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   27-MAR-2024, entry version 203.
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}.
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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; 5.
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   EPD; P25940; -.
DR   jPOST; P25940; -.
DR   MassIVE; P25940; -.
DR   MaxQB; P25940; -.
DR   PaxDb; 9606-ENSP00000264828; -.
DR   PeptideAtlas; P25940; -.
DR   ProteomicsDB; 54301; -.
DR   Antibodypedia; 25107; 128 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; 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.
DR   Genevisible; P25940; HS.
PE   1: Evidence at protein level;
KW   Collagen; Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Hydroxylation; Proteoglycan; Reference proteome; Repeat;
KW   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
//