ID CO5A3_HUMAN Reviewed; 1745 AA. AC P25940; Q9NZQ6; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2009, sequence version 3. DT 02-OCT-2024, entry version 206. DE RecName: Full=Collagen alpha-3(V) chain; DE Flags: Precursor; GN Name=COL5A3; 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], AND VARIANT GLY-322. RC TISSUE=Heart, and Placenta; RX PubMed=10722718; DOI=10.1074/jbc.275.12.8749; RA Imamura Y., Scott I.C., Greenspan D.S.; RT "The pro-alpha3 (V) collagen chain. Complete primary structure, expression RT domains in adult and developing tissues, and comparison to the structures RT and expression domains of the other types V and XI procollagen chains."; RL J. Biol. Chem. 275:8749-8759(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP PRELIMINARY PROTEIN SEQUENCE OF 479-564; 665-709; 723-758; 787-816; RP 922-1008; 1054-1088; 1248-1287 AND 1313-1334. 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 [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102 AND ASN-141. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [5] RP TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-349. RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3; RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K., RA Pandey A.; RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides."; RL J. Proteins Proteom. 13:187-203(2022). RN [6] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-349. RX PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617; RA Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.; RT "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected RT Correlation Between Glycan Sulfation and Attachment Site Characteristics."; RL Mol. Cell. Proteomics 22:100617-100617(2023). 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. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. Secreted CC {ECO:0000269|PubMed:37453717}. CC -!- TISSUE SPECIFICITY: Detected in fibroblasts (at protein level) CC (PubMed:36213313). Detected in urine (at protein level) CC (PubMed:37453717). {ECO:0000269|PubMed:36213313, CC ECO:0000269|PubMed:37453717}. 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 -!- 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; AF177941; AAF59902.1; -; mRNA. DR EMBL; AC008742; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS12222.1; -. DR PIR; S20375; S20375. DR RefSeq; NP_056534.2; NM_015719.3. DR AlphaFoldDB; P25940; -. DR SMR; P25940; -. DR BioGRID; 119080; 7. DR ComplexPortal; CPX-1728; Collagen type V trimer variant 2. DR IntAct; P25940; 1. DR MINT; P25940; -. DR STRING; 9606.ENSP00000264828; -. DR ChEMBL; CHEMBL2364188; -. DR GlyConnect; 1138; 2 N-Linked glycans (1 site). DR GlyCosmos; P25940; 6 sites, 3 glycans. DR GlyGen; P25940; 7 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (4 sites). DR iPTMnet; P25940; -. DR PhosphoSitePlus; P25940; -. DR BioMuta; COL5A3; -. DR DMDM; 281185497; -. DR jPOST; P25940; -. DR MassIVE; P25940; -. DR PaxDb; 9606-ENSP00000264828; -. DR PeptideAtlas; P25940; -. DR ProteomicsDB; 54301; -. DR Antibodypedia; 25107; 131 antibodies from 26 providers. DR DNASU; 50509; -. DR Ensembl; ENST00000264828.4; ENSP00000264828.3; ENSG00000080573.7. DR GeneID; 50509; -. DR KEGG; hsa:50509; -. DR MANE-Select; ENST00000264828.4; ENSP00000264828.3; NM_015719.4; NP_056534.2. DR UCSC; uc002mmq.1; human. DR AGR; HGNC:14864; -. DR CTD; 50509; -. DR DisGeNET; 50509; -. DR GeneCards; COL5A3; -. DR HGNC; HGNC:14864; COL5A3. DR HPA; ENSG00000080573; Low tissue specificity. DR MIM; 120216; gene. DR neXtProt; NX_P25940; -. DR OpenTargets; ENSG00000080573; -. DR PharmGKB; PA26726; -. DR VEuPathDB; HostDB:ENSG00000080573; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000162394; -. DR HOGENOM; CLU_001074_2_0_1; -. DR InParanoid; P25940; -. DR OMA; NHGSQGI; -. DR OrthoDB; 2970887at2759; -. DR PhylomeDB; P25940; -. DR TreeFam; TF323987; -. DR PathwayCommons; P25940; -. 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; P25940; -. DR BioGRID-ORCS; 50509; 13 hits in 1142 CRISPR screens. DR ChiTaRS; COL5A3; human. DR GeneWiki; COL5A3; -. DR GenomeRNAi; 50509; -. DR Pharos; P25940; Tbio. DR PRO; PR:P25940; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P25940; protein. DR Bgee; ENSG00000080573; Expressed in sural nerve and 167 other cell types or tissues. DR GO; GO:0005588; C:collagen type V trimer; NAS:UniProtKB. 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:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005518; F:collagen binding; NAS:UniProtKB. DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL. DR GO; GO:0008201; F:heparin binding; IBA:GO_Central. DR GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl. DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; NAS:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0043588; P:skin development; NAS:UniProtKB. DR Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR050149; Collagen_superfamily. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000885; Fib_collagen_C. DR InterPro; IPR048287; TSPN-like_N. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF1100; FIBRILLAR COLLAGEN NC1 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01410; COLFI; 1. DR Pfam; PF01391; Collagen; 2. DR SMART; SM00038; COLFI; 1. DR SMART; SM00210; TSPN; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS51461; NC1_FIB; 1. PE 1: Evidence at protein level; KW Collagen; Direct protein sequencing; Disulfide bond; Extracellular matrix; KW Glycoprotein; Hydroxylation; Proteoglycan; Proteomics identification; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..1745 FT /note="Collagen alpha-3(V) chain" FT /id="PRO_0000005845" FT DOMAIN 62..224 FT /note="Laminin G-like" FT DOMAIN 391..440 FT /note="Collagen-like 1" FT DOMAIN 482..538 FT /note="Collagen-like 2" FT DOMAIN 824..877 FT /note="Collagen-like 3" FT DOMAIN 905..950 FT /note="Collagen-like 4" FT DOMAIN 951..989 FT /note="Collagen-like 5" FT DOMAIN 1430..1488 FT /note="Collagen-like 6" FT DOMAIN 1514..1744 FT /note="Fibrillar collagen NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT REGION 211..391 FT /note="Nonhelical region" FT REGION 230..304 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 322..362 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 387..439 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 392..1489 FT /note="Triple-helical region" FT REGION 476..1492 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 246..266 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 272..292 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 336..352 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 398..427 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1052..1066 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1079..1093 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1316..1331 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1431..1448 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 102 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 141 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 349 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:36213313, FT ECO:0000269|PubMed:37453717" FT DISULFID 1544 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1567 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1576 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1585..1742 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT DISULFID 1651..1696 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793" FT VARIANT 134 FT /note="R -> H (in dbSNP:rs2303098)" FT /id="VAR_020015" FT VARIANT 322 FT /note="R -> G (in dbSNP:rs2287803)" FT /evidence="ECO:0000269|PubMed:10722718" FT /id="VAR_060789" FT VARIANT 1042 FT /note="R -> P (in dbSNP:rs2161468)" FT /id="VAR_055678" FT VARIANT 1207 FT /note="R -> P (in dbSNP:rs2287813)" FT /id="VAR_020016" FT VARIANT 1428 FT /note="V -> M (in dbSNP:rs3815746)" FT /id="VAR_020017" FT VARIANT 1488 FT /note="A -> P (in dbSNP:rs3745584)" FT /id="VAR_055679" FT VARIANT 1594 FT /note="I -> M (in dbSNP:rs3745581)" FT /id="VAR_020018" FT VARIANT 1691 FT /note="V -> I (in dbSNP:rs2277969)" FT /id="VAR_020019" FT CONFLICT 1687 FT /note="A -> T (in Ref. 1; AAF59902)" FT /evidence="ECO:0000305" SQ SEQUENCE 1745 AA; 172121 MW; 4F5644D2A919D864 CRC64; MGNRRDLGQP RAGLCLLLAA LQLLPGTQAD PVDVLKALGV QGGQAGVPEG PGFCPQRTPE GDRAFRIGQA STLGIPTWEL FPEGHFPENF SLLITLRGQP ANQSVLLSIY DERGARQLGL ALGPALGLLG DPFRPLPQQV NLTDGRWHRV AVSIDGEMVT LVADCEAQPP VLGHGPRFIS IAGLTVLGTQ DLGEKTFEGD IQELLISPDP QAAFQACERY LPDCDNLAPA ATVAPQGEPE TPRPRRKGKG KGRKKGRGRK GKGRKKNKEI WTSSPPPDSA ENQTSTDIPK TETPAPNLPP TPTPLVVTST VTTGLNATIL ERSLDPDSGT ELGTLETKAA REDEEGDDST MGPDFRAAEY PSRTQFQIFP GAGEKGAKGE PAVIEKGQQF EGPPGAPGPQ GVVGPSGPPG PPGFPGDPGP PGPAGLPGIP GIDGIRGPPG TVIMMPFQFA GGSFKGPPVS FQQAQAQAVL QQTQLSMKGP PGPVGLTGRP GPVGLPGHPG LKGEEGAEGP QGPRGLQGPH GPPGRVGKMG RPGADGARGL PGDTGPKGDR GFDGLPGLPG EKGQRGDFGH VGQPGPPGED GERGAEGPPG PTGQAGEPGP RGLLGPRGSP GPTGRPGVTG IDGAPGAKGN VGPPGEPGPP GQQGNHGSQG LPGPQGLIGT PGEKGPPGNP GIPGLPGSDG PLGHPGHEGP TGEKGAQGPP GSAGPPGYPG PRGVKGTSGN RGLQGEKGEK GEDGFPGFKG DVGLKGDQGK PGAPGPRGED GPEGPKGQAG QAGEEGPPGS AGEKGKLGVP GLPGYPGRPG PKGSIGFPGP LGPIGEKGKS GKTGQPGLEG ERGPPGSRGE RGQPGATGQP GPKGDVGQDG APGIPGEKGL PGLQGPPGFP GPKGPPGHQG KDGRPGHPGQ RGELGFQGQT GPPGPAGVLG PQGKTGEVGP LGERGPPGPP GPPGEQGLPG LEGREGAKGE LGPPGPLGKE GPAGLRGFPG PKGGPGDPGP TGLKGDKGPP GPVGANGSPG ERGPLGPAGG IGLPGQSGSE GPVGPAGKKG SRGERGPPGP TGKDGIPGPL GPLGPPGAAG PSGEEGDKGD VGAPGHKGSK GDKGDAGPPG QPGIRGPAGH PGPPGADGAQ GRRGPPGLFG QKGDDGVRGF VGVIGPPGLQ GLPGPPGEKG EVGDVGSMGP HGAPGPRGPQ GPTGSEGTPG LPGGVGQPGA VGEKGERGDA GDPGPPGAPG IPGPKGDIGE KGDSGPSGAA GPPGKKGPPG EDGAKGSVGP TGLPGDLGPP GDPGVSGIDG SPGEKGDPGD VGGPGPPGAS GEPGAPGPPG KRGPSGHMGR EGREGEKGAK GEPGPDGPPG RTGPMGARGP PGRVGPEGLR GIPGPVGEPG LLGAPGQMGP PGPLGPSGLP GLKGDTGPKG EKGHIGLIGL IGPPGEAGEK GDQGLPGVQG PPGPKGDPGP PGPIGSLGHP GPPGVAGPLG QKGSKGSPGS MGPRGDTGPA GPPGPPGAPA ELHGLRRRRR FVPVPLPVVE GGLEEVLASL TSLSLELEQL RRPPGTAERP GLVCHELHRN HPHLPDGEYW IDPNQGCARD SFRVFCNFTA GGETCLYPDK KFEIVKLASW SKEKPGGWYS TFRRGKKFSY VDADGSPVNV VQLNFLKLLS ATARQNFTYS CQNAAAWLDE ATGDYSHSAR FLGTNGEELS FNQTTAATVS VPQDGCRLRK GQTKTLFEFS SSRAGFLPLW DVAATDFGQT NQKFGFELGP VCFSS //