ID CO5A2_HUMAN Reviewed; 1499 AA. AC P05997; P78440; Q13908; Q53WR4; Q59GR4; Q6LDJ5; Q7KZ55; Q86XF6; Q96QB0; AC Q96QB3; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 3. DT 02-OCT-2024, entry version 237. DE RecName: Full=Collagen alpha-2(V) chain; DE Flags: Precursor; GN Name=COL5A2; 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]. RA Richards A.J.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-463. RX PubMed=2914927; DOI=10.1016/s0021-9258(19)81674-5; RA Woodbury D., Benson-Chanda V., Ramirez F.; RT "Amino-terminal propeptide of human pro-alpha 2(V) collagen conforms to the RT structural criteria of a fibrillar procollagen molecule."; RL J. Biol. Chem. 264:2735-2738(1989). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104 AND 153-1499. RX PubMed=11566270; DOI=10.1016/s0945-053x(01)00145-7; RA Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G., RA Ala-Kokko L.; RT "Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has RT evolved differently than the other minor fibrillar collagen genes."; RL Matrix Biol. 20:357-366(2001). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32. RX PubMed=1820205; RA Greenspan D.S., Lee S.T., Lee B.S., Hoffman G.G.; RT "Homology between alpha 2(V) and alpha 1(III) collagen promoters and RT evidence for negatively acting elements in the alpha 2(V) first intron and RT 5' flanking sequences."; RL Gene Expr. 1:29-39(1991). RN [7] RP PROTEIN SEQUENCE OF 208-227. 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 [8] RP PROTEIN SEQUENCE OF 288-297 AND 609-620, AND HYDROXYLATION AT PRO-290; RP PRO-293; PRO-296; PRO-611 AND PRO-617. RC TISSUE=Bone; 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 398-1499. RX PubMed=3029669; DOI=10.1093/nar/15.1.181; RA Weil D., Bernard M.P., Gargano S., Ramirez F.; RT "The pro alpha 2(V) collagen gene is evolutionarily related to the major RT fibrillar-forming collagens."; RL Nucleic Acids Res. 15:181-198(1987). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 878-1499. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1229, AND PROTEIN SEQUENCE OF 1006-1036. RX PubMed=2985598; DOI=10.1016/s0021-9258(18)89055-x; RA Myers J.C., Loidl H.R., Stolle C.A., Seyer J.M.; RT "Partial covalent structure of the human alpha 2 type V collagen chain."; RL J. Biol. Chem. 260:5533-5541(1985). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1006-1037. RX PubMed=3858826; DOI=10.1073/pnas.82.10.3385; RA Emanuel B.S., Cannizzaro L.A., Seyer J.M., Myers J.C.; RT "Human alpha 1(III) and alpha 2(V) procollagen genes are located on the RT long arm of chromosome 2."; RL Proc. Natl. Acad. Sci. U.S.A. 82:3385-3389(1985). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1230-1499. RX PubMed=2411731; DOI=10.1016/s0021-9258(17)39168-8; RA Myers J.C., Loidl H.R., Seyer J.M., Dion A.S.; RT "Complete primary structure of the human alpha 2 type V procollagen COOH- RT terminal propeptide."; RL J. Biol. Chem. 260:11216-11222(1985). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1452-1499. RX PubMed=3224983; DOI=10.1016/0888-7543(88)90089-4; RA Tsipouras P., Schwartz R.C., Liddell A.C., Salkeld C.S., Weil D., RA Ramirez F.; RT "Genetic distance of two fibrillar collagen loci, COL3A1 and COL5A2, RT located on the long arm of human chromosome 2."; RL Genomics 3:275-277(1988). RN [15] RP INVOLVEMENT IN EDSCL2. RX PubMed=9425231; DOI=10.1093/hmg/7.2.249; RA Michalickova K., Susic M., Willing M.C., Wenstrup R.J., Cole W.G.; RT "Mutations of the alpha2(V) chain of type V collagen impair matrix assembly RT and produce Ehlers-Danlos syndrome type I."; RL Hum. Mol. Genet. 7:249-255(1998). RN [16] RP HYDROXYLATION AT PRO-919 AND PRO-1156, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=21757687; DOI=10.1074/jbc.m111.267906; RA Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.; RT "A role for prolyl 3-hydroxylase 2 in post-translational modification of RT fibril-forming collagens."; RL J. Biol. Chem. 286:30662-30669(2011). RN [17] RP VARIANT EDSCL2 ARG-963. RX PubMed=9783710; DOI=10.1136/jmg.35.10.846; RA Richards A.J., Martin S., Nicholls A.C., Harrison J.B., Pope F.M., RA Burrows N.P.; RT "A single base mutation in COL5A2 causes Ehlers-Danlos syndrome type II."; RL J. Med. Genet. 35:846-848(1998). RN [18] RP VARIANTS ALA-512; LEU-833; SER-1230 AND VAL-1432. RX PubMed=11940702; DOI=10.1212/wnl.58.7.1103; RA Grond-Ginsbach C., Wigger F., Morcher M., von Pein F., Grau A., Hausser I., RA Brandt T.; RT "Sequence analysis of the COL5A2 gene in patients with spontaneous cervical RT artery dissections."; RL Neurology 58:1103-1105(2002). RN [19] RP VARIANT EDSCL2 ARG-228. RX PubMed=27656288; DOI=10.1038/hgv.2016.30; RA Watanabe M., Nakagawa R., Naruto T., Kohmoto T., Suga K., Goji A., RA Kagami S., Masuda K., Imoto I.; RT "A novel missense mutation of COL5A2 in a patient with Ehlers-Danlos RT syndrome."; RL Hum. Genome Var. 3:16030-16030(2016). 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. Type V collagen is a key CC determinant in the assembly of tissue-specific matrices (By CC similarity). {ECO:0000250}. 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. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. 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-P) are hydroxylated in some or all of the chains. Probably 3- CC hydroxylated on Pro-919 and Pro-1156 by LEPREL1. CC {ECO:0000269|PubMed:21757687, ECO:0000269|PubMed:8181482}. CC -!- DISEASE: Ehlers-Danlos syndrome, classic type, 2 (EDSCL2) [MIM:130010]: 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. EDSCL2 inheritance is autosomal dominant. CC {ECO:0000269|PubMed:27656288, ECO:0000269|PubMed:9425231, CC ECO:0000269|PubMed:9783710}. 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 -!- SEQUENCE CAUTION: CC Sequence=AAH43613.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAY24185.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BAD92282.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; Y14690; CAA75002.1; -; mRNA. DR EMBL; AB209045; BAD92282.1; ALT_INIT; mRNA. DR EMBL; AC064833; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC133106; AAY24185.1; ALT_SEQ; Genomic_DNA. DR EMBL; J04478; AAA51859.1; -; mRNA. DR EMBL; AY016288; AAL13165.1; -; Genomic_DNA. DR EMBL; AY016287; AAL13165.1; JOINED; Genomic_DNA. DR EMBL; AY016295; AAL13166.1; -; Genomic_DNA. DR EMBL; AY016289; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; AY016290; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; AY016291; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; AY016292; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; AY016293; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; AY016294; AAL13166.1; JOINED; Genomic_DNA. DR EMBL; M58529; AAC41699.1; -; Genomic_DNA. DR EMBL; X04758; CAA28454.1; -; mRNA. DR EMBL; BC043613; AAH43613.1; ALT_INIT; mRNA. DR EMBL; M10956; AAA52007.1; -; mRNA. DR EMBL; M11135; AAA51857.1; -; mRNA. DR EMBL; M11718; AAA52058.1; -; mRNA. DR EMBL; J03051; AAA51858.1; -; Genomic_DNA. DR CCDS; CCDS33350.1; -. DR PIR; A31427; CGHU2V. DR RefSeq; NP_000384.2; NM_000393.4. DR AlphaFoldDB; P05997; -. DR SMR; P05997; -. DR BioGRID; 107687; 15. DR ComplexPortal; CPX-1727; Collagen type V trimer variant 1. DR ComplexPortal; CPX-1728; Collagen type V trimer variant 2. DR ComplexPortal; CPX-1751; Collagen type XI trimer variant 2. DR ComplexPortal; CPX-1752; Collagen type XI trimer variant 3. DR IntAct; P05997; 5. DR STRING; 9606.ENSP00000364000; -. DR ChEMBL; CHEMBL2364188; -. DR GlyConnect; 1136; 6 N-Linked glycans (2 sites). DR GlyCosmos; P05997; 3 sites, 7 glycans. DR GlyGen; P05997; 5 sites, 6 N-linked glycans (2 sites), 2 O-linked glycans (3 sites). DR iPTMnet; P05997; -. DR PhosphoSitePlus; P05997; -. DR BioMuta; COL5A2; -. DR DMDM; 143811378; -. DR jPOST; P05997; -. DR MassIVE; P05997; -. DR PaxDb; 9606-ENSP00000364000; -. DR PeptideAtlas; P05997; -. DR ProteomicsDB; 51866; -. DR Antibodypedia; 34019; 194 antibodies from 28 providers. DR DNASU; 1290; -. DR Ensembl; ENST00000374866.9; ENSP00000364000.3; ENSG00000204262.14. DR GeneID; 1290; -. DR KEGG; hsa:1290; -. DR MANE-Select; ENST00000374866.9; ENSP00000364000.3; NM_000393.5; NP_000384.2. DR UCSC; uc002uqk.4; human. DR AGR; HGNC:2210; -. DR CTD; 1290; -. DR DisGeNET; 1290; -. DR GeneCards; COL5A2; -. DR GeneReviews; COL5A2; -. DR HGNC; HGNC:2210; COL5A2. DR HPA; ENSG00000204262; Low tissue specificity. DR MalaCards; COL5A2; -. DR MIM; 120190; gene. DR MIM; 130010; phenotype. DR neXtProt; NX_P05997; -. DR OpenTargets; ENSG00000204262; -. DR Orphanet; 287; Classical Ehlers-Danlos syndrome. DR PharmGKB; PA26725; -. DR VEuPathDB; HostDB:ENSG00000204262; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000155675; -. DR InParanoid; P05997; -. DR OMA; CESPQVP; -. DR OrthoDB; 2970887at2759; -. DR PhylomeDB; P05997; -. DR TreeFam; TF344135; -. DR PathwayCommons; P05997; -. 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; P05997; -. DR SIGNOR; P05997; -. DR BioGRID-ORCS; 1290; 10 hits in 1146 CRISPR screens. DR ChiTaRS; COL5A2; human. DR GeneWiki; COL5A2; -. DR GenomeRNAi; 1290; -. DR Pharos; P05997; Tbio. DR PRO; PR:P05997; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P05997; protein. DR Bgee; ENSG00000204262; Expressed in tendon of biceps brachii and 202 other cell types or tissues. DR ExpressionAtlas; P05997; baseline and differential. DR GO; GO:0005588; C:collagen type V trimer; IMP:UniProtKB. DR GO; GO:0005592; C:collagen type XI trimer; NAS:ComplexPortal. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0048592; P:eye morphogenesis; IMP:UniProtKB. DR GO; GO:1903225; P:negative regulation of endodermal cell differentiation; IDA:UniProtKB. DR GO; GO:0001503; P:ossification; IEA:Ensembl. DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl. DR GO; GO:0043588; P:skin development; IMP:UniProtKB. DR Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 6.20.200.20; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR050149; Collagen_superfamily. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 6. DR Pfam; PF00093; VWC; 1. DR SMART; SM00038; COLFI; 1. DR SMART; SM00214; VWC; 1. DR SUPFAM; SSF57603; FnI-like domain; 1. DR PROSITE; PS51461; NC1_FIB; 1. DR PROSITE; PS01208; VWFC_1; 1. DR PROSITE; PS50184; VWFC_2; 1. PE 1: Evidence at protein level; KW Calcium; Collagen; Direct protein sequencing; Disease variant; KW Disulfide bond; Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; KW Hydroxylation; Metal-binding; Proteomics identification; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..26 FT CHAIN 27..1229 FT /note="Collagen alpha-2(V) chain" FT /id="PRO_0000005830" FT PROPEP 1230..1499 FT /note="C-terminal propeptide" FT /id="PRO_0000005831" FT DOMAIN 39..97 FT /note="VWFC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 1266..1499 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 104..1268 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 506..508 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 944..946 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1067..1069 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1070..1072 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1100..1102 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1127..1129 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1136..1138 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 168..183 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 675..689 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 921..935 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1030..1044 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1128..1143 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1171..1185 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1212..1227 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1314 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1316 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1317 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 1322 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT MOD_RES 290 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 293 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 296 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 611 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 617 FT /note="Hydroxyproline" FT /evidence="ECO:0000269|PubMed:8181482" FT MOD_RES 919 FT /note="3-hydroxyproline; partial" FT /evidence="ECO:0000269|PubMed:21757687" FT MOD_RES 1156 FT /note="3-hydroxyproline; partial" FT /evidence="ECO:0000269|PubMed:21757687" FT CARBOHYD 1262 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1400 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 1296..1328 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1336..1497 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1405..1450 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT VARIANT 228 FT /note="G -> R (in EDSCL2; dbSNP:rs2105652981)" FT /evidence="ECO:0000269|PubMed:27656288" FT /id="VAR_078424" FT VARIANT 460 FT /note="P -> S (in dbSNP:rs35830636)" FT /id="VAR_048799" FT VARIANT 512 FT /note="V -> A (in dbSNP:rs35852101)" FT /evidence="ECO:0000269|PubMed:11940702" FT /id="VAR_057910" FT VARIANT 833 FT /note="P -> L (in dbSNP:rs116298748)" FT /evidence="ECO:0000269|PubMed:11940702" FT /id="VAR_057911" FT VARIANT 956 FT /note="R -> P (in dbSNP:rs6434313)" FT /id="VAR_048800" FT VARIANT 963 FT /note="G -> R (in EDSCL2; dbSNP:rs1186550791)" FT /evidence="ECO:0000269|PubMed:9783710" FT /id="VAR_013588" FT VARIANT 1230 FT /note="T -> S (in dbSNP:rs767234623)" FT /evidence="ECO:0000269|PubMed:11940702" FT /id="VAR_057912" FT VARIANT 1432 FT /note="D -> V (in dbSNP:rs141777954)" FT /evidence="ECO:0000269|PubMed:11940702" FT /id="VAR_057913" FT CONFLICT 292 FT /note="A -> P (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 361 FT /note="M -> L (in Ref. 5; AAL13166)" FT /evidence="ECO:0000305" FT CONFLICT 430 FT /note="A -> P (in Ref. 1; CAA75002, 4; AAA51859 and 9; FT CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 463..466 FT /note="IRGQ -> NSGL (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 463 FT /note="I -> N (in Ref. 4; AAA51859)" FT /evidence="ECO:0000305" FT CONFLICT 472..474 FT /note="Missing (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 512 FT /note="V -> L (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 608 FT /note="R -> K (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 613 FT /note="S -> T (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 623 FT /note="S -> N (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 635 FT /note="A -> P (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 649 FT /note="E -> K (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 653 FT /note="S -> Y (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 656 FT /note="V -> P (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 662 FT /note="A -> R (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 679 FT /note="L -> H (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 700 FT /note="D -> G (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 797 FT /note="R -> G (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 811..812 FT /note="PT -> LL (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 853 FT /note="P -> S (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 943 FT /note="L -> P (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 955 FT /note="D -> V (in Ref. 1; CAA75002 and 9; CAA28454)" FT /evidence="ECO:0000305" FT CONFLICT 1111..1112 FT /note="PP -> HL (in Ref. 1; CAA75002, 9; CAA28454 and 11; FT AAA52007)" FT /evidence="ECO:0000305" FT CONFLICT 1196 FT /note="I -> L (in Ref. 1; CAA75002, 9; CAA28454 and 11; FT AAA52007)" FT /evidence="ECO:0000305" FT CONFLICT 1421 FT /note="K -> T (in Ref. 13; AAA52058)" FT /evidence="ECO:0000305" FT CONFLICT 1441 FT /note="F -> S (in Ref. 13; AAA52058)" FT /evidence="ECO:0000305" FT CONFLICT 1467 FT /note="Q -> E (in Ref. 14; AAA51858)" FT /evidence="ECO:0000305" SQ SEQUENCE 1499 AA; 144910 MW; E8C92BF5E749EC97 CRC64; MMANWAEARP LLILIVLLGQ FVSIKAQEED EDEGYGEEIA CTQNGQMYLN RDIWKPAPCQ ICVCDNGAIL CDKIECQDVL DCADPVTPPG ECCPVCSQTP GGGNTNFGRG RKGQKGEPGL VPVVTGIRGR PGPAGPPGSQ GPRGERGPKG RPGPRGPQGI DGEPGVPGQP GAPGPPGHPS HPGPDGLSRP FSAQMAGLDE KSGLGSQVGL MPGSVGPVGP RGPQGLQGQQ GGAGPTGPPG EPGDPGPMGP IGSRGPEGPP GKPGEDGEPG RNGNPGEVGF AGSPGARGFP GAPGLPGLKG HRGHKGLEGP KGEVGAPGSK GEAGPTGPMG AMGPLGPRGM PGERGRLGPQ GAPGQRGAHG MPGKPGPMGP LGIPGSSGFP GNPGMKGEAG PTGARGPEGP QGQRGETGPP GPVGSPGLPG AIGTDGTPGA KGPTGSPGTS GPPGSAGPPG SPGPQGSTGP QGIRGQPGDP GVPGFKGEAG PKGEPGPHGI QGPIGPPGEE GKRGPRGDPG TVGPPGPVGE RGAPGNRGFP GSDGLPGPKG AQGERGPVGS SGPKGSQGDP GRPGEPGLPG ARGLTGNPGV QGPEGKLGPL GAPGEDGRPG PPGSIGIRGQ PGSMGLPGPK GSSGDPGKPG EAGNAGVPGQ RGAPGKDGEV GPSGPVGPPG LAGERGEQGP PGPTGFQGLP GPPGPPGEGG KPGDQGVPGD PGAVGPLGPR GERGNPGERG EPGITGLPGE KGMAGGHGPD GPKGSPGPSG TPGDTGPPGL QGMPGERGIA GTPGPKGDRG GIGEKGAEGT AGNDGARGLP GPLGPPGPAG PTGEKGEPGP RGLVGPPGSR GNPGSRGENG PTGAVGFAGP QGPDGQPGVK GEPGEPGQKG DAGSPGPQGL AGSPGPHGPN GVPGLKGGRG TQGPPGATGF PGSAGRVGPP GPAGAPGPAG PLGEPGKEGP PGLRGDPGSH GRVGDRGPAG PPGGPGDKGD PGEDGQPGPD GPPGPAGTTG QRGIVGMPGQ RGERGMPGLP GPAGTPGKVG PTGATGDKGP PGPVGPPGSN GPVGEPGPEG PAGNDGTPGR DGAVGERGDR GDPGPAGLPG SQGAPGTPGP VGAPGDAGQR GDPGSRGPIG PPGRAGKRGL PGPQGPRGDK GDHGDRGDRG QKGHRGFTGL QGLPGPPGPN GEQGSAGIPG PFGPRGPPGP VGPSGKEGNP GPLGPIGPPG VRGSVGEAGP EGPPGEPGPP GPPGPPGHLT AALGDIMGHY DESMPDPLPE FTEDQAAPDD KNKTDPGVHA TLKSLSSQIE TMRSPDGSKK HPARTCDDLK LCHSAKQSGE YWIDPNQGSV EDAIKVYCNM ETGETCISAN PSSVPRKTWW ASKSPDNKPV WYGLDMNRGS QFAYGDHQSP NTAITQMTFL RLLSKEASQN ITYICKNSVG YMDDQAKNLK KAVVLKGAND LDIKAEGNIR FRYIVLQDTC SKRNGNVGKT VFEYRTQNVA RLPIIDLAPV DVGGTDQEFG VEIGPVCFV //