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 03-AUG-2022, entry version 226.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 556-565
RP (ISOFORMS 1/2).
RX PubMed=2071595; DOI=10.1016/s0021-9258(18)98813-7;
RA Takahara K., Seto Y., Okasawa K., Okamoto N., Noda A., Yaoi Y., 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; DOI=10.1016/s0021-9258(18)54290-3;
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., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., 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., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., 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., Rogers J.,
RA 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 PRO-621;
RP LYS-627; PRO-639; LYS-642; PRO-648; PRO-654; PRO-657; PRO-675; PRO-678;
RP LYS-687; PRO-690; PRO-696; PRO-705; LYS-708; PRO-717; PRO-720; PRO-726;
RP PRO-732; LYS-744; PRO-750; PRO-756; PRO-762; PRO-765; PRO-771; LYS-774;
RP PRO-780; PRO-789; LYS-795; 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; 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 [7]
RP PROTEIN SEQUENCE OF 565-576; 756-772; 1012-1029; 1219-1232 AND 1465-1477
RP (ISOFORMS 1/2), AND HYDROXYLATION AT PRO-570; PRO-576; PRO-756; PRO-762;
RP PRO-834; LYS-846; PRO-861; LYS-864; PRO-870; PRO-873; PRO-876; LYS-882;
RP PRO-888; PRO-891; LYS-897; PRO-903; PRO-906; PRO-930; PRO-945; PRO-1017;
RP PRO-1020; PRO-1023; PRO-1029; 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 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 through
RT 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., Naeyaert J.-M.;
RT "Mutations in the COL5A1 gene are causal in the Ehlers-Danlos syndromes I
RT and II.";
RL Am. J. Hum. Genet. 60:547-554(1997).
RN [11]
RP VARIANT ASN-229, AND ASSOCIATION WITH INCREASED RISK OF CERVICAL ARTERY
RP 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 with
RT 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-modifying
RT G530S substitution in COL5A1 of a patient with the classical type of
RT Ehlers-Danlos syndrome: an explanation of intrafamilial variability?";
RL Am. J. Med. Genet. 90:72-79(2000).
RN [13]
RP ERRATUM OF PUBMED:10602121.
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 Ehlers-
RT 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 AND
RP 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 comprehensive
RT study of biochemical and molecular findings in 48 unrelated patients.";
RL Hum. Mutat. 25:28-37(2005).
RN [16]
RP VARIANTS EDSCL1 ARG-25 AND PRO-25, AND CHARACTERIZATION OF VARIANTS EDSCL1
RP 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 cause
RT 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., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT 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., Dionne-Laporte A.,
RA Ospina L.H., Lemyre E., Massicotte C., Laframboise R., Maranda B.,
RA Labuda D., Decarie J.C., Rypens F., Goldsher D., Fallet-Bianco C.,
RA Soucy J.F., Laberge A.M., Maftei C., Boycott K., Brais B., Boucher R.M.,
RA Rouleau G.A., Katsanis N., Majewski J., Elpeleg O., Kukolich M.K.,
RA Shalev S., Michaud J.L.;
RT "Joubert Syndrome in French Canadians and Identification of Mutations in
RT CEP104.";
RL Am. J. Hum. Genet. 97:744-753(2015).
RN [19]
RP VARIANT ASP-114, VARIANTS FMDMF GLU-123; SER-514; TRP-611; LEU-1164 AND
RP SER-1400, AND INVOLVEMENT IN FMDMF.
RX PubMed=32938213; DOI=10.1161/atvbaha.119.313885;
RA Richer J., Hill H.L., Wang Y., Yang M.L., Hunker K.L., Lane J.,
RA Blackburn S., Coleman D.M., Eliason J., Sillon G., D'Agostino M.D.,
RA Jetty P., Mongeon F.P., Laberge A.M., Ryan S.E., Fendrikova-Mahlay N.,
RA Coutinho T., Mathis M.R., Zawistowski M., Hazen S.L., Katz A.E.,
RA Gornik H.L., Brummett C.M., Abecasis G., Bergin I.L., Stanley J.C.,
RA Li J.Z., Ganesh S.K.;
RT "A novel recurrent COL5A1 genetic variant is associated with a dysplasia-
RT associated arterial disease exhibiting dissections and fibromuscular
RT dysplasia.";
RL Arterioscler. Thromb. Vasc. Biol. 40:2686-2699(2020).
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. Interacts with CSPG4.
CC {ECO:0000269|PubMed:9099729}.
CC -!- INTERACTION:
CC P20908; P13497: BMP1; NbExp=2; IntAct=EBI-2464511, EBI-489827;
CC P20908; P02751-1: FN1; NbExp=2; IntAct=EBI-2464511, EBI-22099195;
CC P20908; P08253: MMP2; NbExp=3; IntAct=EBI-2464511, EBI-1033518;
CC P20908; Q15113: PCOLCE; NbExp=2; IntAct=EBI-2464511, EBI-8869614;
CC P20908; P01033: TIMP1; NbExp=2; IntAct=EBI-2464511, EBI-712536;
CC P20908; 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, 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-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) [MIM:130000]:
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. EDSCL1 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:10602121, ECO:0000269|PubMed:11992482,
CC ECO:0000269|PubMed:15580559, ECO:0000269|PubMed:18972565,
CC ECO:0000269|PubMed:9042913}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Fibromuscular dysplasia, multifocal (FMDMF) [MIM:619329]: An
CC autosomal dominant vascular disorder with incomplete penetrance,
CC characterized by fibrous tissue and webs developing in the artery wall
CC and leading to multiple arterial stenoses. Patients with multifocal
CC fibromuscular dysplasia can develop arterial tortuosity,
CC macroaneurysms, and dissections. Arterial rupture may occur.
CC {ECO:0000269|PubMed:32938213}. 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}.
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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 AlphaFoldDB; P20908; -.
DR SMR; P20908; -.
DR BioGRID; 107686; 39.
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; 34.
DR STRING; 9606.ENSP00000360882; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyConnect; 1128; 10 N-Linked glycans (3 sites).
DR GlyGen; P20908; 9 sites, 9 N-linked glycans (3 sites), 3 O-linked glycans (6 sites).
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 Antibodypedia; 3446; 455 antibodies from 37 providers.
DR DNASU; 1289; -.
DR Ensembl; ENST00000371817.8; ENSP00000360882.3; ENSG00000130635.16. [P20908-1]
DR Ensembl; ENST00000618395.4; ENSP00000481360.1; ENSG00000130635.16. [P20908-2]
DR GeneID; 1289; -.
DR KEGG; hsa:1289; -.
DR MANE-Select; ENST00000371817.8; ENSP00000360882.3; NM_000093.5; NP_000084.3.
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; ENSG00000130635; Tissue enhanced (cervix).
DR MalaCards; COL5A1; -.
DR MIM; 120215; gene.
DR MIM; 130000; phenotype.
DR MIM; 619329; phenotype.
DR neXtProt; NX_P20908; -.
DR OpenTargets; ENSG00000130635; -.
DR Orphanet; 287; Classical Ehlers-Danlos syndrome.
DR PharmGKB; PA26724; -.
DR VEuPathDB; HostDB:ENSG00000130635; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000159211; -.
DR HOGENOM; CLU_001074_2_1_1; -.
DR InParanoid; P20908; -.
DR OMA; VAGMDGQ; -.
DR OrthoDB; 199083at2759; -.
DR PhylomeDB; P20908; -.
DR TreeFam; TF323987; -.
DR PathwayCommons; P20908; -.
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; P20908; -.
DR SIGNOR; P20908; -.
DR BioGRID-ORCS; 1289; 17 hits in 1076 CRISPR screens.
DR ChiTaRS; COL5A1; human.
DR GeneWiki; Collagen,_type_V,_alpha_1; -.
DR GenomeRNAi; 1289; -.
DR Pharos; P20908; Tbio.
DR PRO; PR:P20908; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P20908; protein.
DR Bgee; ENSG00000130635; Expressed in stromal cell of endometrium and 175 other tissues.
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:0005592; C:collagen type XI trimer; IC:ComplexPortal.
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 Alternative splicing; Calcium; Collagen; Direct protein sequencing;
KW Disease variant; Disulfide bond; Ehlers-Danlos syndrome;
KW Extracellular matrix; Heparin-binding; Hydroxylation; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..1605
FT /note="Collagen alpha-1(V) chain"
FT /id="PRO_0000005756"
FT PROPEP 1606..1838
FT /note="C-terminal propeptide"
FT /id="PRO_0000005757"
FT DOMAIN 72..244
FT /note="Laminin G-like"
FT DOMAIN 1609..1837
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 231..443
FT /note="Nonhelical region"
FT REGION 242..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..558
FT /note="Interrupted collagenous region"
FT REGION 470..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..1570
FT /note="Triple-helical region"
FT REGION 1571..1605
FT /note="Nonhelical region"
FT COMPBIAS 281..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..700
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..973
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1657
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1659
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1660
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1662
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1665
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 234
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 236
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 240
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 262
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 263
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 338
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 340
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 346
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 347
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 416
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 417
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 420
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 421
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 570
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 576
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 621
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 627
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 639
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 642
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 648
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 654
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 657
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 675
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 678
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 687
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 690
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 696
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 705
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 708
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 717
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 720
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 726
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 732
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 744
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 750
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 756
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 762
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 765
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 771
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 774
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 780
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 789
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 795
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 804
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 807
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 810
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 816
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 819
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661"
FT MOD_RES 834
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 846
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 861
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 864
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 870
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 873
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 876
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 882
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 888
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 891
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 897
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 903
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 906
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2496661,
FT ECO:0000269|PubMed:8181482"
FT MOD_RES 930
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 945
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 1017
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 1020
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 1023
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 1029
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 1221
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 1224
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 1467
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 1470
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 1601
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1604
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT DISULFID 1639..1671
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1645
FT /note="Interchain (with C-1662)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1662
FT /note="Interchain (with C-1645)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1680..1835
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1746..1789
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT VAR_SEQ 1690..1711
FT /note="ARITSWPKENPGSWFSEFKRGK -> SKMARWPKEQPSTWYSQYKRGS (in
FT isoform 2)"
FT /id="VSP_059655"
FT VARIANT 25
FT /note="L -> P (in EDSCL1; not or less efficiently secreted
FT into the extracellular matrix)"
FT /evidence="ECO:0000269|PubMed:18972565"
FT /id="VAR_057902"
FT VARIANT 25
FT /note="L -> R (in EDSCL1; not or less efficiently secreted
FT into the extracellular matrix)"
FT /evidence="ECO:0000269|PubMed:18972565"
FT /id="VAR_057903"
FT VARIANT 114
FT /note="A -> D (in dbSNP:rs147589613)"
FT /evidence="ECO:0000269|PubMed:15580559,
FT ECO:0000269|PubMed:32938213"
FT /id="VAR_057904"
FT VARIANT 123
FT /note="Q -> E (in FMDMF; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32938213"
FT /id="VAR_085830"
FT VARIANT 192
FT /note="D -> N (in dbSNP:rs138579182)"
FT /evidence="ECO:0000269|PubMed:15580559"
FT /id="VAR_057905"
FT VARIANT 229
FT /note="D -> N (associated with increased risk of cervical
FT artery dissection)"
FT /evidence="ECO:0000269|PubMed:10471441"
FT /id="VAR_057906"
FT VARIANT 514
FT /note="G -> S (in FMDMF)"
FT /evidence="ECO:0000269|PubMed:32938213"
FT /id="VAR_085831"
FT VARIANT 530
FT /note="G -> S (in EDSCL1; dbSNP:rs61735045)"
FT /evidence="ECO:0000269|PubMed:10602121,
FT ECO:0000269|PubMed:11992482, ECO:0000269|PubMed:15580559"
FT /id="VAR_015412"
FT VARIANT 611
FT /note="R -> W (in FMDMF; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32938213"
FT /id="VAR_085832"
FT VARIANT 863
FT /note="E -> V (in dbSNP:rs139788610)"
FT /evidence="ECO:0000269|PubMed:26477546"
FT /id="VAR_075702"
FT VARIANT 908
FT /note="P -> L (found in a renal cell carcinoma case;
FT somatic mutation; dbSNP:rs772211736)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064702"
FT VARIANT 951
FT /note="N -> S (in dbSNP:rs61736966)"
FT /evidence="ECO:0000269|PubMed:15580559"
FT /id="VAR_057908"
FT VARIANT 1140
FT /note="V -> M (in dbSNP:rs149616140)"
FT /evidence="ECO:0000269|PubMed:26477546"
FT /id="VAR_075703"
FT VARIANT 1164
FT /note="P -> L (in FMDMF; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32938213"
FT /id="VAR_085833"
FT VARIANT 1400
FT /note="P -> S (in FMDMF; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:32938213"
FT /id="VAR_085834"
FT VARIANT 1486
FT /note="G -> C (in EDSCL1)"
FT /evidence="ECO:0000269|PubMed:15580559"
FT /id="VAR_057909"
FT VARIANT 1489
FT /note="G -> D (in EDSCL1)"
FT /evidence="ECO:0000269|PubMed:10602121"
FT /id="VAR_015413"
FT VARIANT 1639
FT /note="C -> S (in EDSCL1; dbSNP:rs80338764)"
FT /evidence="ECO:0000269|PubMed:9042913"
FT /id="VAR_001808"
FT CONFLICT 82..83
FT /note="QL -> HV (in Ref. 2; AAA59993)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="A -> R (in Ref. 2; AAA59993)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="E -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="P -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="R -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="E -> K (in Ref. 1; BAA14323)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="L -> P (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 692..699
FT /note="PPGPPGVT -> VTGEPGAP (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="G -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="P -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="L -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="P -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="D -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 776..777
FT /note="GQ -> QK (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 849..855
FT /note="GGPNGDP -> IGPPGPR (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1295..1299
FT /note="LPGEG -> PSGRS (in Ref. 1; BAA14323)"
FT /evidence="ECO:0000305"
FT CONFLICT 1554
FT /note="K -> R (in Ref. 1; BAA14323)"
FT /evidence="ECO:0000305"
FT CONFLICT 1813
FT /note="V -> A (in Ref. 2; AAA59993)"
FT /evidence="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
