CO5A3_HUMAN
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 03-AUG-2022, entry version 194.
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).
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}.
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}.
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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; 3.
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 GlyGen; P25940; 6 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 EPD; P25940; -.
DR jPOST; P25940; -.
DR MassIVE; P25940; -.
DR MaxQB; P25940; -.
DR PaxDb; P25940; -.
DR PeptideAtlas; P25940; -.
DR PRIDE; P25940; -.
DR ProteomicsDB; 54301; -.
DR Antibodypedia; 25107; 123 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 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; PGHQGKD; -.
DR OrthoDB; 1018065at2759; -.
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 1062 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 165 other tissues.
DR Genevisible; P25940; HS.
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:0031012; C:extracellular matrix; IBA:GO_Central.
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; 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; IEA:Ensembl.
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 InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 2.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 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; 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 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
