CSPG2_HUMAN
ID CSPG2_HUMAN Reviewed; 3396 AA.
AC P13611; P20754; Q13010; Q13189; Q15123; Q9UCL9; Q9UNW5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 242.
DE RecName: Full=Versican core protein;
DE AltName: Full=Chondroitin sulfate proteoglycan core protein 2;
DE Short=Chondroitin sulfate proteoglycan 2;
DE AltName: Full=Glial hyaluronate-binding protein;
DE Short=GHAP;
DE AltName: Full=Large fibroblast proteoglycan;
DE AltName: Full=PG-M;
DE Flags: Precursor;
GN Name=VCAN; Synonyms=CSPG2;
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 V1), AND SUBCELLULAR LOCATION.
RC TISSUE=Placenta;
RX PubMed=2583089; DOI=10.1002/j.1460-2075.1989.tb08447.x;
RA Zimmermann D.R., Ruoslahti E.;
RT "Multiple domains of the large fibroblast proteoglycan, versican.";
RL EMBO J. 8:2975-2981(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V2).
RC TISSUE=Glial tumor;
RX PubMed=7806529; DOI=10.1016/s0021-9258(20)30089-2;
RA Dours-Zimmermann M.T., Zimmermann D.R.;
RT "A novel glycosaminoglycan attachment domain identified in two alternative
RT splice variants of human versican.";
RL J. Biol. Chem. 269:32992-32998(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM V0).
RX PubMed=7528742; DOI=10.1016/s0021-9258(20)30090-9;
RA Naso M.F., Zimmermann D.R., Iozzo R.V.;
RT "Characterization of the complete genomic structure of the human versican
RT gene and functional analysis of its promoter.";
RL J. Biol. Chem. 269:32999-33008(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V3).
RC TISSUE=Brain;
RX PubMed=7876137; DOI=10.1074/jbc.270.8.3914;
RA Zako M., Shinomura T., Ujita M., Ito K., Kimata K.;
RT "Expression of PG-M(V3), an alternatively spliced form of PG-M without a
RT chondroitin sulfate attachment in region in mouse and human tissues.";
RL J. Biol. Chem. 270:3914-3918(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 208-1427; 2081-2372 AND 2897-3233 (ISOFORM
RP V1), AND DEVELOPMENTAL STAGE.
RX PubMed=7921538; DOI=10.1016/0945-053x(94)90185-6;
RA Yao L.Y., Moody C., Schoenherr E., Wight T.N., Sandell L.J.;
RT "Identification of the proteoglycan versican in aorta and smooth muscle
RT cells by DNA sequence analysis, in situ hybridization and
RT immunohistochemistry.";
RL Matrix Biol. 14:213-225(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-347.
RX PubMed=1478664; DOI=10.1016/s0888-7543(05)80103-x;
RA Iozzo R.V., Naso M.F., Cannizzaro L.A., Wasmuth J.J., McPherson J.D.;
RT "Mapping of the versican proteoglycan gene (CSPG2) to the long arm of human
RT chromosome 5 (5q12-5q14).";
RL Genomics 14:845-851(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2709-3396.
RC TISSUE=Lung fibroblast;
RX PubMed=2820964; DOI=10.1016/s0021-9258(18)45176-9;
RA Krusius T., Gehlsen K.R., Ruoslahti E.;
RT "A fibroblast chondroitin sulfate proteoglycan core protein contains
RT lectin-like and growth factor-like sequences.";
RL J. Biol. Chem. 262:13120-13125(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3333-3396 (ISOFORM VINT).
RC TISSUE=Aortic smooth muscle;
RX PubMed=10397680; DOI=10.1161/01.atv.19.7.1630;
RA Lemire J.M., Braun K.R., Maurel P., Kaplan E.D., Schwartz S.M., Wight T.N.;
RT "Versican/PG-M isoforms in vascular smooth muscle cells.";
RL Arterioscler. Thromb. Vasc. Biol. 19:1630-1639(1999).
RN [9]
RP PROTEIN SEQUENCE OF 21-37.
RX PubMed=1429726; DOI=10.1016/s0021-9258(18)35919-2;
RA Perides G., Rahemtulla F., Lane W.S., Asher R.A., Bignami A.;
RT "Isolation of a large aggregating proteoglycan from human brain.";
RL J. Biol. Chem. 267:23883-23887(1992).
RN [10]
RP PROTEIN SEQUENCE OF 24-50; 80-119; 128-155; 167-218; 229-268 AND 277-290.
RC TISSUE=Brain;
RX PubMed=2466833; DOI=10.1016/s0021-9258(18)83646-8;
RA Perides G., Lane W.S., Andrews D., Dahl D., Bignami A.;
RT "Isolation and partial characterization of a glial hyaluronate-binding
RT protein.";
RL J. Biol. Chem. 264:5981-5987(1989).
RN [11]
RP PROTEIN SEQUENCE OF 171-210 AND 289-303, AND TISSUE SPECIFICITY.
RX PubMed=2469524; DOI=10.1016/0361-9230(89)90129-9;
RA Bignami A., Lane W.S., Andrews D., Dahl D.;
RT "Structural similarity of hyaluronate binding proteins in brain and
RT cartilage.";
RL Brain Res. Bull. 22:67-70(1989).
RN [12]
RP TISSUE SPECIFICITY (ISOFORMS V0; V1; V2 AND V3).
RX PubMed=8627343; DOI=10.1097/00005072-199605000-00005;
RA Paulus W., Baur I., Dours-Zimmermann M.T., Zimmermann D.R.;
RT "Differential expression of versican isoforms in brain tumors.";
RL J. Neuropathol. Exp. Neurol. 55:528-533(1996).
RN [13]
RP INVOLVEMENT IN WGVRP.
RX PubMed=16043844; DOI=10.1167/iovs.05-0057;
RA Miyamoto T., Inoue H., Sakamoto Y., Kudo E., Naito T., Mikawa T.,
RA Mikawa Y., Isashiki Y., Osabe D., Shinohara S., Shiota H., Itakura M.;
RT "Identification of a novel splice site mutation of the CSPG2 gene in a
RT Japanese family with Wagner syndrome.";
RL Invest. Ophthalmol. Vis. Sci. 46:2726-2735(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP INVOLVEMENT IN WGVRP, AND PATHOLOGICAL MECHANISM.
RX PubMed=22739342; DOI=10.1038/ejhg.2012.137;
RA Kloeckener-Gruissem B., Neidhardt J., Magyar I., Plauchu H., Zech J.C.,
RA Morle L., Palmer-Smith S.M., Macdonald M.J., Nas V., Fry A.E., Berger W.;
RT "Novel VCAN mutations and evidence for unbalanced alternative splicing in
RT the pathogenesis of Wagner syndrome.";
RL Eur. J. Hum. Genet. 21:352-356(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2116 AND THR-2617, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP PHOSPHORYLATION AT SER-2116.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [18]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023;
RA Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y.,
RA Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C.,
RA Lako M.;
RT "Extracellular matrix component expression in human pluripotent stem cell-
RT derived retinal organoids recapitulates retinogenesis in vivo and reveals
RT an important role for IMPG1 and CD44 in the development of photoreceptors
RT and interphotoreceptor matrix.";
RL Acta Biomater. 74:207-221(2018).
CC -!- FUNCTION: May play a role in intercellular signaling and in connecting
CC cells with the extracellular matrix. May take part in the regulation of
CC cell motility, growth and differentiation. Binds hyaluronic acid.
CC -!- SUBUNIT: Interacts with FBLN1. {ECO:0000250}.
CC -!- INTERACTION:
CC P13611; P14780: MMP9; NbExp=3; IntAct=EBI-8515977, EBI-1382326;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305|PubMed:2583089}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000269|PubMed:29777959}. Secreted,
CC extracellular space, extracellular matrix, interphotoreceptor matrix
CC {ECO:0000269|PubMed:29777959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=V0;
CC IsoId=P13611-1; Sequence=Displayed;
CC Name=V1;
CC IsoId=P13611-2; Sequence=VSP_003082, VSP_003083;
CC Name=V2;
CC IsoId=P13611-3; Sequence=VSP_003084;
CC Name=V3;
CC IsoId=P13611-4; Sequence=VSP_003082, VSP_003085;
CC Name=Vint;
CC IsoId=P13611-5; Sequence=VSP_003086;
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level)
CC (PubMed:29777959). Cerebral white matter and plasma (PubMed:2469524).
CC Isoform V0: Expressed in normal brain, gliomas, medulloblastomas,
CC schwannomas, neurofibromas, and meningiomas (PubMed:8627343). Isoform
CC V1: Expressed in normal brain, gliomas, medulloblastomas, schwannomas,
CC neurofibromas, and meningiomas (PubMed:8627343). Isoform V2: Restricted
CC to normal brain and gliomas (PubMed:8627343). Isoform V3: Found in all
CC these tissues except medulloblastomas (PubMed:8627343).
CC {ECO:0000269|PubMed:2469524, ECO:0000269|PubMed:29777959,
CC ECO:0000269|PubMed:8627343}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing photoreceptors and the
CC interphotoreceptor matrix between 12 and 17 weeks post conception (at
CC protein level) (PubMed:29777959). Disappears in aorta after the
CC cartilage development (PubMed:7921538). {ECO:0000269|PubMed:29777959,
CC ECO:0000269|PubMed:7921538}.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000269|PubMed:26091039}.
CC -!- PTM: Proteolytically cleaved by ADAMTS5 and ADAMTS15 in the
CC pericellular matrix surrounding myoblasts, facilitating myoblast
CC contact and fusion which is required for skeletal muscle development
CC and regeneration. {ECO:0000250|UniProtKB:Q62059}.
CC -!- DISEASE: Wagner vitreoretinopathy (WGVRP) [MIM:143200]: A rare
CC vitreoretinopathy characterized by an optically empty vitreous cavity
CC with fibrillary condensations and a preretinal avascular membrane.
CC Other optical features include progressive chorioretinal atrophy,
CC perivascular sheating, subcapsular cataract and myopia.
CC {ECO:0000269|PubMed:16043844, ECO:0000269|PubMed:22739342}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. The pathological mechanism involves a quantitative imbalance of
CC the normally occurring splice variants (PubMed:22739342).
CC {ECO:0000269|PubMed:22739342}.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Versican;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_214";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/VCANID40173ch5q14.html";
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DR EMBL; X15998; CAA34128.1; -; mRNA.
DR EMBL; U16306; AAA65018.1; -; mRNA.
DR EMBL; U26555; AAA67565.1; -; mRNA.
DR EMBL; D32039; BAA06801.1; -; mRNA.
DR EMBL; S52488; AAB24878.1; -; Genomic_DNA.
DR EMBL; J02814; AAA36437.1; -; mRNA.
DR EMBL; AF084545; AAD48545.1; -; mRNA.
DR CCDS; CCDS4060.1; -. [P13611-1]
DR CCDS; CCDS47242.1; -. [P13611-4]
DR CCDS; CCDS54875.1; -. [P13611-3]
DR CCDS; CCDS54876.1; -. [P13611-2]
DR PIR; S06014; A60979.
DR RefSeq; NP_001119808.1; NM_001126336.2. [P13611-4]
DR RefSeq; NP_001157569.1; NM_001164097.1. [P13611-2]
DR RefSeq; NP_001157570.1; NM_001164098.1. [P13611-3]
DR RefSeq; NP_004376.2; NM_004385.4. [P13611-1]
DR SMR; P13611; -.
DR BioGRID; 107844; 48.
DR IntAct; P13611; 11.
DR MINT; P13611; -.
DR STRING; 9606.ENSP00000265077; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR CarbonylDB; P13611; -.
DR GlyConnect; 1890; 14 N-Linked glycans (9 sites), 1 O-Linked glycan (1 site).
DR GlyGen; P13611; 193 sites, 13 N-linked glycans (9 sites), 10 O-linked glycans (167 sites).
DR iPTMnet; P13611; -.
DR PhosphoSitePlus; P13611; -.
DR SwissPalm; P13611; -.
DR BioMuta; VCAN; -.
DR DMDM; 2506816; -.
DR EPD; P13611; -.
DR jPOST; P13611; -.
DR MassIVE; P13611; -.
DR MaxQB; P13611; -.
DR PaxDb; P13611; -.
DR PeptideAtlas; P13611; -.
DR PRIDE; P13611; -.
DR ProteomicsDB; 52938; -. [P13611-1]
DR ProteomicsDB; 52939; -. [P13611-2]
DR ProteomicsDB; 52940; -. [P13611-3]
DR ProteomicsDB; 52941; -. [P13611-4]
DR ProteomicsDB; 52942; -. [P13611-5]
DR Antibodypedia; 1346; 323 antibodies from 30 providers.
DR DNASU; 1462; -.
DR Ensembl; ENST00000265077.8; ENSP00000265077.3; ENSG00000038427.16. [P13611-1]
DR Ensembl; ENST00000342785.8; ENSP00000342768.4; ENSG00000038427.16. [P13611-3]
DR Ensembl; ENST00000343200.9; ENSP00000340062.5; ENSG00000038427.16. [P13611-2]
DR Ensembl; ENST00000502527.2; ENSP00000421362.2; ENSG00000038427.16. [P13611-4]
DR GeneID; 1462; -.
DR KEGG; hsa:1462; -.
DR MANE-Select; ENST00000265077.8; ENSP00000265077.3; NM_004385.5; NP_004376.2.
DR UCSC; uc003kii.4; human. [P13611-1]
DR CTD; 1462; -.
DR DisGeNET; 1462; -.
DR GeneCards; VCAN; -.
DR GeneReviews; VCAN; -.
DR HGNC; HGNC:2464; VCAN.
DR HPA; ENSG00000038427; Tissue enhanced (lymphoid tissue, placenta).
DR MalaCards; VCAN; -.
DR MIM; 118661; gene.
DR MIM; 143200; phenotype.
DR neXtProt; NX_P13611; -.
DR OpenTargets; ENSG00000038427; -.
DR Orphanet; 898; Wagner disease.
DR PharmGKB; PA162408788; -.
DR VEuPathDB; HostDB:ENSG00000038427; -.
DR eggNOG; ENOG502QRBE; Eukaryota.
DR GeneTree; ENSGT00940000156102; -.
DR HOGENOM; CLU_000303_1_1_1; -.
DR InParanoid; P13611; -.
DR OMA; GDSTDNF; -.
DR PhylomeDB; P13611; -.
DR TreeFam; TF332134; -.
DR PathwayCommons; P13611; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-HSA-2024101; CS/DS degradation.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR Reactome; R-HSA-3595172; Defective CHST3 causes SEDCJD.
DR Reactome; R-HSA-3595174; Defective CHST14 causes EDS, musculocontractural type.
DR Reactome; R-HSA-3595177; Defective CHSY1 causes TPBS.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P13611; -.
DR SIGNOR; P13611; -.
DR BioGRID-ORCS; 1462; 7 hits in 1064 CRISPR screens.
DR ChiTaRS; VCAN; human.
DR GeneWiki; Versican; -.
DR GenomeRNAi; 1462; -.
DR Pharos; P13611; Tbio.
DR PRO; PR:P13611; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P13611; protein.
DR Bgee; ENSG00000038427; Expressed in monocyte and 206 other tissues.
DR ExpressionAtlas; P13611; baseline and differential.
DR Genevisible; P13611; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA: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; HDA:BHF-UCL.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0033165; C:interphotoreceptor matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; ISS:BHF-UCL.
DR GO; GO:0005539; F:glycosaminoglycan binding; TAS:ProtInc.
DR GO; GO:0005540; F:hyaluronic acid binding; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0008037; P:cell recognition; TAS:ProtInc.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0008347; P:glial cell migration; IDA:BHF-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR CDD; cd00033; CCP; 1.
DR CDD; cd03588; CLECT_CSPGs; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 3.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033987; CSPG_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00445; LINK; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 3.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS01241; LINK_1; 2.
DR PROSITE; PS50963; LINK_2; 2.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cataract; Cell projection;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Hyaluronic acid; Immunoglobulin domain;
KW Lectin; Phosphoprotein; Proteoglycan; Reference proteome; Repeat; Secreted;
KW Signal; Sushi.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1429726"
FT CHAIN 21..3396
FT /note="Versican core protein"
FT /id="PRO_0000017522"
FT DOMAIN 21..146
FT /note="Ig-like V-type"
FT DOMAIN 150..245
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 251..347
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 3089..3125
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3127..3163
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3176..3290
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 3294..3354
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 348..1335
FT /note="GAG-alpha (glucosaminoglycan attachment domain)"
FT REGION 420..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..3089
FT /note="GAG-beta"
FT REGION 1420..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1717..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1759..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1962..1994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2107..2134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2168..2188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2371..2396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2445..2473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2493..2518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2598..2617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2834..2856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2881..2905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3371..3396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1963..1994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2445..2463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2493..2517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3378..3396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1428..1429
FT /note="Cleavage; by ADAMTS15"
FT /evidence="ECO:0000250|UniProtKB:Q62059"
FT MOD_RES 2116
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62059"
FT MOD_RES 2617
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3067
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..130
FT /evidence="ECO:0000250"
FT DISULFID 172..243
FT /evidence="ECO:0000250"
FT DISULFID 196..217
FT /evidence="ECO:0000250"
FT DISULFID 270..345
FT /evidence="ECO:0000250"
FT DISULFID 294..315
FT /evidence="ECO:0000250"
FT DISULFID 3093..3104
FT /evidence="ECO:0000250"
FT DISULFID 3098..3113
FT /evidence="ECO:0000250"
FT DISULFID 3115..3124
FT /evidence="ECO:0000250"
FT DISULFID 3131..3142
FT /evidence="ECO:0000250"
FT DISULFID 3136..3151
FT /evidence="ECO:0000250"
FT DISULFID 3153..3162
FT /evidence="ECO:0000250"
FT DISULFID 3169..3180
FT /evidence="ECO:0000250"
FT DISULFID 3197..3289
FT /evidence="ECO:0000250"
FT DISULFID 3265..3281
FT /evidence="ECO:0000250"
FT DISULFID 3296..3339
FT /evidence="ECO:0000250"
FT DISULFID 3325..3352
FT /evidence="ECO:0000250"
FT VAR_SEQ 348
FT /note="P -> R (in isoform V1 and isoform V3)"
FT /evidence="ECO:0000303|PubMed:2583089,
FT ECO:0000303|PubMed:7876137, ECO:0000303|PubMed:7921538"
FT /id="VSP_003082"
FT VAR_SEQ 349..3089
FT /note="Missing (in isoform V3)"
FT /evidence="ECO:0000303|PubMed:7876137"
FT /id="VSP_003085"
FT VAR_SEQ 349..1335
FT /note="Missing (in isoform V1)"
FT /evidence="ECO:0000303|PubMed:2583089,
FT ECO:0000303|PubMed:7921538"
FT /id="VSP_003083"
FT VAR_SEQ 1336..3089
FT /note="Missing (in isoform V2)"
FT /evidence="ECO:0000303|PubMed:7806529"
FT /id="VSP_003084"
FT VAR_SEQ 3355..3396
FT /note="PSAYQRTYSMKYFKNSSSAKDNSINTSKHDHRWSRRWQESRR -> RKWSFR
FT KNGLPCYNNY (in isoform Vint)"
FT /evidence="ECO:0000303|PubMed:10397680"
FT /id="VSP_003086"
FT VARIANT 300
FT /note="S -> L (in dbSNP:rs2652098)"
FT /id="VAR_021958"
FT VARIANT 428
FT /note="G -> D (in dbSNP:rs2287926)"
FT /id="VAR_020214"
FT VARIANT 1516
FT /note="K -> R (in dbSNP:rs309559)"
FT /id="VAR_021959"
FT VARIANT 1826
FT /note="R -> H (in dbSNP:rs188703)"
FT /id="VAR_031632"
FT VARIANT 2301
FT /note="F -> Y (in dbSNP:rs160278)"
FT /id="VAR_020215"
FT VARIANT 2315
FT /note="V -> L (in dbSNP:rs3734094)"
FT /id="VAR_020216"
FT VARIANT 2937
FT /note="D -> Y (in dbSNP:rs160277)"
FT /id="VAR_021960"
FT VARIANT 3011
FT /note="N -> K (in dbSNP:rs16900532)"
FT /id="VAR_031633"
FT CONFLICT 88
FT /note="N -> D (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="K -> I (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="D -> A (in Ref. 4; BAA06801)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="Q -> G (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 2709..2713
FT /note="IKAEA -> EFREV (in Ref. 7; AAA36437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3396 AA; 372820 MW; D174A1BBB8304FEC CRC64;
MFINIKSILW MCSTLIVTHA LHKVKVGKSP PVRGSLSGKV SLPCHFSTMP TLPPSYNTSE
FLRIKWSKIE VDKNGKDLKE TTVLVAQNGN IKIGQDYKGR VSVPTHPEAV GDASLTVVKL
LASDAGLYRC DVMYGIEDTQ DTVSLTVDGV VFHYRAATSR YTLNFEAAQK ACLDVGAVIA
TPEQLFAAYE DGFEQCDAGW LADQTVRYPI RAPRVGCYGD KMGKAGVRTY GFRSPQETYD
VYCYVDHLDG DVFHLTVPSK FTFEEAAKEC ENQDARLATV GELQAAWRNG FDQCDYGWLS
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTGFPPPDSR FDAYCFKPKE ATTIDLSILA
ETASPSLSKE PQMVSDRTTP IIPLVDELPV IPTEFPPVGN IVSFEQKATV QPQAITDSLA
TKLPTPTGST KKPWDMDDYS PSASGPLGKL DISEIKEEVL QSTTGVSHYA TDSWDGVVED
KQTQESVTQI EQIEVGPLVT SMEILKHIPS KEFPVTETPL VTARMILESK TEKKMVSTVS
ELVTTGHYGF TLGEEDDEDR TLTVGSDEST LIFDQIPEVI TVSKTSEDTI HTHLEDLESV
SASTTVSPLI MPDNNGSSMD DWEERQTSGR ITEEFLGKYL STTPFPSQHR TEIELFPYSG
DKILVEGIST VIYPSLQTEM THRRERTETL IPEMRTDTYT DEIQEEITKS PFMGKTEEEV
FSGMKLSTSL SEPIHVTESS VEMTKSFDFP TLITKLSAEP TEVRDMEEDF TATPGTTKYD
ENITTVLLAH GTLSVEAATV SKWSWDEDNT TSKPLESTEP SASSKLPPAL LTTVGMNGKD
KDIPSFTEDG ADEFTLIPDS TQKQLEEVTD EDIAAHGKFT IRFQPTTSTG IAEKSTLRDS
TTEEKVPPIT STEGQVYATM EGSALGEVED VDLSKPVSTV PQFAHTSEVE GLAFVSYSST
QEPTTYVDSS HTIPLSVIPK TDWGVLVPSV PSEDEVLGEP SQDILVIDQT RLEATISPET
MRTTKITEGT TQEEFPWKEQ TAEKPVPALS STAWTPKEAV TPLDEQEGDG SAYTVSEDEL
LTGSERVPVL ETTPVGKIDH SVSYPPGAVT EHKVKTDEVV TLTPRIGPKV SLSPGPEQKY
ETEGSSTTGF TSSLSPFSTH ITQLMEETTT EKTSLEDIDL GSGLFEKPKA TELIEFSTIK
VTVPSDITTA FSSVDRLHTT SAFKPSSAIT KKPPLIDREP GEETTSDMVI IGESTSHVPP
TTLEDIVAKE TETDIDREYF TTSSPPATQP TRPPTVEDKE AFGPQALSTP QPPASTKFHP
DINVYIIEVR ENKTGRMSDL SVIGHPIDSE SKEDEPCSEE TDPVHDLMAE ILPEFPDIIE
IDLYHSEENE EEEEECANAT DVTTTPSVQY INGKHLVTTV PKDPEAAEAR RGQFESVAPS
QNFSDSSESD THPFVIAKTE LSTAVQPNES TETTESLEVT WKPETYPETS EHFSGGEPDV
FPTVPFHEEF ESGTAKKGAE SVTERDTEVG HQAHEHTEPV SLFPEESSGE IAIDQESQKI
AFARATEVTF GEEVEKSTSV TYTPTIVPSS ASAYVSEEEA VTLIGNPWPD DLLSTKESWV
EATPRQVVEL SGSSSIPITE GSGEAEEDED TMFTMVTDLS QRNTTDTLIT LDTSRIITES
FFEVPATTIY PVSEQPSAKV VPTKFVSETD TSEWISSTTV EEKKRKEEEG TTGTASTFEV
YSSTQRSDQL ILPFELESPN VATSSDSGTR KSFMSLTTPT QSEREMTDST PVFTETNTLE
NLGAQTTEHS SIHQPGVQEG LTTLPRSPAS VFMEQGSGEA AADPETTTVS SFSLNVEYAI
QAEKEVAGTL SPHVETTFST EPTGLVLSTV MDRVVAENIT QTSREIVISE RLGEPNYGAE
IRGFSTGFPL EEDFSGDFRE YSTVSHPIAK EETVMMEGSG DAAFRDTQTS PSTVPTSVHI
SHISDSEGPS STMVSTSAFP WEEFTSSAEG SGEQLVTVSS SVVPVLPSAV QKFSGTASSI
IDEGLGEVGT VNEIDRRSTI LPTAEVEGTK APVEKEEVKV SGTVSTNFPQ TIEPAKLWSR
QEVNPVRQEI ESETTSEEQI QEEKSFESPQ NSPATEQTIF DSQTFTETEL KTTDYSVLTT
KKTYSDDKEM KEEDTSLVNM STPDPDANGL ESYTTLPEAT EKSHFFLATA LVTESIPAEH
VVTDSPIKKE ESTKHFPKGM RPTIQESDTE LLFSGLGSGE EVLPTLPTES VNFTEVEQIN
NTLYPHTSQV ESTSSDKIED FNRMENVAKE VGPLVSQTDI FEGSGSVTST TLIEILSDTG
AEGPTVAPLP FSTDIGHPQN QTVRWAEEIQ TSRPQTITEQ DSNKNSSTAE INETTTSSTD
FLARAYGFEM AKEFVTSAPK PSDLYYEPSG EGSGEVDIVD SFHTSATTQA TRQESSTTFV
SDGSLEKHPE VPSAKAVTAD GFPTVSVMLP LHSEQNKSSP DPTSTLSNTV SYERSTDGSF
QDRFREFEDS TLKPNRKKPT ENIIIDLDKE DKDLILTITE STILEILPEL TSDKNTIIDI
DHTKPVYEDI LGMQTDIDTE VPSEPHDSND ESNDDSTQVQ EIYEAAVNLS LTEETFEGSA
DVLASYTQAT HDESMTYEDR SQLDHMGFHF TTGIPAPSTE TELDVLLPTA TSLPIPRKSA
TVIPEIEGIK AEAKALDDMF ESSTLSDGQA IADQSEIIPT LGQFERTQEE YEDKKHAGPS
FQPEFSSGAE EALVDHTPYL SIATTHLMDQ SVTEVPDVME GSNPPYYTDT TLAVSTFAKL
SSQTPSSPLT IYSGSEASGH TEIPQPSALP GIDVGSSVMS PQDSFKEIHV NIEATFKPSS
EEYLHITEPP SLSPDTKLEP SEDDGKPELL EEMEASPTEL IAVEGTEILQ DFQNKTDGQV
SGEAIKMFPT IKTPEAGTVI TTADEIELEG ATQWPHSTSA SATYGVEAGV VPWLSPQTSE
RPTLSSSPEI NPETQAALIR GQDSTIAASE QQVAARILDS NDQATVNPVE FNTEVATPPF
SLLETSNETD FLIGINEESV EGTAIYLPGP DRCKMNPCLN GGTCYPTETS YVCTCVPGYS
GDQCELDFDE CHSNPCRNGA TCVDGFNTFR CLCLPSYVGA LCEQDTETCD YGWHKFQGQC
YKYFAHRRTW DAAERECRLQ GAHLTSILSH EEQMFVNRVG HDYQWIGLND KMFEHDFRWT
DGSTLQYENW RPNQPDSFFS AGEDCVVIIW HENGQWNDVP CNYHLTYTCK KGTVACGQPP
VVENAKTFGK MKPRYEINSL IRYHCKDGFI QRHLPTIRCL GNGRWAIPKI TCMNPSAYQR
TYSMKYFKNS SSAKDNSINT SKHDHRWSRR WQESRR
