ID CO5A2_HUMAN Reviewed; 1499 AA.
AC P05997; P78440; Q13908; Q53WR4; Q59GR4; Q6LDJ5; Q7KZ55; Q86XF6; Q96QB0;
AC Q96QB3;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 27-MAR-2024, entry version 234.
DE RecName: Full=Collagen alpha-2(V) chain;
DE Flags: Precursor;
GN Name=COL5A2;
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].
RA Richards A.J.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-463.
RX PubMed=2914927; DOI=10.1016/s0021-9258(19)81674-5;
RA Woodbury D., Benson-Chanda V., Ramirez F.;
RT "Amino-terminal propeptide of human pro-alpha 2(V) collagen conforms to the
RT structural criteria of a fibrillar procollagen molecule.";
RL J. Biol. Chem. 264:2735-2738(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104 AND 153-1499.
RX PubMed=11566270; DOI=10.1016/s0945-053x(01)00145-7;
RA Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G.,
RA Ala-Kokko L.;
RT "Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has
RT evolved differently than the other minor fibrillar collagen genes.";
RL Matrix Biol. 20:357-366(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=1820205;
RA Greenspan D.S., Lee S.T., Lee B.S., Hoffman G.G.;
RT "Homology between alpha 2(V) and alpha 1(III) collagen promoters and
RT evidence for negatively acting elements in the alpha 2(V) first intron and
RT 5' flanking sequences.";
RL Gene Expr. 1:29-39(1991).
RN [7]
RP PROTEIN SEQUENCE OF 208-227.
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 [8]
RP PROTEIN SEQUENCE OF 288-297 AND 609-620, AND HYDROXYLATION AT PRO-290;
RP PRO-293; PRO-296; PRO-611 AND PRO-617.
RC TISSUE=Bone;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 398-1499.
RX PubMed=3029669; DOI=10.1093/nar/15.1.181;
RA Weil D., Bernard M.P., Gargano S., Ramirez F.;
RT "The pro alpha 2(V) collagen gene is evolutionarily related to the major
RT fibrillar-forming collagens.";
RL Nucleic Acids Res. 15:181-198(1987).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 878-1499.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1229, AND PROTEIN SEQUENCE OF 1006-1036.
RX PubMed=2985598; DOI=10.1016/s0021-9258(18)89055-x;
RA Myers J.C., Loidl H.R., Stolle C.A., Seyer J.M.;
RT "Partial covalent structure of the human alpha 2 type V collagen chain.";
RL J. Biol. Chem. 260:5533-5541(1985).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1006-1037.
RX PubMed=3858826; DOI=10.1073/pnas.82.10.3385;
RA Emanuel B.S., Cannizzaro L.A., Seyer J.M., Myers J.C.;
RT "Human alpha 1(III) and alpha 2(V) procollagen genes are located on the
RT long arm of chromosome 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3385-3389(1985).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1230-1499.
RX PubMed=2411731; DOI=10.1016/s0021-9258(17)39168-8;
RA Myers J.C., Loidl H.R., Seyer J.M., Dion A.S.;
RT "Complete primary structure of the human alpha 2 type V procollagen COOH-
RT terminal propeptide.";
RL J. Biol. Chem. 260:11216-11222(1985).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1452-1499.
RX PubMed=3224983; DOI=10.1016/0888-7543(88)90089-4;
RA Tsipouras P., Schwartz R.C., Liddell A.C., Salkeld C.S., Weil D.,
RA Ramirez F.;
RT "Genetic distance of two fibrillar collagen loci, COL3A1 and COL5A2,
RT located on the long arm of human chromosome 2.";
RL Genomics 3:275-277(1988).
RN [15]
RP INVOLVEMENT IN EDSCL2.
RX PubMed=9425231; DOI=10.1093/hmg/7.2.249;
RA Michalickova K., Susic M., Willing M.C., Wenstrup R.J., Cole W.G.;
RT "Mutations of the alpha2(V) chain of type V collagen impair matrix assembly
RT and produce Ehlers-Danlos syndrome type I.";
RL Hum. Mol. Genet. 7:249-255(1998).
RN [16]
RP HYDROXYLATION AT PRO-919 AND PRO-1156, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=21757687; DOI=10.1074/jbc.m111.267906;
RA Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.;
RT "A role for prolyl 3-hydroxylase 2 in post-translational modification of
RT fibril-forming collagens.";
RL J. Biol. Chem. 286:30662-30669(2011).
RN [17]
RP VARIANT EDSCL2 ARG-963.
RX PubMed=9783710; DOI=10.1136/jmg.35.10.846;
RA Richards A.J., Martin S., Nicholls A.C., Harrison J.B., Pope F.M.,
RA Burrows N.P.;
RT "A single base mutation in COL5A2 causes Ehlers-Danlos syndrome type II.";
RL J. Med. Genet. 35:846-848(1998).
RN [18]
RP VARIANTS ALA-512; LEU-833; SER-1230 AND VAL-1432.
RX PubMed=11940702; DOI=10.1212/wnl.58.7.1103;
RA Grond-Ginsbach C., Wigger F., Morcher M., von Pein F., Grau A., Hausser I.,
RA Brandt T.;
RT "Sequence analysis of the COL5A2 gene in patients with spontaneous cervical
RT artery dissections.";
RL Neurology 58:1103-1105(2002).
RN [19]
RP VARIANT EDSCL2 ARG-228.
RX PubMed=27656288; DOI=10.1038/hgv.2016.30;
RA Watanabe M., Nakagawa R., Naruto T., Kohmoto T., Suga K., Goji A.,
RA Kagami S., Masuda K., Imoto I.;
RT "A novel missense mutation of COL5A2 in a patient with Ehlers-Danlos
RT syndrome.";
RL Hum. Genome Var. 3:16030-16030(2016).
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. Type V collagen is a key
CC determinant in the assembly of tissue-specific matrices (By
CC similarity). {ECO:0000250}.
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 -!- 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-P) are hydroxylated in some or all of the chains. Probably 3-
CC hydroxylated on Pro-919 and Pro-1156 by LEPREL1.
CC {ECO:0000269|PubMed:21757687, ECO:0000269|PubMed:8181482}.
CC -!- DISEASE: Ehlers-Danlos syndrome, classic type, 2 (EDSCL2) [MIM:130010]:
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. EDSCL2 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:27656288, ECO:0000269|PubMed:9425231,
CC ECO:0000269|PubMed:9783710}. 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43613.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAY24185.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD92282.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y14690; CAA75002.1; -; mRNA.
DR EMBL; AB209045; BAD92282.1; ALT_INIT; mRNA.
DR EMBL; AC064833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133106; AAY24185.1; ALT_SEQ; Genomic_DNA.
DR EMBL; J04478; AAA51859.1; -; mRNA.
DR EMBL; AY016288; AAL13165.1; -; Genomic_DNA.
DR EMBL; AY016287; AAL13165.1; JOINED; Genomic_DNA.
DR EMBL; AY016295; AAL13166.1; -; Genomic_DNA.
DR EMBL; AY016289; AAL13166.1; JOINED; Genomic_DNA.
DR EMBL; AY016290; AAL13166.1; JOINED; Genomic_DNA.
DR EMBL; AY016291; AAL13166.1; JOINED; Genomic_DNA.
DR EMBL; AY016292; AAL13166.1; JOINED; Genomic_DNA.
DR EMBL; AY016293; AAL13166.1; JOINED; Genomic_DNA.
DR EMBL; AY016294; AAL13166.1; JOINED; Genomic_DNA.
DR EMBL; M58529; AAC41699.1; -; Genomic_DNA.
DR EMBL; X04758; CAA28454.1; -; mRNA.
DR EMBL; BC043613; AAH43613.1; ALT_INIT; mRNA.
DR EMBL; M10956; AAA52007.1; -; mRNA.
DR EMBL; M11135; AAA51857.1; -; mRNA.
DR EMBL; M11718; AAA52058.1; -; mRNA.
DR EMBL; J03051; AAA51858.1; -; Genomic_DNA.
DR CCDS; CCDS33350.1; -.
DR PIR; A31427; CGHU2V.
DR RefSeq; NP_000384.2; NM_000393.4.
DR AlphaFoldDB; P05997; -.
DR SMR; P05997; -.
DR BioGRID; 107687; 13.
DR ComplexPortal; CPX-1727; Collagen type V trimer variant 1.
DR ComplexPortal; CPX-1728; Collagen type V trimer variant 2.
DR ComplexPortal; CPX-1751; Collagen type XI trimer variant 2.
DR ComplexPortal; CPX-1752; Collagen type XI trimer variant 3.
DR IntAct; P05997; 4.
DR STRING; 9606.ENSP00000364000; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyConnect; 1136; 6 N-Linked glycans (2 sites).
DR GlyCosmos; P05997; 3 sites, 7 glycans.
DR GlyGen; P05997; 5 sites, 6 N-linked glycans (2 sites), 2 O-linked glycans (3 sites).
DR iPTMnet; P05997; -.
DR PhosphoSitePlus; P05997; -.
DR BioMuta; COL5A2; -.
DR DMDM; 143811378; -.
DR EPD; P05997; -.
DR jPOST; P05997; -.
DR MassIVE; P05997; -.
DR MaxQB; P05997; -.
DR PaxDb; 9606-ENSP00000364000; -.
DR PeptideAtlas; P05997; -.
DR ProteomicsDB; 51866; -.
DR Antibodypedia; 34019; 195 antibodies from 28 providers.
DR DNASU; 1290; -.
DR Ensembl; ENST00000374866.9; ENSP00000364000.3; ENSG00000204262.14.
DR GeneID; 1290; -.
DR KEGG; hsa:1290; -.
DR MANE-Select; ENST00000374866.9; ENSP00000364000.3; NM_000393.5; NP_000384.2.
DR UCSC; uc002uqk.4; human.
DR AGR; HGNC:2210; -.
DR CTD; 1290; -.
DR DisGeNET; 1290; -.
DR GeneCards; COL5A2; -.
DR GeneReviews; COL5A2; -.
DR HGNC; HGNC:2210; COL5A2.
DR HPA; ENSG00000204262; Low tissue specificity.
DR MalaCards; COL5A2; -.
DR MIM; 120190; gene.
DR MIM; 130010; phenotype.
DR neXtProt; NX_P05997; -.
DR OpenTargets; ENSG00000204262; -.
DR Orphanet; 287; Classical Ehlers-Danlos syndrome.
DR PharmGKB; PA26725; -.
DR VEuPathDB; HostDB:ENSG00000204262; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155675; -.
DR InParanoid; P05997; -.
DR OMA; CESPQVP; -.
DR OrthoDB; 2970887at2759; -.
DR PhylomeDB; P05997; -.
DR TreeFam; TF344135; -.
DR PathwayCommons; P05997; -.
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; P05997; -.
DR SIGNOR; P05997; -.
DR BioGRID-ORCS; 1290; 10 hits in 1146 CRISPR screens.
DR ChiTaRS; COL5A2; human.
DR GeneWiki; COL5A2; -.
DR GenomeRNAi; 1290; -.
DR Pharos; P05997; Tbio.
DR PRO; PR:P05997; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P05997; Protein.
DR Bgee; ENSG00000204262; Expressed in tendon of biceps brachii and 202 other cell types or tissues.
DR ExpressionAtlas; P05997; baseline and differential.
DR Genevisible; P05997; HS.
DR GO; GO:0005588; C:collagen type V trimer; IMP:UniProtKB.
DR GO; GO:0005592; C:collagen type XI trimer; NAS:ComplexPortal.
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; NAS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
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:1903225; P:negative regulation of endodermal cell differentiation; IDA:UniProtKB.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR GO; GO:0043588; P:skin development; IMP:UniProtKB.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 6.20.200.20; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF58; COLLAGEN ALPHA-1(II) CHAIN; 1.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 6.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Collagen; Direct protein sequencing; Disease variant;
KW Disulfide bond; Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein;
KW Hydroxylation; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT CHAIN 27..1229
FT /note="Collagen alpha-2(V) chain"
FT /id="PRO_0000005830"
FT PROPEP 1230..1499
FT /note="C-terminal propeptide"
FT /id="PRO_0000005831"
FT DOMAIN 39..97
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1266..1499
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 104..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 506..508
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 944..946
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1067..1069
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1070..1072
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1100..1102
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1127..1129
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1136..1138
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 168..183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..935
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1044
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 290
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 293
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 296
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 611
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 617
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8181482"
FT MOD_RES 919
FT /note="3-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:21757687"
FT MOD_RES 1156
FT /note="3-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:21757687"
FT CARBOHYD 1262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1296..1328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1336..1497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1405..1450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT VARIANT 228
FT /note="G -> R (in EDSCL2)"
FT /evidence="ECO:0000269|PubMed:27656288"
FT /id="VAR_078424"
FT VARIANT 460
FT /note="P -> S (in dbSNP:rs35830636)"
FT /id="VAR_048799"
FT VARIANT 512
FT /note="V -> A (in dbSNP:rs35852101)"
FT /evidence="ECO:0000269|PubMed:11940702"
FT /id="VAR_057910"
FT VARIANT 833
FT /note="P -> L (in dbSNP:rs116298748)"
FT /evidence="ECO:0000269|PubMed:11940702"
FT /id="VAR_057911"
FT VARIANT 956
FT /note="R -> P (in dbSNP:rs6434313)"
FT /id="VAR_048800"
FT VARIANT 963
FT /note="G -> R (in EDSCL2; dbSNP:rs1186550791)"
FT /evidence="ECO:0000269|PubMed:9783710"
FT /id="VAR_013588"
FT VARIANT 1230
FT /note="T -> S (in dbSNP:rs767234623)"
FT /evidence="ECO:0000269|PubMed:11940702"
FT /id="VAR_057912"
FT VARIANT 1432
FT /note="D -> V (in dbSNP:rs141777954)"
FT /evidence="ECO:0000269|PubMed:11940702"
FT /id="VAR_057913"
FT CONFLICT 292
FT /note="A -> P (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="M -> L (in Ref. 5; AAL13166)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="A -> P (in Ref. 1; CAA75002, 4; AAA51859 and 9;
FT CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 463..466
FT /note="IRGQ -> NSGL (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="I -> N (in Ref. 4; AAA51859)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..474
FT /note="Missing (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="V -> L (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="R -> K (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="S -> T (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="S -> N (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="A -> P (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="E -> K (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="S -> Y (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="V -> P (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="A -> R (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="L -> H (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="D -> G (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="R -> G (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 811..812
FT /note="PT -> LL (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="P -> S (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="L -> P (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 955
FT /note="D -> V (in Ref. 1; CAA75002 and 9; CAA28454)"
FT /evidence="ECO:0000305"
FT CONFLICT 1111..1112
FT /note="PP -> HL (in Ref. 1; CAA75002, 9; CAA28454 and 11;
FT AAA52007)"
FT /evidence="ECO:0000305"
FT CONFLICT 1196
FT /note="I -> L (in Ref. 1; CAA75002, 9; CAA28454 and 11;
FT AAA52007)"
FT /evidence="ECO:0000305"
FT CONFLICT 1421
FT /note="K -> T (in Ref. 13; AAA52058)"
FT /evidence="ECO:0000305"
FT CONFLICT 1441
FT /note="F -> S (in Ref. 13; AAA52058)"
FT /evidence="ECO:0000305"
FT CONFLICT 1467
FT /note="Q -> E (in Ref. 14; AAA51858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1499 AA; 144910 MW; E8C92BF5E749EC97 CRC64;
MMANWAEARP LLILIVLLGQ FVSIKAQEED EDEGYGEEIA CTQNGQMYLN RDIWKPAPCQ
ICVCDNGAIL CDKIECQDVL DCADPVTPPG ECCPVCSQTP GGGNTNFGRG RKGQKGEPGL
VPVVTGIRGR PGPAGPPGSQ GPRGERGPKG RPGPRGPQGI DGEPGVPGQP GAPGPPGHPS
HPGPDGLSRP FSAQMAGLDE KSGLGSQVGL MPGSVGPVGP RGPQGLQGQQ GGAGPTGPPG
EPGDPGPMGP IGSRGPEGPP GKPGEDGEPG RNGNPGEVGF AGSPGARGFP GAPGLPGLKG
HRGHKGLEGP KGEVGAPGSK GEAGPTGPMG AMGPLGPRGM PGERGRLGPQ GAPGQRGAHG
MPGKPGPMGP LGIPGSSGFP GNPGMKGEAG PTGARGPEGP QGQRGETGPP GPVGSPGLPG
AIGTDGTPGA KGPTGSPGTS GPPGSAGPPG SPGPQGSTGP QGIRGQPGDP GVPGFKGEAG
PKGEPGPHGI QGPIGPPGEE GKRGPRGDPG TVGPPGPVGE RGAPGNRGFP GSDGLPGPKG
AQGERGPVGS SGPKGSQGDP GRPGEPGLPG ARGLTGNPGV QGPEGKLGPL GAPGEDGRPG
PPGSIGIRGQ PGSMGLPGPK GSSGDPGKPG EAGNAGVPGQ RGAPGKDGEV GPSGPVGPPG
LAGERGEQGP PGPTGFQGLP GPPGPPGEGG KPGDQGVPGD PGAVGPLGPR GERGNPGERG
EPGITGLPGE KGMAGGHGPD GPKGSPGPSG TPGDTGPPGL QGMPGERGIA GTPGPKGDRG
GIGEKGAEGT AGNDGARGLP GPLGPPGPAG PTGEKGEPGP RGLVGPPGSR GNPGSRGENG
PTGAVGFAGP QGPDGQPGVK GEPGEPGQKG DAGSPGPQGL AGSPGPHGPN GVPGLKGGRG
TQGPPGATGF PGSAGRVGPP GPAGAPGPAG PLGEPGKEGP PGLRGDPGSH GRVGDRGPAG
PPGGPGDKGD PGEDGQPGPD GPPGPAGTTG QRGIVGMPGQ RGERGMPGLP GPAGTPGKVG
PTGATGDKGP PGPVGPPGSN GPVGEPGPEG PAGNDGTPGR DGAVGERGDR GDPGPAGLPG
SQGAPGTPGP VGAPGDAGQR GDPGSRGPIG PPGRAGKRGL PGPQGPRGDK GDHGDRGDRG
QKGHRGFTGL QGLPGPPGPN GEQGSAGIPG PFGPRGPPGP VGPSGKEGNP GPLGPIGPPG
VRGSVGEAGP EGPPGEPGPP GPPGPPGHLT AALGDIMGHY DESMPDPLPE FTEDQAAPDD
KNKTDPGVHA TLKSLSSQIE TMRSPDGSKK HPARTCDDLK LCHSAKQSGE YWIDPNQGSV
EDAIKVYCNM ETGETCISAN PSSVPRKTWW ASKSPDNKPV WYGLDMNRGS QFAYGDHQSP
NTAITQMTFL RLLSKEASQN ITYICKNSVG YMDDQAKNLK KAVVLKGAND LDIKAEGNIR
FRYIVLQDTC SKRNGNVGKT VFEYRTQNVA RLPIIDLAPV DVGGTDQEFG VEIGPVCFV
//
