GenomeNet

Database: UniProt/SWISS-PROT
Entry: CO5A1_HUMAN
LinkDB: CO5A1_HUMAN
Original site: CO5A1_HUMAN 
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   16-OCT-2019, entry version 213.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF
RP   556-565 (ISOFORMS 1/2).
RX   PubMed=2071595;
RA   Takahara K., Seto Y., Okasawa K., Okamoto N., Noda A., Yaoi Y.,
RA   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;
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.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   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.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   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.,
RA   Rogers J., 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
RP   PRO-621; LYS-627; PRO-639; LYS-642; PRO-648; PRO-654; PRO-657;
RP   PRO-675; PRO-678; LYS-687; PRO-690; PRO-696; PRO-705; LYS-708;
RP   PRO-717; PRO-720; PRO-726; PRO-732; LYS-744; PRO-750; PRO-756;
RP   PRO-762; PRO-765; PRO-771; LYS-774; PRO-780; PRO-789; LYS-795;
RP   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;
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
RP   1465-1477 (ISOFORMS 1/2), AND HYDROXYLATION AT PRO-570; PRO-576;
RP   PRO-756; PRO-762; PRO-834; LYS-846; PRO-861; LYS-864; PRO-870;
RP   PRO-873; PRO-876; LYS-882; PRO-888; PRO-891; LYS-897; PRO-903;
RP   PRO-906; PRO-930; PRO-945; PRO-1017; PRO-1020; PRO-1023; PRO-1029;
RP   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
RT   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
RT   through 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.,
RA   Naeyaert J.-M.;
RT   "Mutations in the COL5A1 gene are causal in the Ehlers-Danlos
RT   syndromes I and II.";
RL   Am. J. Hum. Genet. 60:547-554(1997).
RN   [11]
RP   VARIANT ASN-229, AND ASSOCIATION WITH INCREASED RISK OF CERVICAL
RP   ARTERY 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
RT   with 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-
RT   modifying G530S substitution in COL5A1 of a patient with the classical
RT   type of Ehlers-Danlos syndrome: an explanation of intrafamilial
RT   variability?";
RL   Am. J. Med. Genet. 90:72-79(2000).
RN   [13]
RP   ERRATUM.
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
RT   Ehlers-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;
RP   SER-393 AND 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
RT   comprehensive study of biochemical and molecular findings in 48
RT   unrelated patients.";
RL   Hum. Mutat. 25:28-37(2005).
RN   [16]
RP   VARIANTS EDSCL1 ARG-25 AND PRO-25, AND CHARACTERIZATION OF VARIANTS
RP   EDSCL1 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
RT   cause 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.,
RA   Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA   Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA   Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA   Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA   Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA   Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA   Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA   Futreal P.A.;
RT   "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT   gene 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.,
RA   Dionne-Laporte A., Ospina L.H., Lemyre E., Massicotte C.,
RA   Laframboise R., Maranda B., Labuda D., Decarie J.C., Rypens F.,
RA   Goldsher D., Fallet-Bianco C., Soucy J.F., Laberge A.M., Maftei C.,
RA   Boycott K., Brais B., Boucher R.M., Rouleau G.A., Katsanis N.,
RA   Majewski J., Elpeleg O., Kukolich M.K., Shalev S., Michaud J.L.;
RT   "Joubert Syndrome in French Canadians and Identification of Mutations
RT   in CEP104.";
RL   Am. J. Hum. Genet. 97:744-753(2015).
CC   -!- FUNCTION: Type V collagen is a member of group I collagen
CC       (fibrillar forming collagen). It is a minor connective tissue
CC       component of nearly ubiquitous distribution. Type V collagen binds
CC       to DNA, heparan sulfate, thrombospondin, heparin, and insulin.
CC   -!- SUBUNIT: Trimers of two alpha 1(V) and one alpha 2(V) chains in
CC       most tissues and trimers of one alpha 1(V), one alpha 2(V), and
CC       one alpha 3(V) chains in placenta. Interacts with CSPG4.
CC       {ECO:0000269|PubMed:9099729}.
CC   -!- INTERACTION:
CC       P13497:BMP1; NbExp=2; IntAct=EBI-2464511, EBI-489827;
CC       P02751:FN1; NbExp=2; IntAct=EBI-2464511, EBI-1220319;
CC       P08253:MMP2; NbExp=3; IntAct=EBI-2464511, EBI-1033518;
CC       Q15113:PCOLCE; NbExp=2; IntAct=EBI-2464511, EBI-8869614;
CC       P01033:TIMP1; NbExp=2; IntAct=EBI-2464511, EBI-712536;
CC       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,
CC       have crucial roles in tissue growth and repair by controlling both
CC       the intracellular assembly of procollagen molecules and the
CC       extracellular assembly of collagen fibrils. It binds a calcium ion
CC       which is essential for its function (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating
CC       unit (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)
CC       [MIM:130000]: A form of Ehlers-Danlos syndrome, a group of
CC       connective tissue disorders characterized by skin
CC       hyperextensibility, articular hypermobility, and tissue fragility.
CC       The main features of classic Ehlers-Danlos syndrome are joint
CC       hypermobility and dislocation, and fragile, bruisable skin. EDSCL1
CC       inheritance is autosomal dominant. {ECO:0000269|PubMed:10602121,
CC       ECO:0000269|PubMed:11992482, ECO:0000269|PubMed:15580559,
CC       ECO:0000269|PubMed:18972565, ECO:0000269|PubMed:9042913}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00793}.
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; 1A89; Model; -; A/B/C=904-924.
DR   PDB; 1A9A; Model; -; A/C=904-924.
DR   PDBsum; 1A89; -.
DR   PDBsum; 1A9A; -.
DR   SMR; P20908; -.
DR   BioGrid; 107686; 27.
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; 31.
DR   STRING; 9606.ENSP00000360882; -.
DR   ChEMBL; CHEMBL2364188; -.
DR   GlyConnect; 1128; -.
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; P20908; -.
DR   PeptideAtlas; P20908; -.
DR   PRIDE; P20908; -.
DR   ProteomicsDB; 53822; -.
DR   Ensembl; ENST00000371817; ENSP00000360882; ENSG00000130635. [P20908-1]
DR   Ensembl; ENST00000618395; ENSP00000481360; ENSG00000130635. [P20908-2]
DR   GeneID; 1289; -.
DR   KEGG; hsa:1289; -.
DR   UCSC; uc004cfe.5; human. [P20908-1]
DR   CTD; 1289; -.
DR   DisGeNET; 1289; -.
DR   GeneCards; COL5A1; -.
DR   GeneReviews; COL5A1; -.
DR   HGNC; HGNC:2209; COL5A1.
DR   HPA; HPA030769; -.
DR   MalaCards; COL5A1; -.
DR   MIM; 120215; gene.
DR   MIM; 130000; phenotype.
DR   neXtProt; NX_P20908; -.
DR   OpenTargets; ENSG00000130635; -.
DR   Orphanet; 287; Classical Ehlers-Danlos syndrome.
DR   PharmGKB; PA26724; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   eggNOG; ENOG410XNMM; LUCA.
DR   GeneTree; ENSGT00940000159211; -.
DR   HOGENOM; HOG000085654; -.
DR   InParanoid; P20908; -.
DR   KO; K19721; -.
DR   OMA; DGQTGPK; -.
DR   OrthoDB; 199083at2759; -.
DR   PhylomeDB; P20908; -.
DR   TreeFam; TF323987; -.
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   SIGNOR; P20908; -.
DR   ChiTaRS; COL5A1; human.
DR   GeneWiki; Collagen,_type_V,_alpha_1; -.
DR   GenomeRNAi; 1289; -.
DR   Pharos; P20908; -.
DR   PMAP-CutDB; P20908; -.
DR   PRO; PR:P20908; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000130635; Expressed in 211 organ(s), highest expression level in tendon of biceps brachii.
DR   ExpressionAtlas; P20908; baseline and differential.
DR   Genevisible; P20908; HS.
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:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; 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:0030198; P:extracellular matrix organization; IBA:GO_Central.
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   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; 5.
DR   SMART; SM00038; COLFI; 1.
DR   SMART; SM00282; LamG; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Collagen;
KW   Complete proteome; Direct protein sequencing; Disease mutation;
KW   Disulfide bond; Ehlers-Danlos syndrome; Extracellular matrix;
KW   Heparin-binding; Hydroxylation; Metal-binding; Polymorphism;
KW   Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL        1     37       {ECO:0000255}.
FT   CHAIN        38   1605       Collagen alpha-1(V) chain.
FT                                /FTId=PRO_0000005756.
FT   PROPEP     1606   1838       C-terminal propeptide.
FT                                /FTId=PRO_0000005757.
FT   DOMAIN       72    244       Laminin G-like.
FT   DOMAIN     1609   1837       Fibrillar collagen NC1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00793}.
FT   REGION      231    443       Nonhelical region.
FT   REGION      444    558       Interrupted collagenous region.
FT   REGION      559   1570       Triple-helical region.
FT   REGION     1571   1605       Nonhelical region.
FT   METAL      1657   1657       Calcium. {ECO:0000250}.
FT   METAL      1659   1659       Calcium. {ECO:0000250}.
FT   METAL      1660   1660       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL      1662   1662       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL      1665   1665       Calcium. {ECO:0000250}.
FT   MOD_RES     234    234       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     236    236       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     240    240       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     262    262       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     263    263       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     338    338       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     340    340       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     346    346       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     347    347       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     416    416       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     417    417       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     420    420       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     421    421       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES     570    570       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES     576    576       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES     621    621       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     627    627       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     639    639       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     642    642       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     648    648       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     654    654       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     657    657       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     675    675       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     678    678       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     687    687       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     690    690       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     696    696       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     705    705       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     708    708       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     717    717       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     720    720       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     726    726       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     732    732       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     744    744       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     750    750       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     756    756       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     762    762       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     765    765       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     771    771       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     774    774       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     780    780       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     789    789       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     795    795       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     804    804       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     807    807       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     810    810       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     816    816       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     819    819       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661}.
FT   MOD_RES     834    834       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     846    846       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     861    861       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     864    864       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     870    870       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     873    873       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     876    876       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     882    882       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     888    888       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     891    891       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     897    897       5-hydroxylysine.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     903    903       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     906    906       Hydroxyproline.
FT                                {ECO:0000269|PubMed:2496661,
FT                                ECO:0000269|PubMed:8181482}.
FT   MOD_RES     930    930       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES     945    945       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES    1017   1017       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES    1020   1020       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES    1023   1023       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES    1029   1029       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES    1221   1221       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES    1224   1224       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES    1467   1467       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES    1470   1470       Hydroxyproline.
FT                                {ECO:0000269|PubMed:8181482}.
FT   MOD_RES    1601   1601       Sulfotyrosine. {ECO:0000255}.
FT   MOD_RES    1604   1604       Sulfotyrosine. {ECO:0000255}.
FT   DISULFID   1639   1671       {ECO:0000255|PROSITE-ProRule:PRU00793}.
FT   DISULFID   1645   1645       Interchain (with C-1662).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00793}.
FT   DISULFID   1662   1662       Interchain (with C-1645).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00793}.
FT   DISULFID   1680   1835       {ECO:0000255|PROSITE-ProRule:PRU00793}.
FT   DISULFID   1746   1789       {ECO:0000255|PROSITE-ProRule:PRU00793}.
FT   VAR_SEQ    1690   1711       ARITSWPKENPGSWFSEFKRGK -> SKMARWPKEQPSTWY
FT                                SQYKRGS (in isoform 2).
FT                                /FTId=VSP_059655.
FT   VARIANT      25     25       L -> P (in EDSCL1; not or less
FT                                efficiently secreted into the
FT                                extracellular matrix).
FT                                {ECO:0000269|PubMed:18972565}.
FT                                /FTId=VAR_057902.
FT   VARIANT      25     25       L -> R (in EDSCL1; not or less
FT                                efficiently secreted into the
FT                                extracellular matrix).
FT                                {ECO:0000269|PubMed:18972565}.
FT                                /FTId=VAR_057903.
FT   VARIANT     114    114       A -> D (unclassified mutation;
FT                                dbSNP:rs147589613).
FT                                {ECO:0000269|PubMed:15580559}.
FT                                /FTId=VAR_057904.
FT   VARIANT     192    192       D -> N (in dbSNP:rs138579182).
FT                                {ECO:0000269|PubMed:15580559}.
FT                                /FTId=VAR_057905.
FT   VARIANT     229    229       D -> N (associated with increased risk of
FT                                cervical artery dissection).
FT                                {ECO:0000269|PubMed:10471441}.
FT                                /FTId=VAR_057906.
FT   VARIANT     393    393       P -> S (unclassified mutation).
FT                                {ECO:0000269|PubMed:15580559}.
FT                                /FTId=VAR_057907.
FT   VARIANT     530    530       G -> S (in EDSCL1; dbSNP:rs61735045).
FT                                {ECO:0000269|PubMed:10602121,
FT                                ECO:0000269|PubMed:11992482,
FT                                ECO:0000269|PubMed:15580559}.
FT                                /FTId=VAR_015412.
FT   VARIANT     863    863       E -> V (in dbSNP:rs139788610).
FT                                {ECO:0000269|PubMed:26477546}.
FT                                /FTId=VAR_075702.
FT   VARIANT     908    908       P -> L (found in a renal cell carcinoma
FT                                case; somatic mutation;
FT                                dbSNP:rs772211736).
FT                                {ECO:0000269|PubMed:21248752}.
FT                                /FTId=VAR_064702.
FT   VARIANT     951    951       N -> S (unclassified mutation;
FT                                dbSNP:rs61736966).
FT                                {ECO:0000269|PubMed:15580559}.
FT                                /FTId=VAR_057908.
FT   VARIANT    1140   1140       V -> M (in dbSNP:rs149616140).
FT                                {ECO:0000269|PubMed:26477546}.
FT                                /FTId=VAR_075703.
FT   VARIANT    1486   1486       G -> C (in EDSCL1).
FT                                {ECO:0000269|PubMed:15580559}.
FT                                /FTId=VAR_057909.
FT   VARIANT    1489   1489       G -> D (in EDSCL1).
FT                                {ECO:0000269|PubMed:10602121}.
FT                                /FTId=VAR_015413.
FT   VARIANT    1639   1639       C -> S (in EDSCL1; dbSNP:rs80338764).
FT                                {ECO:0000269|PubMed:9042913}.
FT                                /FTId=VAR_001808.
FT   CONFLICT     82     83       QL -> HV (in Ref. 2; AAA59993).
FT                                {ECO:0000305}.
FT   CONFLICT    390    390       A -> R (in Ref. 2; AAA59993).
FT                                {ECO:0000305}.
FT   CONFLICT    641    641       E -> G (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    650    650       P -> L (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    663    663       R -> E (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    668    668       E -> Q (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    677    677       E -> K (in Ref. 1; BAA14323).
FT                                {ECO:0000305}.
FT   CONFLICT    677    677       E -> Q (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    684    684       L -> P (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    692    699       PPGPPGVT -> VTGEPGAP (in Ref. 4; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    727    727       G -> Q (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    741    741       P -> L (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    747    747       L -> Q (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    753    753       P -> A (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    759    759       D -> N (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    776    777       GQ -> QK (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    849    855       GGPNGDP -> IGPPGPR (in Ref. 5; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    894    894       N -> D (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT   1295   1299       LPGEG -> PSGRS (in Ref. 1; BAA14323).
FT                                {ECO:0000305}.
FT   CONFLICT   1554   1554       K -> R (in Ref. 1; BAA14323).
FT                                {ECO:0000305}.
FT   CONFLICT   1813   1813       V -> A (in Ref. 2; AAA59993).
FT                                {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
//
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