ID CO5A1_HUMAN Reviewed; 1838 AA. AC P20908; A0A087WXW9; Q15094; Q5SUX4; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 3. DT 27-MAR-2024, entry version 235. DE RecName: Full=Collagen alpha-1(V) chain; DE Flags: Precursor; GN Name=COL5A1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 556-565 RP (ISOFORMS 1/2). RX PubMed=2071595; DOI=10.1016/s0021-9258(18)98813-7; RA Takahara K., Seto Y., Okasawa K., Okamoto N., Noda A., Yaoi Y., Kato I.; RT "Complete primary structure of human collagen alpha 1 (V) chain."; RL J. Biol. Chem. 266:13124-13129(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1722213; DOI=10.1016/s0021-9258(18)54290-3; RA Greenspan D.S., Cheng W., Hoffman G.G.; RT "The pro-alpha-1(V) collagen chain: complete primary structure, RT distribution of expression, and comparison with the pro-alpha-1(XI) RT collagen chain."; RL J. Biol. Chem. 266:24727-24733(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP PROTEIN SEQUENCE OF 621-822 (ISOFORMS 1/2), AND HYDROXYLATION AT PRO-621; RP LYS-627; PRO-639; LYS-642; PRO-648; PRO-654; PRO-657; PRO-675; PRO-678; RP LYS-687; PRO-690; PRO-696; PRO-705; LYS-708; PRO-717; PRO-720; PRO-726; RP PRO-732; LYS-744; PRO-750; PRO-756; PRO-762; PRO-765; PRO-771; LYS-774; RP PRO-780; PRO-789; LYS-795; LYS-804; LYS-807; LYS-810; PRO-816 AND LYS-819. RC TISSUE=Chorioamniotic membrane; RX PubMed=2496661; DOI=10.1016/0003-9861(89)90262-2; RA Seyer J.M., Kang A.H.; RT "Covalent structure of collagen: amino acid sequence of three cyanogen RT bromide-derived peptides from human alpha 1(V) collagen chain."; RL Arch. Biochem. Biophys. 271:120-129(1989). RN [5] RP PROTEIN SEQUENCE OF 823-950 (ISOFORMS 1/2), AND HEPARIN-BINDING. RX PubMed=2203476; DOI=10.1016/0304-4165(90)90108-9; RA Yaoi Y., Hashimoto K., Koitabashi H., Takahara K., Ito M., Kato I.; RT "Primary structure of the heparin-binding site of type V collagen."; RL Biochim. Biophys. Acta 1035:139-145(1990). RN [6] RP PROTEIN SEQUENCE OF 556-571 (ISOFORMS 1/2). RC TISSUE=Placenta; RX PubMed=1571108; DOI=10.1515/bchm3.1992.373.1.69; RA Mann K.; RT "Isolation of the alpha 3-chain of human type V collagen and RT characterization by partial sequencing."; RL Biol. Chem. Hoppe-Seyler 373:69-75(1992). RN [7] RP PROTEIN SEQUENCE OF 565-576; 756-772; 1012-1029; 1219-1232 AND 1465-1477 RP (ISOFORMS 1/2), AND HYDROXYLATION AT PRO-570; PRO-576; PRO-756; PRO-762; RP PRO-834; LYS-846; PRO-861; LYS-864; PRO-870; PRO-873; PRO-876; LYS-882; RP PRO-888; PRO-891; LYS-897; PRO-903; PRO-906; PRO-930; PRO-945; PRO-1017; RP PRO-1020; PRO-1023; PRO-1029; PRO-1221; PRO-1224; PRO-1467 AND PRO-1470. RC TISSUE=Chorioamniotic membrane; RX PubMed=8181482; DOI=10.1111/j.1432-1033.1994.tb18815.x; RA Moradi-Ameli M., Rousseau J.C., Kleman J.P., Champliaud M.-F., RA Boutillon M.-M., Bernillon J., Wallach J.M., van der Rest M.; RT "Diversity in the processing events at the N-terminus of type-V collagen."; RL Eur. J. Biochem. 221:987-995(1994). RN [8] RP INTERACTION WITH CSPG4. RX PubMed=9099729; DOI=10.1074/jbc.272.16.10769; RA Tillet E., Ruggiero F., Nishiyama A., Stallcup W.B.; RT "The membrane-spanning proteoglycan NG2 binds to collagens V and VI through RT the central nonglobular domain of its core protein."; RL J. Biol. Chem. 272:10769-10776(1997). RN [9] RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2). RX PubMed=22149965; DOI=10.3109/03008207.2011.636160; RA Mitchell A.L., Judis L.M., Schwarze U., Vaynshtok P.M., Drumm M.L., RA Byers P.H.; RT "Characterization of tissue-specific and developmentally regulated RT alternative splicing of exon 64 in the COL5A1 gene."; RL Connect. Tissue Res. 53:267-276(2012). RN [10] RP INVOLVEMENT IN EDSCL1, AND VARIANT EDSCL1 SER-1639. RX PubMed=9042913; RA de Paepe A., Nuytinck L., Hausser I., Anton-Lamprecht I., Naeyaert J.-M.; RT "Mutations in the COL5A1 gene are causal in the Ehlers-Danlos syndromes I RT and II."; RL Am. J. Hum. Genet. 60:547-554(1997). RN [11] RP VARIANT ASN-229, AND ASSOCIATION WITH INCREASED RISK OF CERVICAL ARTERY RP DISSECTION. RX PubMed=10471441; DOI=10.1161/01.str.30.9.1887; RA Grond-Ginsbach C., Weber R., Haas J., Orberk E., Kunz S., Busse O., RA Hausser I., Brandt T., Wildemann B.; RT "Mutations in the COL5A1 coding sequence are not common in patients with RT spontaneous cervical artery dissections."; RL Stroke 30:1887-1890(1999). RN [12] RP VARIANTS EDSCL1 SER-530 AND ASP-1489. RX PubMed=10602121; RX DOI=10.1002/(sici)1096-8628(20000103)90:1<72::aid-ajmg13>3.0.co;2-c; RA Giunta C., Steinmann B.; RT "Compound heterozygosity for a disease-causing G1489E and disease-modifying RT G530S substitution in COL5A1 of a patient with the classical type of RT Ehlers-Danlos syndrome: an explanation of intrafamilial variability?"; RL Am. J. Med. Genet. 90:72-79(2000). RN [13] RP ERRATUM OF PUBMED:10602121. RA Giunta C., Steinmann B.; RL Am. J. Med. Genet. 93:342-342(2000). RN [14] RP VARIANT EDSCL1 SER-530. RX PubMed=11992482; DOI=10.1002/ajmg.10373; RA Giunta C., Nuytinck L., Raghunath M., Hausser I., De Paepe A., RA Steinmann B.; RT "Homozygous Gly530Ser substitution in COL5A1 causes mild classical Ehlers- RT Danlos syndrome."; RL Am. J. Med. Genet. 109:284-290(2002). RN [15] RP VARIANTS EDSCL1 SER-530 AND CYS-1486, AND VARIANTS ASP-114; ASN-192 AND RP SER-951. RX PubMed=15580559; DOI=10.1002/humu.20107; RA Malfait F., Coucke P., Symoens S., Loeys B., Nuytinck L., De Paepe A.; RT "The molecular basis of classic Ehlers-Danlos syndrome: a comprehensive RT study of biochemical and molecular findings in 48 unrelated patients."; RL Hum. Mutat. 25:28-37(2005). RN [16] RP VARIANTS EDSCL1 ARG-25 AND PRO-25, AND CHARACTERIZATION OF VARIANTS EDSCL1 RP ARG-25 AND PRO-25. RX PubMed=18972565; DOI=10.1002/humu.20887; RA Symoens S., Malfait F., Renard M., Andre J., Hausser I., Loeys B., RA Coucke P., De Paepe A.; RT "COL5A1 signal peptide mutations interfere with protein secretion and cause RT classic Ehlers-Danlos syndrome."; RL Hum. Mutat. 30:E395-E403(2009). RN [17] RP VARIANT LEU-908. RX PubMed=21248752; DOI=10.1038/nature09639; RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M., RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.; RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene RT PBRM1 in renal carcinoma."; RL Nature 469:539-542(2011). RN [18] RP VARIANTS VAL-863 AND MET-1140. RX PubMed=26477546; DOI=10.1016/j.ajhg.2015.09.009; RG Care4Rare Canada Consortium; RA Srour M., Hamdan F.F., McKnight D., Davis E., Mandel H., RA Schwartzentruber J., Martin B., Patry L., Nassif C., Dionne-Laporte A., RA Ospina L.H., Lemyre E., Massicotte C., Laframboise R., Maranda B., RA Labuda D., Decarie J.C., Rypens F., Goldsher D., Fallet-Bianco C., RA Soucy J.F., Laberge A.M., Maftei C., Boycott K., Brais B., Boucher R.M., RA Rouleau G.A., Katsanis N., Majewski J., Elpeleg O., Kukolich M.K., RA Shalev S., Michaud J.L.; RT "Joubert Syndrome in French Canadians and Identification of Mutations in RT CEP104."; RL Am. J. Hum. Genet. 97:744-753(2015). RN [19] RP VARIANT ASP-114, VARIANTS FMDMF GLU-123; SER-514; TRP-611; LEU-1164 AND RP SER-1400, AND INVOLVEMENT IN FMDMF. RX PubMed=32938213; DOI=10.1161/atvbaha.119.313885; RA Richer J., Hill H.L., Wang Y., Yang M.L., Hunker K.L., Lane J., RA Blackburn S., Coleman D.M., Eliason J., Sillon G., D'Agostino M.D., RA Jetty P., Mongeon F.P., Laberge A.M., Ryan S.E., Fendrikova-Mahlay N., RA Coutinho T., Mathis M.R., Zawistowski M., Hazen S.L., Katz A.E., RA Gornik H.L., Brummett C.M., Abecasis G., Bergin I.L., Stanley J.C., RA Li J.Z., Ganesh S.K.; RT "A novel recurrent COL5A1 genetic variant is associated with a dysplasia- RT associated arterial disease exhibiting dissections and fibromuscular RT dysplasia."; RL Arterioscler. Thromb. Vasc. Biol. 40:2686-2699(2020). CC -!- FUNCTION: Type V collagen is a member of group I collagen (fibrillar CC forming collagen). It is a minor connective tissue component of nearly CC ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, CC thrombospondin, heparin, and insulin. CC -!- SUBUNIT: Trimers of two alpha 1(V) and one alpha 2(V) chains in most CC tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha CC 3(V) chains in placenta. Interacts with CSPG4. CC {ECO:0000269|PubMed:9099729}. CC -!- INTERACTION: CC P20908; P13497: BMP1; NbExp=2; IntAct=EBI-2464511, EBI-489827; CC P20908; P02751-1: FN1; NbExp=2; IntAct=EBI-2464511, EBI-22099195; CC P20908; P08253: MMP2; NbExp=3; IntAct=EBI-2464511, EBI-1033518; CC P20908; Q15113: PCOLCE; NbExp=2; IntAct=EBI-2464511, EBI-8869614; CC P20908; P01033: TIMP1; NbExp=2; IntAct=EBI-2464511, EBI-712536; CC P20908; P24821: TNC; NbExp=2; IntAct=EBI-2464511, EBI-9979894; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=A {ECO:0000303|PubMed:22149965}; CC IsoId=P20908-1; Sequence=Displayed; CC Name=2; Synonyms=B {ECO:0000303|PubMed:22149965}; CC IsoId=P20908-2; Sequence=VSP_059655; CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have CC crucial roles in tissue growth and repair by controlling both the CC intracellular assembly of procollagen molecules and the extracellular CC assembly of collagen fibrils. It binds a calcium ion which is essential CC for its function (By similarity). {ECO:0000250}. CC -!- PTM: Prolines at the third position of the tripeptide repeating unit CC (G-X-Y) are hydroxylated in some or all of the chains. CC {ECO:0000269|PubMed:2496661}. CC -!- PTM: Sulfated on 40% of tyrosines. CC -!- DISEASE: Ehlers-Danlos syndrome, classic type, 1 (EDSCL1) [MIM:130000]: CC A form of Ehlers-Danlos syndrome, a group of connective tissue CC disorders characterized by skin hyperextensibility, articular CC hypermobility, and tissue fragility. The main features of classic CC Ehlers-Danlos syndrome are joint hypermobility and dislocation, and CC fragile, bruisable skin. EDSCL1 inheritance is autosomal dominant. CC {ECO:0000269|PubMed:10602121, ECO:0000269|PubMed:11992482, CC ECO:0000269|PubMed:15580559, ECO:0000269|PubMed:18972565, CC ECO:0000269|PubMed:9042913}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Fibromuscular dysplasia, multifocal (FMDMF) [MIM:619329]: An CC autosomal dominant vascular disorder with incomplete penetrance, CC characterized by fibrous tissue and webs developing in the artery wall CC and leading to multiple arterial stenoses. Patients with multifocal CC fibromuscular dysplasia can develop arterial tortuosity, CC macroaneurysms, and dissections. Arterial rupture may occur. CC {ECO:0000269|PubMed:32938213}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the fibrillar collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00793}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D90279; BAA14323.1; -; mRNA. DR EMBL; M76729; AAA59993.1; -; mRNA. DR EMBL; AL591890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL645768; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL603650; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS6982.1; -. [P20908-1] DR CCDS; CCDS75932.1; -. [P20908-2] DR PIR; S18802; CGHU1V. DR RefSeq; NP_000084.3; NM_000093.4. [P20908-1] DR PDB; 7Y37; X-ray; 1.45 A; A/B/C=1052-1087. DR PDBsum; 7Y37; -. DR AlphaFoldDB; P20908; -. DR SMR; P20908; -. DR BioGRID; 107686; 44. DR ComplexPortal; CPX-1727; Collagen type V trimer variant 1. DR ComplexPortal; CPX-1728; Collagen type V trimer variant 2. DR ComplexPortal; CPX-1729; Collagen type V trimer variant 3. DR ComplexPortal; CPX-1752; Collagen type XI trimer variant 3. DR IntAct; P20908; 34. DR STRING; 9606.ENSP00000360882; -. DR ChEMBL; CHEMBL2364188; -. DR GlyConnect; 1128; 10 N-Linked glycans (3 sites). DR GlyCosmos; P20908; 9 sites, 12 glycans. DR GlyGen; P20908; 11 sites, 9 N-linked glycans (3 sites), 4 O-linked glycans (8 sites). DR iPTMnet; P20908; -. DR PhosphoSitePlus; P20908; -. DR BioMuta; COL5A1; -. DR DMDM; 85687376; -. DR EPD; P20908; -. DR jPOST; P20908; -. DR MassIVE; P20908; -. DR MaxQB; P20908; -. DR PaxDb; 9606-ENSP00000360882; -. DR PeptideAtlas; P20908; -. DR ProteomicsDB; 53822; -. DR Pumba; P20908; -. DR Antibodypedia; 3446; 491 antibodies from 37 providers. DR DNASU; 1289; -. DR Ensembl; ENST00000371817.8; ENSP00000360882.3; ENSG00000130635.17. [P20908-1] DR Ensembl; ENST00000371820.4; ENSP00000360885.4; ENSG00000130635.17. [P20908-2] DR GeneID; 1289; -. DR KEGG; hsa:1289; -. DR MANE-Select; ENST00000371817.8; ENSP00000360882.3; NM_000093.5; NP_000084.3. DR UCSC; uc004cfe.5; human. [P20908-1] DR AGR; HGNC:2209; -. DR CTD; 1289; -. DR DisGeNET; 1289; -. DR GeneCards; COL5A1; -. DR GeneReviews; COL5A1; -. DR HGNC; HGNC:2209; COL5A1. DR HPA; ENSG00000130635; Tissue enhanced (cervix). DR MalaCards; COL5A1; -. DR MIM; 120215; gene. DR MIM; 130000; phenotype. DR MIM; 619329; phenotype. DR neXtProt; NX_P20908; -. DR OpenTargets; ENSG00000130635; -. DR Orphanet; 287; Classical Ehlers-Danlos syndrome. DR PharmGKB; PA26724; -. DR VEuPathDB; HostDB:ENSG00000130635; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000159211; -. DR HOGENOM; CLU_001074_2_1_1; -. DR InParanoid; P20908; -. DR OMA; TQGFQGK; -. DR OrthoDB; 2970887at2759; -. DR PhylomeDB; P20908; -. DR TreeFam; TF323987; -. DR PathwayCommons; P20908; -. DR Reactome; R-HSA-1442490; Collagen degradation. DR Reactome; R-HSA-1474244; Extracellular matrix organization. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-186797; Signaling by PDGF. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-3000170; Syndecan interactions. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-419037; NCAM1 interactions. DR Reactome; R-HSA-8874081; MET activates PTK2 signaling. DR Reactome; R-HSA-8948216; Collagen chain trimerization. DR SignaLink; P20908; -. DR SIGNOR; P20908; -. DR BioGRID-ORCS; 1289; 33 hits in 1150 CRISPR screens. DR ChiTaRS; COL5A1; human. DR GeneWiki; Collagen,_type_V,_alpha_1; -. DR GenomeRNAi; 1289; -. DR Pharos; P20908; Tbio. DR PRO; PR:P20908; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P20908; Protein. DR Bgee; ENSG00000130635; Expressed in stromal cell of endometrium and 177 other cell types or tissues. DR ExpressionAtlas; P20908; baseline and differential. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. DR GO; GO:0005588; C:collagen type V trimer; IMP:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IMP:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL. DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB. DR GO; GO:0005178; F:integrin binding; NAS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI. DR GO; GO:0043394; F:proteoglycan binding; IPI:UniProtKB. DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IMP:UniProtKB. DR GO; GO:0016477; P:cell migration; IMP:UniProtKB. DR GO; GO:0032964; P:collagen biosynthetic process; IMP:UniProtKB. DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB. DR GO; GO:0048592; P:eye morphogenesis; IMP:UniProtKB. DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl. DR GO; GO:0045112; P:integrin biosynthetic process; IMP:UniProtKB. DR GO; GO:1903225; P:negative regulation of endodermal cell differentiation; IDA:UniProtKB. DR GO; GO:0051128; P:regulation of cellular component organization; IEA:Ensembl. DR GO; GO:0043588; P:skin development; IMP:UniProtKB. DR GO; GO:0097435; P:supramolecular fiber organization; IMP:UniProtKB. DR GO; GO:0035989; P:tendon development; IEA:Ensembl. DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IMP:UniProtKB. DR Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR048287; TSPN-like_N. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF387; COLLAGEN ALPHA-1(V) CHAIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 4. DR Pfam; PF02210; Laminin_G_2; 1. DR SMART; SM00038; COLFI; 1. DR SMART; SM00282; LamG; 1. DR SMART; SM00210; TSPN; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS51461; NC1_FIB; 1. DR Genevisible; P20908; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Collagen; KW Direct protein sequencing; Disease variant; Disulfide bond; KW Ehlers-Danlos syndrome; Extracellular matrix; Heparin-binding; KW Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal; KW Sulfation. FT SIGNAL 1..37 FT /evidence="ECO:0000255" FT CHAIN 38..1605 FT /note="Collagen alpha-1(V) chain" FT /id="PRO_0000005756" FT PROPEP 1606..1838 FT /note="C-terminal propeptide" FT /id="PRO_0000005757" FT DOMAIN 72..244 FT /note="Laminin G-like" FT DOMAIN 1609..1837 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 231..443 FT /note="Nonhelical region" FT REGION 242..269 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 281..457 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 444..558 FT /note="Interrupted collagenous region" FT REGION 470..520 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 526..545 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 559..1574 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 559..1570 FT /note="Triple-helical region" FT REGION 1571..1605 FT /note="Nonhelical region" FT COMPBIAS 281..305 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..391 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 682..700 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 802..816 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 946..973 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1156..1170 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1321..1357 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1381..1396 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1454..1468 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1525..1540 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1556..1573 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1657 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1659 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1660 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1662 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1665 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT MOD_RES 234 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 236 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 240 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 262 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 263 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 338 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 340 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 346 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 347 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 416 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 417 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 420 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 421 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 570 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 576 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 621 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 627 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 639 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 642 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 648 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 654 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 657 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 675 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 678 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 687 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 690 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 696 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 705 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 708 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 717 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 720 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 726 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 732 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 744 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 750 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 756 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 762 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 765 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 771 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 774 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 780 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 789 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 795 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 804 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 807 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 810 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 816 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 819 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661" FT MOD_RES 834 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 846 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 861 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 864 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 870 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 873 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 876 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 882 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 888 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 891 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 897 FT /note="5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 903 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 906 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:2496661, FT ECO:0000269|PubMed:8181482" FT MOD_RES 930 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 945 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 1017 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 1020 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 1023 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 1029 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 1221 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 1224 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 1467 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 1470 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 1601 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT MOD_RES 1604 FT /note="Sulfotyrosine" FT /evidence="ECO:0000255" FT DISULFID 1639..1671 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1645 FT /note="Interchain (with C-1662)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1662 FT /note="Interchain (with C-1645)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1680..1835 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1746..1789 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT VAR_SEQ 1690..1711 FT /note="ARITSWPKENPGSWFSEFKRGK -> SKMARWPKEQPSTWYSQYKRGS (in FT isoform 2)" FT /id="VSP_059655" FT VARIANT 25 FT /note="L -> P (in EDSCL1; not or less efficiently secreted FT into the extracellular matrix)" FT /evidence="ECO:0000269|PubMed:18972565" FT /id="VAR_057902" FT VARIANT 25 FT /note="L -> R (in EDSCL1; not or less efficiently secreted FT into the extracellular matrix)" FT /evidence="ECO:0000269|PubMed:18972565" FT /id="VAR_057903" FT VARIANT 114 FT /note="A -> D (in dbSNP:rs147589613)" FT /evidence="ECO:0000269|PubMed:15580559, FT ECO:0000269|PubMed:32938213" FT /id="VAR_057904" FT VARIANT 123 FT /note="Q -> E (in FMDMF; uncertain significance; FT dbSNP:rs142114921)" FT /evidence="ECO:0000269|PubMed:32938213" FT /id="VAR_085830" FT VARIANT 192 FT /note="D -> N (in dbSNP:rs138579182)" FT /evidence="ECO:0000269|PubMed:15580559" FT /id="VAR_057905" FT VARIANT 229 FT /note="D -> N (risk factor for cervical artery dissection)" FT /evidence="ECO:0000269|PubMed:10471441" FT /id="VAR_057906" FT VARIANT 514 FT /note="G -> S (in FMDMF; dbSNP:rs878853652)" FT /evidence="ECO:0000269|PubMed:32938213" FT /id="VAR_085831" FT VARIANT 530 FT /note="G -> S (in EDSCL1; dbSNP:rs61735045)" FT /evidence="ECO:0000269|PubMed:10602121, FT ECO:0000269|PubMed:11992482, ECO:0000269|PubMed:15580559" FT /id="VAR_015412" FT VARIANT 611 FT /note="R -> W (in FMDMF; uncertain significance)" FT /evidence="ECO:0000269|PubMed:32938213" FT /id="VAR_085832" FT VARIANT 863 FT /note="E -> V (in dbSNP:rs139788610)" FT /evidence="ECO:0000269|PubMed:26477546" FT /id="VAR_075702" FT VARIANT 908 FT /note="P -> L (found in a renal cell carcinoma case; FT somatic mutation; dbSNP:rs772211736)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064702" FT VARIANT 951 FT /note="N -> S (in dbSNP:rs61736966)" FT /evidence="ECO:0000269|PubMed:15580559" FT /id="VAR_057908" FT VARIANT 1140 FT /note="V -> M (in dbSNP:rs149616140)" FT /evidence="ECO:0000269|PubMed:26477546" FT /id="VAR_075703" FT VARIANT 1164 FT /note="P -> L (in FMDMF; uncertain significance)" FT /evidence="ECO:0000269|PubMed:32938213" FT /id="VAR_085833" FT VARIANT 1400 FT /note="P -> S (in FMDMF; uncertain significance)" FT /evidence="ECO:0000269|PubMed:32938213" FT /id="VAR_085834" FT VARIANT 1486 FT /note="G -> C (in EDSCL1)" FT /evidence="ECO:0000269|PubMed:15580559" FT /id="VAR_057909" FT VARIANT 1489 FT /note="G -> D (in EDSCL1)" FT /evidence="ECO:0000269|PubMed:10602121" FT /id="VAR_015413" FT VARIANT 1639 FT /note="C -> S (in EDSCL1; dbSNP:rs80338764)" FT /evidence="ECO:0000269|PubMed:9042913" FT /id="VAR_001808" FT CONFLICT 82..83 FT /note="QL -> HV (in Ref. 2; AAA59993)" FT /evidence="ECO:0000305" FT CONFLICT 390 FT /note="A -> R (in Ref. 2; AAA59993)" FT /evidence="ECO:0000305" FT CONFLICT 641 FT /note="E -> G (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 650 FT /note="P -> L (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 663 FT /note="R -> E (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 668 FT /note="E -> Q (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 677 FT /note="E -> K (in Ref. 1; BAA14323)" FT /evidence="ECO:0000305" FT CONFLICT 677 FT /note="E -> Q (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 684 FT /note="L -> P (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 692..699 FT /note="PPGPPGVT -> VTGEPGAP (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 727 FT /note="G -> Q (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 741 FT /note="P -> L (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 747 FT /note="L -> Q (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 753 FT /note="P -> A (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 759 FT /note="D -> N (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 776..777 FT /note="GQ -> QK (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 849..855 FT /note="GGPNGDP -> IGPPGPR (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 894 FT /note="N -> D (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1295..1299 FT /note="LPGEG -> PSGRS (in Ref. 1; BAA14323)" FT /evidence="ECO:0000305" FT CONFLICT 1554 FT /note="K -> R (in Ref. 1; BAA14323)" FT /evidence="ECO:0000305" FT CONFLICT 1813 FT /note="V -> A (in Ref. 2; AAA59993)" FT /evidence="ECO:0000305" SQ SEQUENCE 1838 AA; 183560 MW; 8F18AB0B91B3A0C7 CRC64; MDVHTRWKAR SALRPGAPLL PPLLLLLLWA PPPSRAAQPA DLLKVLDFHN LPDGITKTTG FCATRRSSKG PDVAYRVTKD AQLSAPTKQL YPASAFPEDF SILTTVKAKK GSQAFLVSIY NEQGIQQIGL ELGRSPVFLY EDHTGKPGPE DYPLFRGINL SDGKWHRIAL SVHKKNVTLI LDCKKKTTKF LDRSDHPMID INGIIVFGTR ILDEEVFEGD IQQLLFVSDH RAAYDYCEHY SPDCDTAVPD TPQSQDPNPD EYYTEGDGEG ETYYYEYPYY EDPEDLGKEP TPSKKPVEAA KETTEVPEEL TPTPTEAAPM PETSEGAGKE EDVGIGDYDY VPSEDYYTPS PYDDLTYGEG EENPDQPTDP GAGAEIPTST ADTSNSSNPA PPPGEGADDL EGEFTEETIR NLDENYYDPY YDPTSSPSEI GPGMPANQDT IYEGIGGPRG EKGQKGEPAI IEPGMLIEGP PGPEGPAGLP GPPGTMGPTG QVGDPGERGP PGRPGLPGAD GLPGPPGTML MLPFRFGGGG DAGSKGPMVS AQESQAQAIL QQARLALRGP AGPMGLTGRP GPVGPPGSGG LKGEPGDVGP QGPRGVQGPP GPAGKPGRRG RAGSDGARGM PGQTGPKGDR GFDGLAGLPG EKGHRGDPGP SGPPGPPGDD GERGDDGEVG PRGLPGEPGP RGLLGPKGPP GPPGPPGVTG MDGQPGPKGN VGPQGEPGPP GQQGNPGAQG LPGPQGAIGP PGEKGPLGKP GLPGMPGADG PPGHPGKEGP PGEKGGQGPP GPQGPIGYPG PRGVKGADGI RGLKGTKGEK GEDGFPGFKG DMGIKGDRGE IGPPGPRGED GPEGPKGRGG PNGDPGPLGP PGEKGKLGVP GLPGYPGRQG PKGSIGFPGF PGANGEKGGR GTPGKPGPRG QRGPTGPRGE RGPRGITGKP GPKGNSGGDG PAGPPGERGP NGPQGPTGFP GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPPGVVG PQGPTGETGP MGERGHPGPP GPPGEQGLPG LAGKEGTKGD PGPAGLPGKD GPPGLRGFPG DRGLPGPVGA LGLKGNEGPP GPPGPAGSPG ERGPAGAAGP IGIPGRPGPQ GPPGPAGEKG APGEKGPQGP AGRDGLQGPV GLPGPAGPVG PPGEDGDKGE IGEPGQKGSK GDKGEQGPPG PTGPQGPIGQ PGPSGADGEP GPRGQQGLFG QKGDEGPRGF PGPPGPVGLQ GLPGPPGEKG ETGDVGQMGP PGPPGPRGPS GAPGADGPQG PPGGIGNPGA VGEKGEPGEA GEPGLPGEGG PPGPKGERGE KGESGPSGAA GPPGPKGPPG DDGPKGSPGP VGFPGDPGPP GEPGPAGQDG PPGDKGDDGE PGQTGSPGPT GEPGPSGPPG KRGPPGPAGP EGRQGEKGAK GEAGLEGPPG KTGPIGPQGA PGKPGPDGLR GIPGPVGEQG LPGSPGPDGP PGPMGPPGLP GLKGDSGPKG EKGHPGLIGL IGPPGEQGEK GDRGLPGPQG SSGPKGEQGI TGPSGPIGPP GPPGLPGPPG PKGAKGSSGP TGPKGEAGHP GPPGPPGPPG EVIQPLPIQA SRTRRNIDAS QLLDDGNGEN YVDYADGMEE IFGSLNSLKL EIEQMKRPLG TQQNPARTCK DLQLCHPDFP DGEYWVDPNQ GCSRDSFKVY CNFTAGGSTC VFPDKKSEGA RITSWPKENP GSWFSEFKRG KLLSYVDAEG NPVGVVQMTF LRLLSASAHQ NVTYHCYQSV AWQDAATGSY DKALRFLGSN DEEMSYDNNP YIRALVDGCA TKKGYQKTVL EIDTPKVEQV PIVDIMFNDF GEASQKFGFE VGPACFMG //