
340 345 350
Lys Tyr Ile Glu Thr Ser Glu Leu Cys Gly Gly Ala Arg Ile Cys Tyr
355 360 365
Ile Phe His Glu Thr Phe Gly Arg Thr Leu Glu Ser Val Asp Pro Leu
370 375 380
Gly Gly Leu Asn Thr Ile Asp Ile Leu Thr Ala Ile Arg Asn Ala Thr
385 390 395 400
Gly Pro Arg Pro Ala Leu Phe Val Pro Glu Val Ser Phe Glu Leu Leu
405 410 415
Val Lys Arg Gln Ile Lys Arg Leu Glu Glu Pro Ser Leu Arg Cys Val
420 425 430
Glu Leu Val His Glu Glu Met Gln Arg Ile Ile Gln His Cys Ser Asn
435 440 445
Tyr Ser Thr Gln Glu Leu Leu Arg Phe Pro Lys Leu His Asp Ala Ile
450 455 460
Val Glu Val Val Thr Cys Leu Leu Arg Lys Arg Leu Pro Val Thr Asn
465 470 475 480
Glu Met Val His Asn Leu Val Ala Ile Glu Leu Ala Tyr Ile Asn Thr
485 490 495
Lys His Pro Asp Phe Ala Asp Ala Cys Gly Leu Met Asn Asn Asn Ile
500 505 510
Glu Glu Gln Arg Arg Asn Arg Leu Ala Arg Glu Leu Pro Ser Ala Val
515 520 525
Ser Arg Asp Lys Ser Ser Lys Val Pro Ser Ala Leu Ala Pro Ala Ser
530 535 540
Gln Glu Pro Ser Pro Ala Ala Ser Ala Glu Ala Asp Gly Lys Leu Ile
545 550 555 560
Gln Asp Ser Arg Arg Glu Thr Lys Asn Val Ala Ser Gly Gly Gly Gly
565 570 575
Val Gly Asp Gly Val Gln Glu Pro Thr Thr Gly Asn Trp Arg Gly Met
580 585 590
Leu Lys Thr Ser Lys Ala Glu Glu Leu Leu Ala Glu Glu Lys Ser Lys
595 600 605
Pro Ile Pro Ile Met Pro Ala Ser Pro Gln Lys Gly His Ala Val Asn
610 615 620
Leu Leu Asp Val Pro Val Pro Val Ala Arg Lys Leu Ser Ala Arg Glu
625 630 635 640
Gln Arg Asp Cys Glu Val Ile Glu Arg Leu Ile Lys Ser Tyr Phe Leu
645 650 655
Ile Val Arg Lys Asn Ile Gln Asp Ser Val Pro Lys Ala Val Met His
660 665 670
Phe Leu Val Asn His Val Lys Asp Thr Leu Gln Ser Glu Leu Val Gly
675 680 685
Gln Leu Tyr Lys Ser Ser Leu Leu Asp Asp Leu Leu Thr Glu Ser Glu
690 695 700
Asp Met Ala Gln Arg Arg Lys Glu Ala Ala Asp Met Leu Lys Ala Leu
705 710 715 720
Gln Gly Ala Ser Gln Ile Ile Ala Glu Ile Arg Glu Thr His Leu Trp
725 730 735


39
710
PRT
Homo sapiens

39
Met Glu Ala Leu Ile Pro Val Ile Asn Lys Leu Gln Asp Val Phe Asn
1 5 10 15
Thr Val Gly Ala Asp Ile Ile Gln Leu Pro Gln Ile Val Val Val Gly
20 25 30
Thr Gln Ser Ser Gly Lys Ser Ser Val Leu Glu Ser Leu Val Gly Arg
35 40 45
Asp Leu Leu Pro Arg Gly Thr Gly Ile Val Thr Arg Arg Pro Leu Ile
50 55 60
Leu Gln Leu Val His Val Thr Gln Glu Asp Lys Arg Lys Thr Thr Gly
65 70 75 80
Glu Glu Asn Gly Val Glu Ala Glu Glu Trp Gly Lys Phe Leu His Thr
85 90 95
Lys Asn Lys Leu Tyr Thr Asp Phe Asp Glu Ile Arg Gln Glu Ile Glu
100 105 110
Asn Glu Thr Glu Arg Ile Ser Gly Asn Asn Lys Gly Val Ser Pro Glu
115 120 125
Pro Ile His Leu Lys Ile Phe Ser Pro Asn Val Val Asn Leu Thr Leu
130 135 140
Val Asp Leu Pro Gly Met Thr Lys Val Pro Val Gly Asp Gln Pro Lys
145 150 155 160
Asp Ile Glu Leu Gln Ile Arg Glu Leu Ile Leu Arg Phe Ile Ser Asn
165 170 175
Pro Asn Ser Ile Ile Leu Ala Val Thr Ala Ala Asn Thr Asp Met Ala
180 185 190
Thr Ser Glu Ala Leu Lys Ile Ser Arg Glu Val Asp Pro Asp Gly Arg
195 200 205
Arg Thr Leu Ala Val Ile Thr Lys Leu Asp Leu Met Asp Ala Gly Thr
210 215 220
Asp Ala Met Asp Val Leu Met Gly Arg Val Ile Pro Val Lys Leu Gly
225 230 235 240
Ile Ile Gly Val Val Asn Arg Ser Gln Leu Asp Ile Asn Asn Lys Lys
245 250 255
Ser Val Thr Asp Ser Ile Arg Asp Glu Tyr Ala Phe Leu Gln Lys Lys
260 265 270
Tyr Pro Ser Leu Ala Asn Arg Asn Gly Thr Lys Tyr Leu Ala Arg Thr
275 280 285
Leu Asn Arg Leu Leu Met His His Ile Arg Asp Cys Leu Pro Glu Leu
290 295 300
Lys Thr Arg Ile Asn Val Leu Ala Ala Gln Tyr Gln Ser Leu Leu Asn
305 310 315 320
Ser Tyr Gly Glu Pro Val Asp Asp Lys Ser Ala Thr Leu Leu Gln Leu
325 330 335
Ile Thr Lys Phe Ala Thr Glu Tyr Cys Asn Thr Ile Glu Gly Thr Ala
340 345 350
Lys Tyr Ile Glu Thr Ser Glu Leu Cys Gly Gly Ala Arg Ile Cys Tyr
355 360 365
Ile Phe His Glu Thr Phe Gly Arg Thr Leu Glu Ser Val Asp Pro Leu
370 375 380
Gly Gly Leu Asn Thr Ile Asp Ile Leu Thr Ala Ile Arg Asn Ala Thr
385 390 395 400
Gly Pro Arg Pro Ala Leu Phe Val Pro Glu Val Ser Phe Glu Leu Leu
405 410 415
Val Lys Arg Gln Ile Lys Arg Leu Glu Glu Pro Ser Leu Arg Cys Val
420 425 430
Glu Leu Val His Glu Glu Met Gln Arg Ile Ile Gln His Cys Ser Asn
435 440 445
Tyr Ser Thr Gln Glu Leu Leu Arg Phe Pro Lys Leu His Asp Ala Ile
450 455 460
Val Glu Val Val Thr Cys Leu Leu Arg Lys Arg Leu Pro Val Thr Asn
465 470 475 480
Glu Met Val His Asn Leu Val Ala Ile Glu Leu Ala Tyr Ile Asn Thr
485 490 495
Lys His Pro Asp Phe Ala Asp Ala Cys Gly Leu Met Asn Asn Asn Ile
500 505 510
Glu Glu Gln Arg Arg Asn Arg Leu Ala Arg Glu Leu Pro Ser Ala Val
515 520 525
Ser Arg Asp Lys Leu Ile Gln Asp Ser Arg Arg Glu Thr Lys Asn Val
530 535 540
Ala Ser Gly Gly Gly Gly Val Gly Asp Gly Val Gln Glu Pro Thr Thr
545 550 555 560
Gly Asn Trp Arg Gly Met Leu Lys Thr Ser Lys Ala Glu Glu Leu Leu
565 570 575
Ala Glu Glu Lys Ser Lys Pro Ile Pro Ile Met Pro Ala Ser Pro Gln
580 585 590
Lys Gly His Ala Val Asn Leu Leu Asp Val Pro Val Pro Val Ala Arg
595 600 605
Lys Leu Ser Ala Arg Glu Gln Arg Asp Cys Glu Val Ile Glu Arg Leu
610 615 620
Ile Lys Ser Tyr Phe Leu Ile Val Arg Lys Asn Ile Gln Asp Ser Val
625 630 635 640
Pro Lys Ala Val Met His Phe Leu Val Asn His Val Lys Asp Thr Leu
645 650 655
Gln Ser Glu Leu Val Gly Gln Leu Tyr Lys Ser Ser Leu Leu Asp Asp
660 665 670
Leu Leu Thr Glu Ser Glu Asp Met Ala Gln Arg Arg Lys Glu Ala Ala
675 680 685
Asp Met Leu Lys Ala Leu Gln Gly Ala Ser Gln Ile Ile Ala Glu Ile
690 695 700
Arg Glu Thr His Leu Trp
705 710


40
699
PRT
Homo sapiens

40
Met Glu Ala Leu Ile Pro Val Ile Asn Lys Leu Gln Asp Val Phe Asn
1 5 10 15
Thr Val Gly Ala Asp Ile Ile Gln Leu Pro Gln Ile Val Val Val Gly
20 25 30
Thr Gln Ser Ser Gly Lys Ser Ser Val Leu Glu Ser Leu Val Gly Arg
35 40 45
Asp Leu Leu Pro Arg Gly Thr Gly Ile Val Thr Arg Arg Pro Leu Ile
50 55 60
Leu Gln Leu Val His Val Thr Gln Glu Asp Lys Arg Lys Thr Thr Gly
65 70 75 80
Glu Glu Asn Gly Val Glu Ala Glu Glu Trp Gly Lys Phe Leu His Thr
85 90 95
Lys Asn Lys Leu Tyr Thr Asp Phe Asp Glu Ile Arg Gln Glu Ile Glu
100 105 110
Asn Glu Thr Glu Arg Ile Ser Gly Asn Asn Lys Gly Val Ser Pro Glu
115 120 125
Pro Ile His Leu Lys Ile Phe Ser Pro Asn Val Val Asn Leu Thr Leu
130 135 140
Val Asp Leu Pro Gly Met Thr Lys Val Pro Val Gly Asp Gln Pro Lys
145 150 155 160
Asp Ile Glu Leu Gln Ile Arg Glu Leu Ile Leu Arg Phe Ile Ser Asn
165 170 175
Pro Asn Ser Ile Ile Leu Ala Val Thr Ala Ala Asn Thr Asp Met Ala
180 185 190
Thr Ser Glu Ala Leu Lys Ile Ser Arg Glu Val Asp Pro Asp Gly Cys
195 200 205
Arg Thr Leu Ala Val Ile Thr Lys Leu Asp Leu Met Asp Ala Gly Thr
210 215 220
Asp Ala Met Asp Val Leu Met Gly Arg Val Ile Pro Val Lys Leu Gly
225 230 235 240
Ile Ile Gly Val Val Asn Arg Ser Gln Leu Asp Ile Asn Asn Lys Lys
245 250 255
Ser Val Thr Asp Ser Ile Arg Asp Glu Tyr Ala Phe Leu Gln Lys Lys
260 265 270
Tyr Pro Ser Leu Ala Asn Arg Asn Gly Thr Lys Tyr Leu Ala Arg Thr
275 280 285
Leu Asn Arg Leu Leu Met His His Ile Arg Asp Cys Leu Pro Glu Leu
290 295 300
Lys Thr Arg Ile Asn Val Leu Ala Ala Gln Tyr Gln Ser Leu Leu Asn
305 310 315 320
Ser Tyr Gly Glu Pro Val Asp Asp Lys Ser Ala Thr Leu Leu Gln Leu
325 330 335
Ile Thr Lys Phe Ala Thr Glu Tyr Cys Asn Thr Ile Glu Gly Thr Ala
340 345 350
Lys Tyr Ile Glu Thr Ser Glu Leu Cys Gly Gly Ala Arg Ile Cys Tyr
355 360 365
Ile Phe His Glu Thr Phe Gly Arg Thr Leu Glu Ser Val Asp Pro Leu
370 375 380
Gly Gly Leu Asn Thr Ile Asp Ile Leu Thr Ala Ile Arg Asn Ala Thr
385 390 395 400
Gly Pro Arg Pro Ala Leu Phe Val Pro Glu Val Ser Phe Glu Leu Leu
405 410 415
Val Lys Arg Gln Ile Lys Arg Leu Glu Glu Pro Ser Leu Arg Cys Val
420 425 430
Glu Leu Val His Glu Glu Met Gln Arg Ile Ile Gln His Cys Ser Asn
435 440 445
Tyr Ser Thr Gln Glu Leu Leu Arg Phe Pro Lys Leu His Asp Ala Ile
450 455 460
Val Glu Val Val Thr Cys Leu Leu Arg Lys Arg Leu Pro Val Thr Asn
465 470 475 480
Glu Met Val His Asn Leu Val Ala Ile Glu Leu Ala Tyr Ile Asn Thr
485 490 495
Lys His Pro Asp Phe Ala Asp Ala Cys Gly Leu Met Asn Asn Asn Ile
500 505 510
Glu Glu Gln Arg Arg Asn Arg Leu Ala Arg Glu Leu Pro Ser Ala Val
515 520 525
Ser Arg Asp Lys Val Ala Ser Gly Gly Gly Gly Val Gly Asp Gly Val
530 535 540
Gln Glu Pro Thr Thr Gly Asn Trp Arg Gly Met Leu Lys Thr Ser Lys
545 550 555 560
Ala Glu Glu Leu Leu Ala Glu Glu Lys Ser Lys Pro Ile Pro Ile Met
565 570 575
Pro Ala Ser Pro Gln Lys Gly His Ala Val Asn Leu Leu Asp Val Pro
580 585 590
Val Pro Val Ala Arg Lys Leu Ser Ala Arg Glu Gln Arg Asp Cys Glu
595 600 605
Val Ile Glu Arg Leu Ile Lys Ser Tyr Phe Leu Ile Val Arg Lys Asn
610 615 620
Ile Gln Asp Ser Val Pro Lys Ala Val Met His Phe Leu Val Asn His
625 630 635 640
Val Lys Asp Thr Leu Gln Ser Glu Leu Val Gly Gln Leu Tyr Lys Ser
645 650 655
Ser Leu Leu Asp Asp Leu Leu Thr Glu Ser Glu Asp Met Ala Gln Arg
660 665 670
Arg Lys Glu Ala Ala Asp Met Leu Lys Ala Leu Gln Gly Ala Ser Gln
675 680 685
Ile Ile Ala Glu Ile Arg Glu Thr His Leu Trp
690 695


41
954
PRT
Homo sapiens

41
Met Ala Glu Pro Gly His Ser His His Leu Ser Ala Arg Val Arg Gly
1 5 10 15
Arg Thr Glu Arg Arg Ile Pro Arg Leu Trp Arg Leu Leu Leu Trp Ala
20 25 30
Gly Thr Ala Phe Gln Val Thr Gln Gly Thr Gly Pro Glu Leu His Ala
35 40 45
Cys Lys Glu Ser Glu Tyr His Tyr Glu Tyr Thr Ala Cys Asp Ser Thr
50 55 60
Gly Ser Arg Trp Arg Val Ala Val Pro His Thr Pro Gly Leu Cys Thr
65 70 75 80
Ser Leu Pro Asp Pro Ile Lys Gly Thr Glu Cys Ser Phe Ser Cys Asn
85 90 95
Ala Gly Glu Phe Leu Asp Met Lys Asp Gln Ser Cys Lys Pro Cys Ala
100 105 110
Glu Gly Arg Tyr Ser Leu Gly Thr Gly Ile Arg Phe Asp Glu Trp Asp
115 120 125
Glu Leu Pro His Gly Phe Ala Ser Leu Ser Ala Asn Met Glu Leu Asp
130 135 140
Asp Ser Ala Ala Glu Ser Thr Gly Asn Cys Thr Ser Ser Lys Trp Val
145 150 155 160
Pro Arg Gly Asp Tyr Ile Ala Ser Asn Thr Asp Glu Cys Thr Ala Thr
165 170 175
Leu Met Tyr Ala Val Asn Leu Lys Gln Ser Gly Thr Val Asn Phe Glu
180 185 190
Tyr Tyr Tyr Pro Asp Ser Ser Ile Ile Phe Glu Phe Phe Val Gln Asn
195 200 205
Asp Gln Cys Gln Pro Asn Ala Asp Asp Ser Arg Trp Met Lys Thr Thr
210 215 220
Glu Lys Gly Trp Glu Phe His Ser Val Glu Leu Asn Arg Gly Asn Asn
225 230 235 240
Val Leu Tyr Trp Arg Thr Thr Ala Phe Ser Val Trp Thr Lys Val Pro
245 250 255
Lys Pro Val Leu Val Arg Asn Ile Ala Ile Thr Glu Lys Gly Ser Ser
260 265 270
Ser Cys Asn Val Arg Pro Ala Cys Thr Asp Lys Asp Tyr Phe Tyr Thr
275 280 285
His Thr Ala Cys Asp Ala Asn Gly Glu Thr Gln Leu Met Tyr Lys Trp
290 295 300
Ala Lys Pro Lys Ile Cys Ser Glu Asp Leu Glu Gly Ala Val Lys Leu
305 310 315 320
Pro Ala Ser Gly Val Lys Thr His Cys Pro Pro Cys Asn Pro Gly Phe
325 330 335
Phe Lys Thr Asn Asn Ser Thr Cys Gln Pro Cys Pro Tyr Gly Ser Tyr
340 345 350
Ser Asn Gly Ser Asp Cys Thr Arg Cys Pro Ala Gly Thr Glu Pro Ala
355 360 365
Val Gly Phe Glu Tyr Lys Trp Trp Asn Thr Leu Pro Thr Asn Met Glu
370 375 380
Thr Thr Val Leu Ser Gly Ile Asn Phe Glu Tyr Lys Gly Met Thr Gly
385 390 395 400
Trp Glu Val Ala Gly Asp His Ile Tyr Thr Ala Ala Gly Ala Ser Asp
405 410 415
Asn Asp Phe Met Ile Leu Thr Leu Val Val Pro Gly Phe Arg Pro Pro
420 425 430
Gln Ser Val Met Ala Asp Thr Glu Asn Lys Glu Val Ala Arg Ile Thr
435 440 445
Phe Val Phe Glu Thr Leu Cys Ser Val Asn Cys Glu Leu Tyr Phe Met
450 455 460
Val Gly Val Asn Ser Arg Thr Asn Thr Pro Val Glu Thr Trp Lys Gly
465 470 475 480
Ser Lys Gly Lys Gln Ser Tyr Thr Tyr Ile Ile Glu Glu Asn Thr Thr
485 490 495
Thr Ser Phe Thr Trp Ala Phe Gln Arg Thr Thr Phe His Glu Ala Ser
500 505 510
Arg Lys Tyr Thr Asn Asp Val Ala Lys Ile Tyr Ser Ile Asn Val Thr
515 520 525
Asn Val Met Asn Gly Val Ala Ser Tyr Cys Arg Pro Cys Ala Leu Glu
530 535 540
Ala Ser Asp Val Gly Ser Ser Cys Thr Ser Cys Pro Ala Gly Tyr Tyr
545 550 555 560
Ile Asp Arg Asp Ser Gly Thr Cys His Ser Cys Pro Thr Asn Thr Ile
565 570 575
Leu Lys Ala His Gln Pro Tyr Gly Val Gln Ala Cys Val Pro Cys Gly
580 585 590
Pro Gly Thr Lys Asn Asn Lys Ile His Ser Leu Cys Tyr Asn Asp Cys
595 600 605
Thr Phe Ser Arg Asn Thr Pro Thr Arg Thr Phe Asn Tyr Asn Phe Ser
610 615 620
Ala Leu Ala Asn Thr Val Thr Leu Ala Gly Gly Pro Ser Phe Thr Ser
625 630 635 640
Lys Gly Leu Lys Tyr Phe His His Phe Thr Leu Ser Leu Cys Gly Asn
645 650 655
Gln Gly Arg Lys Met Ser Val Cys Thr Asp Asn Val Thr Asp Leu Arg
660 665 670
Ile Pro Glu Gly Glu Ser Gly Phe Ser Lys Ser Ile Thr Ala Tyr Val
675 680 685
Cys Gln Ala Val Ile Ile Pro Pro Glu Val Thr Gly Tyr Lys Ala Gly
690 695 700
Val Ser Ser Gln Pro Val Ser Leu Ala Asp Arg Leu Ile Gly Val Thr
705 710 715 720
Thr Asp Met Thr Leu Asp Gly Ile Thr Ser Pro Ala Glu Leu Phe His
725 730 735
Leu Glu Ser Leu Gly Ile Pro Asp Val Ile Phe Phe Tyr Arg Ser Asn
740 745 750
Asp Val Thr Gln Ser Cys Ser Ser Gly Arg Ser Thr Thr Ile Arg Val
755 760 765
Arg Cys Ser Pro Gln Lys Thr Val Pro Gly Ser Leu Leu Leu Pro Gly
770 775 780
Thr Cys Ser Asp Gly Thr Cys Asp Gly Cys Asn Phe His Phe Leu Trp
785 790 795 800
Glu Ser Ala Ala Ala Cys Pro Leu Cys Ser Val Ala Asp Tyr His Ala
805 810 815
Ile Val Ser Ser Cys Val Ala Gly Ile Gln Lys Thr Thr Tyr Val Trp
820 825 830
Arg Glu Pro Lys Leu Cys Ser Gly Gly Ile Ser Leu Pro Glu Gln Arg
835 840 845
Val Thr Ile Cys Lys Thr Ile Asp Phe Trp Leu Lys Val Gly Ile Ser
850 855 860
Ala Gly Thr Cys Thr Ala Ile Leu Leu Thr Val Leu Thr Cys Tyr Phe
865 870 875 880
Trp Lys Lys Asn Gln Lys Leu Glu Tyr Lys Tyr Ser Lys Leu Val Met
885 890 895
Asn Ala Thr Leu Lys Asp Cys Asp Leu Pro Ala Ala Asp Ser Cys Ala
900 905 910
Ile Met Glu Gly Glu Asp Val Glu Asp Asp Leu Ile Phe Thr Ser Lys
915 920 925
Lys Ser Leu Phe Gly Lys Ile Lys Ser Phe Thr Ser Lys Gln Pro Ala
930 935 940
Pro Val Thr Ile Ser Leu Ser Glu Asp Ser
945 950


42
595
PRT
Homo sapiens

42
Met Thr Met Thr Leu His Thr Lys Ala Ser Gly Met Ala Leu Leu His
1 5 10 15
Gln Ile Gln Gly Asn Glu Leu Glu Pro Leu Asn Arg Pro Gln Leu Lys
20 25 30
Ile Pro Leu Glu Arg Pro Leu Gly Glu Val Tyr Leu Asp Ser Ser Lys
35 40 45
Pro Ala Val Tyr Asn Tyr Pro Glu Gly Ala Ala Tyr Glu Phe Asn Ala
50 55 60
Ala Ala Ala Ala Asn Ala Gln Val Tyr Gly Gln Thr Gly Leu Pro Tyr
65 70 75 80
Gly Pro Gly Ser Glu Ala Ala Ala Phe Gly Ser Asn Gly Leu Gly Gly
85 90 95
Phe Pro Pro Leu Asn Ser Val Ser Pro Ser Pro Leu Met Leu Leu His
100 105 110
Pro Pro Pro Gln Leu Ser Pro Phe Leu Gln Pro His Gly Gln Gln Val
115 120 125
Pro Tyr Tyr Leu Glu Asn Glu Pro Ser Gly Tyr Thr Val Arg Glu Ala
130 135 140
Gly Pro Pro Ala Phe Tyr Arg Pro Asn Ser Asp Asn Arg Arg Gln Gly
145 150 155 160
Gly Arg Glu Arg Leu Ala Ser Thr Asn Asp Lys Gly Ser Met Ala Met
165 170 175
Glu Ser Ala Lys Glu Thr Arg Tyr Cys Ala Val Cys Asn Asp Tyr Ala
180 185 190
Ser Gly Tyr His Tyr Gly Val Trp Ser Cys Glu Gly Cys Lys Ala Phe
195 200 205
Phe Lys Arg Ser Ile Gln Gly His Asn Asp Tyr Met Cys Pro Ala Thr
210 215 220
Asn Gln Cys Thr Ile Asp Lys Asn Arg Arg Lys Ser Cys Gln Ala Cys
225 230 235 240
Arg Leu Arg Lys Cys Tyr Glu Val Gly Met Met Lys Gly Gly Ile Arg
245 250 255
Lys Asp Arg Arg Gly Gly Arg Met Leu Lys His Lys Arg Gln Arg Asp
260 265 270
Asp Gly Glu Gly Arg Gly Glu Val Gly Ser Ala Gly Asp Met Arg Ala
275 280 285
Ala Asn Leu Trp Pro Ser Pro Leu Met Ile Lys Arg Ser Lys Lys Asn
290 295 300
Ser Leu Ala Leu Ser Leu Thr Ala Asp Gln Met Val Ser Ala Leu Leu
305 310 315 320
Asp Ala Glu Pro Pro Ile Leu Tyr Ser Glu Tyr Asp Pro Thr Arg Pro
325 330 335
Phe Ser Glu Ala Ser Met Met Gly Leu Leu Thr Asn Leu Ala Asp Arg
340 345 350
Glu Leu Val His Met Ile Asn Trp Ala Lys Arg Val Pro Gly Phe Val
355 360 365
Asp Leu Thr Leu His Asp Gln Val His Leu Leu Glu Cys Ala Trp Leu
370 375 380
Glu Ile Leu Met Ile Gly Leu Val Trp Arg Ser Met Glu His Pro Val
385 390 395 400
Lys Leu Leu Phe Ala Pro Asn Leu Leu Leu Asp Arg Asn Gln Gly Lys
405 410 415
Cys Val Glu Gly Met Val Glu Ile Phe Asp Met Leu Leu Ala Thr Ser
420 425 430
Ser Arg Phe Arg Met Met Asn Leu Gln Gly Glu Glu Phe Val Cys Leu
435 440 445
Lys Ser Ile Ile Leu Leu Asn Ser Gly Val Tyr Thr Phe Leu Ser Ser
450 455 460
Thr Leu Lys Ser Leu Glu Glu Lys Asp His Ile His Arg Val Leu Asp
465 470 475 480
Lys Ile Thr Asp Thr Leu Ile His Leu Met Ala Lys Ala Gly Leu Thr
485 490 495
Leu Gln Gln Gln His Gln Arg Leu Ala Gln Leu Leu Leu Ile Leu Ser
500 505 510
His Ile Arg His Met Ser Asn Lys Gly Met Glu His Leu Tyr Ser Met
515 520 525
Lys Cys Lys Asn Val Val Pro Leu Tyr Asp Leu Leu Leu Glu Met Leu
530 535 540
Asp Ala His Arg Leu His Ala Pro Thr Ser Arg Gly Gly Ala Ser Val
545 550 555 560
Glu Glu Thr Asp Gln Ser His Leu Ala Thr Ala Gly Ser Thr Ser Ser
565 570 575
His Ser Leu Gln Lys Tyr Tyr Ile Thr Gly Glu Ala Glu Gly Phe Pro
580 585 590
Ala Thr Val
595


43
1575
PRT
Homo sapiens

43
Met Ile Lys Asp Trp Thr Lys Glu His Val Lys Lys Trp Val Asn Glu
1 5 10 15
Asp Leu Lys Ile Asn Glu Gln Tyr Gly Gln Ile Leu Leu Ser Glu Glu
20 25 30
Val Thr Gly Leu Val Leu Gln Glu Leu Thr Glu Lys Asp Leu Val Glu
35 40 45
Met Gly Leu Pro Trp Gly Pro Ala Leu Leu Ile Lys Arg Ser Tyr Asn
50 55 60
Lys Leu Asn Ser Lys Ser Pro Glu Ser Asp Asn His Asp Pro Gly Gln
65 70 75 80
Leu Asp Asn Ser Lys Pro Ser Lys Thr Glu His Gln Lys Asn Pro Lys
85 90 95
His Thr Lys Lys Glu Glu Glu Asn Ser Met Ser Ser Asn Ile Asp Tyr
100 105 110
Asp Pro Arg Glu Ile Arg Asp Ile Lys Gln Glu Glu Ser Ile Leu Met
115 120 125
Lys Glu Asn Val Leu Asp Glu Val Ala Asn Ala Lys His Lys Lys Lys
130 135 140
Gly Lys Leu Lys Pro Glu Gln Leu Thr Cys Met Pro Tyr Pro Phe Asp
145 150 155 160
Gln Phe His Asp Ser His Arg Tyr Ile Glu His Tyr Thr Leu Gln Pro
165 170 175
Glu Thr Gly Ala Leu Asn Leu Ile Asp Pro Ile His Glu Phe Lys Ala
180 185 190
Leu Thr Asn Thr Glu Thr Ala Thr Glu Val Asp Ile Lys Met Lys Phe
195 200 205
Ser Asn Glu Val Phe Arg Phe Ala Ser Ala Cys Met Asn Ser Arg Thr
210 215 220
Asn Gly Thr Ile His Phe Gly Val Lys Asp Lys Pro His Gly Glu Ile
225 230 235 240
Val Gly Val Lys Ile Thr Ser Lys Ala Ala Phe Ile Asp His Phe Asn
245 250 255
Val Met Ile Lys Lys Tyr Phe Glu Glu Ser Glu Ile Asn Glu Ala Lys
260 265 270
Lys Cys Ile Arg Glu Pro Arg Phe Val Glu Val Leu Leu Gln Asn Asn
275 280 285
Thr Pro Ser Asp Arg Phe Val Ile Glu Val Asp Thr Ile Pro Lys His
290 295 300
Ser Ile Cys Asn Asp Lys Tyr Phe Tyr Ile Gln Met Gln Ile Cys Lys
305 310 315 320
Asp Lys Ile Trp Lys Gln Asn Gln Asn Leu Ser Leu Phe Val Arg Glu
325 330 335
Gly Ala Ser Ser Arg Asp Ile Leu Ala Asn Ser Lys Gln Arg Asp Val
340 345 350
Asp Phe Lys Ala Phe Leu Gln Asn Leu Lys Ser Leu Val Ala Ser Arg
355 360 365
Lys Glu Ala Glu Glu Glu Tyr Gly Met Lys Ala Met Lys Lys Glu Ser
370 375 380
Glu Gly Leu Lys Leu Val Lys Leu Leu Ile Gly Asn Arg Asp Ser Leu
385 390 395 400
Asp Asn Ser Tyr Tyr Asp Trp Tyr Ile Leu Val Thr Asn Lys Cys His
405 410 415
Pro Asn Gln Ile Lys His Leu Asp Phe Leu Lys Glu Ile Lys Trp Phe
420 425 430
Ala Val Leu Glu Phe Asp Pro Glu Ser Met Ile Asn Gly Val Val Lys
435 440 445
Ala Tyr Lys Glu Ser Arg Val Ala Asn Leu His Phe Pro Asn Gln Tyr
450 455 460
Glu Asp Lys Thr Thr Asn Met Trp Glu Lys Ile Ser Thr Leu Asn Leu
465 470 475 480
Tyr Gln Gln Pro Ser Trp Ile Phe Cys Asn Gly Arg Ser Asp Leu Lys
485 490 495
Ser Glu Thr Tyr Lys Pro Leu Glu Pro His Leu Trp Gln Arg Glu Arg
500 505 510
Ala Ser Glu Val Arg Lys Leu Ile Leu Phe Leu Thr Asp Glu Asn Ile
515 520 525
Met Thr Arg Gly Lys Phe Leu Val Val Phe Leu Leu Leu Ser Ser Val
530 535 540
Glu Ser Pro Gly Asp Pro Leu Ile Glu Thr Phe Trp Ala Phe Tyr Gln
545 550 555 560
Ala Leu Lys Gly Met Glu Asn Met Leu Cys Ile Ser Val Asn Ser His
565 570 575
Ile Tyr Gln Arg Trp Lys Asp Leu Leu Gln Thr Arg Met Lys Met Glu
580 585 590
Asp Glu Leu Thr Asn His Ser Ile Ser Thr Leu Asn Ile Glu Leu Val
595 600 605
Asn Ser Thr Ile Leu Lys Leu Lys Ser Val Thr Arg Ser Ser Arg Arg
610 615 620
Phe Leu Pro Ala Arg Gly Ser Ser Ser Val Ile Leu Glu Lys Lys Lys
625 630 635 640
Glu Asp Val Leu Thr Ala Leu Glu Ile Leu Cys Glu Asn Glu Cys Thr
645 650 655
Glu Thr Asp Ile Glu Lys Asp Lys Ser Lys Phe Leu Glu Phe Lys Lys
660 665 670
Ser Lys Glu Glu His Phe Tyr Arg Gly Gly Lys Val Ser Trp Trp Asn
675 680 685
Phe Tyr Phe Ser Ser Glu Asn Tyr Ser Ser Asp Phe Val Lys Arg Asp
690 695 700
Ser Tyr Glu Lys Leu Lys Asp Leu Ile His Cys Trp Ala Glu Ser Pro
705 710 715 720
Lys Pro Ile Phe Ala Lys Ile Ile Asn Leu Tyr His His Pro Gly Cys
725 730 735
Gly Gly Thr Thr Leu Ala Met His Val Leu Trp Asp Leu Lys Lys Asn
740 745 750
Phe Arg Cys Ala Val Leu Lys Asn Lys Thr Thr Asp Phe Ala Glu Ile
755 760 765
Ala Glu Gln Val Ile Asn Leu Val Thr Tyr Arg Ala Lys Ser His Gln
770 775 780
Asp Tyr Ile Pro Val Leu Leu Leu Val Asp Asp Phe Glu Glu Gln Glu
785 790 795 800
Asn Val Tyr Phe Leu Gln Asn Ala Ile His Ser Val Leu Ala Glu Lys
805 810 815
Asp Leu Arg Tyr Glu Lys Thr Leu Val Ile Ile Leu Asn Cys Met Arg
820 825 830
Ser Arg Asn Pro Asp Glu Ser Ala Lys Leu Ala Asp Ser Ile Ala Leu
835 840 845
Asn Tyr Gln Leu Ser Ser Lys Glu Gln Arg Ala Phe Gly Ala Lys Leu
850 855 860
Lys Glu Ile Glu Lys Gln His Lys Asn Cys Glu Asn Phe Tyr Ser Phe
865 870 875 880
Met Ile Met Lys Ser Asn Phe Asp Glu Thr Tyr Ile Glu Asn Val Val
885 890 895
Arg Asn Ile Leu Lys Gly Gln Asp Val Asp Ser Lys Glu Ala Gln Leu
900 905 910
Ile Ser Phe Leu Ala Leu Leu Ser Ser Tyr Val Thr Asp Ser Thr Ile
915 920 925
Ser Val Ser Gln Cys Glu Ile Phe Leu Gly Ile Ile Tyr Thr Ser Thr
930 935 940
Pro Trp Glu Pro Glu Ser Leu Glu Asp Lys Met Gly Thr Tyr Ser Thr
945 950 955 960
Leu Leu Ile Lys Thr Glu Val Ala Glu Tyr Gly Arg Tyr Thr Gly Val
965 970 975
Arg Ile Ile His Pro Leu Ile Ala Leu Tyr Cys Leu Lys Glu Leu Glu
980 985 990
Arg Ser Tyr His Leu Asp Lys Cys Gln Ile Ala Leu Asn Ile Leu Glu
995 1000 1005
Glu Asn Leu Phe Tyr Asp Ser Gly Ile Gly Arg Asp Lys Phe Gln
1010 1015 1020
His Asp Val Gln Thr Leu Leu Leu Thr Arg Gln Arg Lys Val Tyr
1025 1030 1035
Gly Asp Glu Thr Asp Thr Leu Phe Ser Pro Leu Met Glu Ala Leu
1040 1045 1050
Gln Asn Lys Asp Ile Glu Lys Val Leu Ser Ala Gly Ser Arg Arg
1055 1060 1065
Phe Pro Gln Asn Ala Phe Ile Cys Gln Ala Leu Ala Arg His Phe
1070 1075 1080
Tyr Ile Lys Glu Lys Asp Phe Asn Thr Ala Leu Asp Trp Ala Arg
1085 1090 1095
Gln Ala Lys Met Lys Ala Pro Lys Asn Ser Tyr Ile Ser Asp Thr
1100 1105 1110
Leu Gly Gln Val Tyr Lys Ser Glu Ile Lys Trp Trp Leu Asp Gly
1115 1120 1125
Asn Lys Asn Cys Arg Ser Ile Thr Val Asn Asp Leu Thr His Leu
1130 1135 1140
Leu Glu Ala Ala Glu Lys Ala Ser Arg Ala Phe Lys Glu Ser Gln
1145 1150 1155
Arg Gln Thr Asp Ser Lys Asn Tyr Glu Thr Glu Asn Trp Ser Pro
1160 1165 1170
Gln Lys Ser Gln Arg Arg Tyr Asp Met Tyr Asn Thr Ala Cys Phe
1175 1180 1185
Leu Gly Glu Ile Glu Val Gly Leu Tyr Thr Ile Gln Ile Leu Gln
1190 1195 1200
Leu Thr Pro Phe Phe His Lys Glu Asn Glu Leu Ser Lys Lys His
1205 1210 1215
Met Val Gln Phe Leu Ser Gly Lys Trp Thr Ile Pro Pro Asp Pro
1220 1225 1230
Arg Asn Glu Cys Tyr Leu Ala Leu Ser Lys Phe Thr Ser His Leu
1235 1240 1245
Lys Asn Leu Gln Ser Asp Leu Lys Arg Cys Phe Asp Phe Phe Ile
1250 1255 1260
Asp Tyr Met Val Leu Leu Lys Met Arg Tyr Thr Gln Lys Glu Ile
1265 1270 1275
Ala Glu Ile Met Leu Ser Lys Lys Val Ser Arg Cys Phe Arg Lys
1280 1285 1290
Tyr Thr Glu Leu Phe Cys His Leu Asp Pro Cys Leu Leu Gln Ser
1295 1300 1305
Lys Glu Ser Gln Leu Leu Gln Glu Glu Asn Cys Arg Lys Lys Leu
1310 1315 1320
Glu Ala Leu Arg Ala Asp Arg Phe Ala Gly Leu Leu Glu Tyr Leu
1325 1330 1335
Asn Pro Asn Tyr Lys Asp Ala Thr Thr Met Glu Ser Ile Val Asn
1340 1345 1350
Glu Tyr Ala Phe Leu Leu Gln Gln Asn Ser Lys Lys Pro Met Thr
1355 1360 1365
Asn Glu Lys Gln Asn Ser Ile Leu Ala Asn Ile Ile Leu Ser Cys
1370 1375 1380
Leu Lys Pro Asn Ser Lys Leu Ile Gln Pro Leu Thr Thr Leu Lys
1385 1390 1395
Lys Gln Leu Arg Glu Val Leu Gln Phe Val Gly Leu Ser His Gln
1400 1405 1410
Tyr Pro Gly Pro Tyr Phe Leu Ala Cys Leu Leu Phe Trp Pro Glu
1415 1420 1425
Asn Gln Glu Leu Asp Gln Asp Ser Lys Leu Ile Glu Lys Tyr Val
1430 1435 1440
Ser Ser Leu Asn Arg Ser Phe Arg Gly Gln Tyr Lys Arg Met Cys
1445 1450 1455
Arg Ser Lys Gln Ala Ser Thr Leu Phe Tyr Leu Gly Lys Arg Lys
1460 1465 1470
Gly Leu Asn Ser Ile Val His Lys Ala Lys Ile Glu Gln Tyr Phe
1475 1480 1485
Asp Lys Ala Gln Asn Thr Asn Ser Leu Trp His Ser Gly Asp Val
1490 1495 1500
Trp Lys Lys Asn Glu Val Lys Asp Leu Leu Arg Arg Leu Thr Gly
1505 1510 1515
Gln Ala Glu Gly Lys Leu Ile Ser Val Glu Tyr Gly Thr Glu Glu
1520 1525 1530
Lys Ile Lys Ile Pro Val Ile Ser Val Tyr Ser Gly Pro Leu Arg
1535 1540 1545
Ser Gly Arg Asn Ile Glu Arg Val Ser Phe Tyr Leu Gly Phe Ser
1550 1555 1560
Ile Glu Gly Pro Leu Ala Tyr Asp Ile Glu Val Ile
1565 1570 1575


44
1770
PRT
Homo sapiens

44
Met Asp Gly Met Thr Glu Ala Cys Ile Lys Gly Gly Ile Glu Ala Cys
1 5 10 15
Tyr Ala Ala Val Ser Cys Val Cys Thr Leu Leu Gly Ala Leu Asp Glu
20 25 30
Leu Ser Gln Gly Lys Gly Leu Ser Glu Gly Gln Val Gln Leu Leu Leu
35 40 45
Leu Arg Leu Glu Glu Leu Lys Asp Gly Ala Glu Trp Ser Arg Asp Ser
50 55 60
Met Glu Ile Asn Glu Ala Asp Phe Arg Trp Gln Arg Arg Val Leu Ser
65 70 75 80
Ser Glu His Thr Pro Trp Glu Ser Gly Asn Glu Arg Ser Leu Asp Ile
85 90 95
Ser Ile Ser Val Thr Thr Asp Thr Gly Gln Thr Thr Leu Glu Gly Glu
100 105 110
Leu Gly Gln Thr Thr Pro Glu Asp His Ser Gly Asn His Lys Asn Ser
115 120 125
Leu Lys Ser Pro Ala Ile Pro Glu Gly Lys Glu Thr Leu Ser Lys Val
130 135 140
Leu Glu Thr Glu Ala Val Asp Gln Pro Asp Val Val Gln Arg Ser His
145 150 155 160
Thr Val Pro Tyr Pro Asp Ile Thr Asn Phe Leu Ser Val Asp Cys Arg
165 170 175
Thr Arg Ser Tyr Gly Ser Arg Tyr Ser Glu Ser Asn Phe Ser Val Asp
180 185 190
Asp Gln Asp Leu Ser Arg Thr Glu Phe Asp Ser Cys Asp Gln Tyr Ser
195 200 205
Met Ala Ala Glu Lys Asp Ser Gly Arg Ser Asp Val Ser Asp Ile Gly
210 215 220
Ser Asp Asn Cys Ser Leu Ala Asp Glu Glu Gln Thr Pro Arg Asp Cys
225 230 235 240
Leu Gly His Arg Ser Leu Arg Thr Ala Ala Leu Ser Leu Lys Leu Leu
245 250 255
Lys Asn Gln Glu Ala Asp Gln His Ser Ala Arg Leu Phe Ile Gln Ser
260 265 270
Leu Glu Gly Leu Leu Pro Arg Leu Leu Ser Leu Ser Asn Val Glu Glu
275 280 285
Val Asp Thr Ala Leu Gln Asn Phe Ala Ser Thr Phe Cys Ser Gly Met
290 295 300
Met His Ser Pro Gly Phe Asp Gly Asn Ser Ser Leu Ser Phe Gln Met
305 310 315 320
Leu Met Asn Ala Asp Ser Leu Tyr Thr Ala Ala His Cys Ala Leu Leu
325 330 335
Leu Asn Leu Lys Leu Ser His Gly Asp Tyr Tyr Arg Lys Arg Pro Thr
340 345 350
Leu Ala Pro Gly Val Met Lys Asp Phe Met Lys Gln Val Gln Thr Ser
355 360 365
Gly Val Leu Met Val Phe Ser Gln Ala Trp Ile Glu Glu Leu Tyr His
370 375 380
Gln Val Leu Asp Arg Asn Met Leu Gly Glu Ala Gly Tyr Trp Gly Ser
385 390 395 400
Pro Glu Asp Asn Ser Leu Pro Leu Ile Thr Met Leu Thr Asp Ile Asp
405 410 415
Gly Leu Glu Ser Ser Ala Ile Gly Gly Gln Leu Met Ala Ser Ala Ala
420 425 430
Thr Glu Ser Pro Phe Ala Gln Ser Arg Arg Ile Asp Asp Ser Thr Val
435 440 445
Ala Gly Val Ala Phe Ala Arg Tyr Ile Leu Val Gly Cys Trp Lys Asn
450 455 460
Leu Ile Asp Thr Leu Ser Thr Pro Leu Thr Gly Arg Met Ala Gly Ser
465 470 475 480
Ser Lys Gly Leu Ala Phe Ile Leu Gly Ala Glu Gly Ile Lys Glu Gln
485 490 495
Asn Gln Lys Glu Arg Asp Ala Ile Cys Met Ser Leu Asp Gly Leu Arg
500 505 510
Lys Ala Ala Arg Leu Ser Cys Ala Leu Gly Val Ala Ala Asn Cys Ala
515 520 525
Ser Ala Leu Ala Gln Met Ala Ala Ala Ser Cys Val Gln Glu Glu Lys
530 535 540
Glu Glu Arg Glu Ala Gln Glu Pro Ser Asp Ala Ile Thr Gln Val Lys
545 550 555 560
Leu Lys Val Glu Gln Lys Leu Glu Gln Ile Gly Lys Val Gln Gly Val
565 570 575
Trp Leu His Thr Ala His Val Leu Cys Met Glu Ala Ile Leu Ser Val
580 585 590
Gly Leu Glu Met Gly Ser His Asn Pro Asp Cys Trp Pro His Val Phe
595 600 605
Arg Val Cys Glu Tyr Val Gly Thr Leu Glu His Asn His Phe Ser Asp
610 615 620
Gly Ala Ser Gln Pro Pro Leu Thr Ile Ser Gln Pro Gln Lys Ala Thr
625 630 635 640
Gly Ser Ala Gly Leu Leu Gly Asp Pro Glu Cys Glu Gly Ser Pro Pro
645 650 655
Glu His Ser Pro Glu Gln Gly Arg Ser Leu Ser Thr Ala Pro Val Val
660 665 670
Gln Pro Leu Ser Ile Gln Asp Leu Val Arg Glu Gly Ser Arg Gly Arg
675 680 685
Ala Ser Asp Phe Arg Gly Gly Ser Leu Met Ser Gly Ser Ser Ala Ala
690 695 700
Lys Val Val Leu Thr Leu Ser Thr Gln Ala Asp Arg Leu Phe Glu Asp
705 710 715 720
Ala Thr Asp Lys Leu Asn Leu Met Ala Leu Gly Gly Phe Leu Tyr Gln
725 730 735
Leu Lys Lys Ala Ser Gln Ser Gln Leu Phe His Ser Val Thr Asp Thr
740 745 750
Val Asp Tyr Ser Leu Ala Met Pro Gly Glu Val Lys Ser Thr Gln Asp
755 760 765
Arg Lys Ser Ala Leu His Leu Phe Arg Leu Gly Asn Ala Met Leu Arg
770 775 780
Ile Val Arg Ser Lys Ala Arg Pro Leu Leu His Val Met Arg Cys Trp
785 790 795 800
Ser Leu Val Ala Pro His Leu Val Glu Ala Ala Cys His Lys Glu Arg
805 810 815
His Val Ser Gln Lys Ala Val Ser Phe Ile His Asp Ile Leu Thr Glu
820 825 830
Val Leu Thr Asp Trp Asn Glu Pro Pro His Phe His Phe Asn Glu Ala
835 840 845
Leu Phe Arg Pro Phe Glu Arg Ile Met Gln Leu Glu Leu Cys Asp Glu
850 855 860
Asp Val Gln Asp Gln Val Val Thr Ser Ile Gly Glu Leu Val Glu Val
865 870 875 880
Cys Ser Thr Gln Ile Gln Ser Gly Trp Arg Pro Leu Phe Ser Ala Leu
885 890 895
Glu Thr Val His Gly Gly Asn Lys Ser Glu Met Lys Glu Tyr Leu Val
900 905 910
Gly Asp Tyr Ser Met Gly Lys Gly Gln Ala Pro Val Phe Asp Val Phe
915 920 925
Glu Ala Phe Leu Asn Thr Asp Asn Ile Gln Val Phe Ala Asn Ala Ala
930 935 940
Thr Ser Tyr Ile Met Cys Leu Met Lys Phe Val Lys Gly Leu Gly Glu
945 950 955 960
Val Asp Cys Lys Glu Ile Gly Asp Cys Ala Pro Ala Pro Gly Ala Pro
965 970 975
Ser Thr Asp Leu Cys Leu Pro Ala Leu Asp Tyr Leu Arg Arg Cys Ser
980 985 990
Gln Leu Leu Ala Lys Ile Tyr Lys Met Pro Leu Lys Pro Ile Phe Leu
995 1000 1005
Ser Gly Arg Leu Ala Gly Leu Pro Arg Arg Leu Gln Glu Gln Ser
1010 1015 1020
Ala Ser Ser Glu Asp Gly Ile Glu Ser Val Leu Ser Asp Phe Asp
1025 1030 1035
Asp Asp Thr Gly Leu Ile Glu Val Trp Ile Ile Leu Leu Glu Gln
1040 1045 1050
Leu Thr Ala Ala Val Ser Asn Cys Pro Arg Gln His Gln Pro Pro
1055 1060 1065
Thr Leu Asp Leu Leu Phe Glu Leu Leu Arg Asp Val Thr Lys Thr
1070 1075 1080
Pro Gly Pro Gly Phe Gly Ile Tyr Ala Val Val His Leu Leu Leu
1085 1090 1095
Pro Val Met Ser Val Trp Leu Arg Arg Ser His Lys Asp His Ser
1100 1105 1110
Tyr Trp Asp Met Ala Ser Ala Asn Phe Lys His Ala Ile Gly Leu
1115 1120 1125
Ser Cys Glu Leu Val Val Glu His Ile Gln Ser Phe Leu His Ser
1130 1135 1140
Asp Ile Arg Tyr Glu Ser Met Ile Asn Thr Met Leu Lys Asp Leu
1145 1150 1155
Phe Glu Leu Leu Val Ala Cys Val Ala Lys Pro Thr Glu Thr Ile
1160 1165 1170
Ser Arg Val Gly Cys Ser Cys Ile Arg Tyr Val Leu Val Thr Ala
1175 1180 1185
Gly Pro Val Phe Thr Glu Glu Met Trp Arg Leu Ala Cys Cys Ala
1190 1195 1200
Leu Gln Asp Ala Phe Ser Ala Thr Leu Lys Pro Val Lys Asp Leu
1205 1210 1215
Leu Gly Cys Phe His Ser Gly Thr Glu Ser Phe Ser Gly Glu Gly
1220 1225 1230
Cys Gln Val Arg Val Ala Ala Pro Ser Ser Ser Pro Ser Ala Glu
1235 1240 1245
Ala Glu Tyr Trp Arg Ile Arg Ala Met Ala Gln Gln Val Phe Met
1250 1255 1260
Leu Asp Thr Gln Cys Ser Pro Lys Thr Pro Asn Asn Phe Asp His
1265 1270 1275
Ala Gln Ser Cys Gln Leu Ile Ile Glu Leu Pro Pro Asp Glu Lys
1280 1285 1290
Pro Asn Gly His Thr Lys Lys Ser Val Ser Phe Arg Glu Ile Val
1295 1300 1305
Val Ser Leu Leu Ser His Gln Val Leu Leu Gln Asn Leu Tyr Asp
1310 1315 1320
Ile Leu Leu Glu Glu Phe Val Lys Gly Pro Ser Pro Gly Glu Glu
1325 1330 1335
Lys Thr Ile Gln Val Pro Glu Ala Lys Leu Ala Gly Phe Leu Arg
1340 1345 1350
Tyr Ile Ser Met Gln Asn Leu Ala Val Ile Phe Asp Leu Leu Leu
1355 1360 1365
Asp Ser Tyr Arg Thr Ala Arg Glu Phe Asp Thr Ser Pro Gly Leu
1370 1375 1380
Lys Cys Leu Leu Lys Lys Val Ser Gly Ile Gly Gly Ala Ala Asn
1385 1390 1395
Leu Tyr Arg Gln Ser Ala Met Ser Phe Asn Ile Tyr Phe His Ala
1400 1405 1410
Leu Val Cys Ala Val Leu Thr Asn Gln Glu Thr Ile Thr Ala Glu
1415 1420 1425
Gln Val Lys Lys Val Leu Phe Glu Asp Asp Glu Arg Ser Thr Asp
1430 1435 1440
Ser Ser Gln Gln Cys Ser Ser Glu Asp Glu Asp Ile Phe Glu Glu
1445 1450 1455
Thr Ala Gln Val Ser Pro Pro Arg Gly Lys Glu Lys Arg Gln Trp
1460 1465 1470
Arg Ala Arg Met Pro Leu Leu Ser Val Gln Pro Val Ser Asn Ala
1475 1480 1485
Asp Trp Val Trp Leu Val Lys Arg Leu His Lys Leu Cys Met Glu
1490 1495 1500
Leu Cys Asn Asn Tyr Ile Gln Met His Leu Asp Leu Glu Asn Cys
1505 1510 1515
Met Glu Glu Pro Pro Ile Phe Lys Gly Asp Pro Phe Phe Ile Leu
1520 1525 1530
Pro Ser Phe Gln Ser Glu Ser Ser Thr Pro Ser Thr Gly Gly Phe
1535 1540 1545
Ser Gly Lys Glu Thr Pro Ser Glu Asp Asp Arg Ser Gln Ser Arg
1550 1555 1560
Glu His Met Gly Glu Ser Leu Ser Leu Lys Ala Gly Gly Gly Asp
1565 1570 1575
Leu Leu Leu Pro Pro Ser Pro Lys Val Glu Lys Lys Asp Pro Ser
1580 1585 1590
Arg Lys Lys Glu Trp Trp Glu Asn Ala Gly Asn Lys Ile Tyr Thr
1595 1600 1605
Met Ala Ala Asp Lys Thr Ile Ser Lys Leu Met Thr Glu Tyr Lys
1610 1615 1620
Lys Arg Lys Gln Gln His Asn Leu Ser Ala Phe Pro Lys Glu Val
1625 1630 1635
Lys Val Glu Lys Lys Gly Glu Pro Leu Gly Pro Arg Gly Gln Asp
1640 1645 1650
Ser Pro Leu Leu Gln Arg Pro Gln His Leu Met Asp Gln Gly Gln
1655 1660 1665
Met Arg His Ser Phe Ser Ala Gly Pro Glu Leu Leu Arg Gln Asp
1670 1675 1680
Lys Arg Pro Arg Ser Gly Ser Thr Gly Ser Ser Leu Ser Val Ser
1685 1690 1695
Val Arg Asp Ala Glu Ala Gln Ile Gln Ala Trp Thr Asn Met Val
1700 1705 1710
Leu Thr Val Leu Asn Gln Ile Gln Ile Leu Pro Asp Gln Thr Phe
1715 1720 1725
Thr Ala Leu Gln Pro Ala Val Phe Pro Cys Ile Ser Gln Leu Thr
1730 1735 1740
Cys His Val Thr Asp Ile Arg Val Arg Gln Ala Val Arg Glu Trp
1745 1750 1755
Leu Gly Arg Val Gly Arg Val Tyr Asp Ile Ile Val
1760 1765 1770