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versican core protein; large fibroblast proteoglycan; chondroitin sulfate proteoglycan core protein 2; PG-M; Glial hyaluronate-binding protein; GHAP (VCAN CSPG2)
Function:
- may play a role in intercellular signaling & in connecting cells with the extracellular matrix
- may take part in regulation of cell motility, growth & differentiation
- binds hyaluronic acid
- interacts with FBLN1 (putative)
Structure:
- belongs to the aggrecan/versican proteoglycan family
- contains 1 C-type lectin domain
- contains 2 EGF-like domains
- contains 1 Ig-like V-type domain (immunoglobulin-like)
- contains 2 link domains
- contains 1 Sushi (CCP/SCR) domain
Compartment:
- secreted, extracellular space, extracellular matrix
Alternative splicing: named isoforms=5; V0,V1,V2,V3,vint; Additional isoforms seem to exist
Expression:
- expressed in cerebral white matter
- isoform V0 & isoform V1 are expressed in normal brain, gliomas, medulloblastomas, schwannomas, neurofibromas, & meningiomas
- isoform V2 is restricted to normal brain & gliomas
- isoform V3 is found in all these tissues except medulloblastomas
- expression disappears after cartilage development
Pathology:
- defects in VCAN are the cause of Wagner syndrome type 1
General
matrix protein
proteoglycan core protein
Properties
SIZE: entity length = 3396 aa
MW = 373 kD
COMPARTMENT: extracellular matrix
MOTIF: signal sequence {1-20}
immunoglobulin superfamily domain {21-146}
MOTIF: cysteine residue {C44}
MODIFICATION: cysteine residue {C130}
N-glycosylation site {N57}
cysteine residue {C130}
MODIFICATION: cysteine residue {C44}
Link 1 {150-245}
MOTIF: cysteine residue {C172}
MODIFICATION: cysteine residue {C243}
cysteine residue {C196}
MODIFICATION: cysteine residue {C217}
cysteine residue {C217}
MODIFICATION: cysteine residue {C196}
cysteine residue {C243}
MODIFICATION: cysteine residue {C172}
Link 2 {251-347}
MOTIF: cysteine residue {C270}
MODIFICATION: cysteine residue {C345}
cysteine residue {C294}
MODIFICATION: cysteine residue {C315}
cysteine residue {C315}
MODIFICATION: cysteine residue {C294}
N-glycosylation site {N330}
cysteine residue {C345}
MODIFICATION: cysteine residue {C270}
GAG-alpha (glucosaminoglycan attachment domain) {348-1335}
MOTIF: N-glycosylation site {N615}
N-glycosylation site {N782}
N-glycosylation site {N809}
N-glycosylation site {N1332}
GAG-beta {1336-3089}
MOTIF: N-glycosylation site {N1398}
N-glycosylation site {N1442}
N-glycosylation site {N1468}
N-glycosylation site {N1663}
N-glycosylation site {N1898}
N-glycosylation site {N2179}
N-glycosylation site {N2272}
N-glycosylation site {N2280}
N-glycosylation site {N2360}
N-glycosylation site {N2385}
N-glycosylation site {N2392}
N-glycosylation site {N2496}
N-glycosylation site {N2628}
N-glycosylation site {N2934}
N-glycosylation site {N3067}
EGF domain {3089-3125}
MOTIF: cysteine residue {C3093}
MODIFICATION: cysteine residue {C3104}
cysteine residue {C3098}
MODIFICATION: cysteine residue {C3113}
cysteine residue {C3104}
MODIFICATION: cysteine residue {C3093}
cysteine residue {C3113}
MODIFICATION: cysteine residue {C3098}
cysteine residue {C3115}
MODIFICATION: cysteine residue {C3124}
cysteine residue {C3124}
MODIFICATION: cysteine residue {C3115}
EGF domain {3127-3163}
MOTIF: cysteine residue {C3131}
MODIFICATION: cysteine residue {C3142}
cysteine residue {C3136}
MODIFICATION: cysteine residue {C3151}
cysteine residue {C3142}
MODIFICATION: cysteine residue {C3131}
cysteine residue {C3151}
MODIFICATION: cysteine residue {C3136}
cysteine residue {C3153}
MODIFICATION: cysteine residue {C3162}
cysteine residue {C3162}
MODIFICATION: cysteine residue {C3153}
cysteine residue {C3169}
MODIFICATION: cysteine residue {C3180}
C-type lectin {3176-3290}
MOTIF: cysteine residue {C3180}
MODIFICATION: cysteine residue {C3169}
cysteine residue {C3197}
MODIFICATION: cysteine residue {C3289}
cysteine residue {C3265}
MODIFICATION: cysteine residue {C3281}
cysteine residue {C3281}
MODIFICATION: cysteine residue {C3265}
cysteine residue {C3289}
MODIFICATION: cysteine residue {C3197}
Sushi domain {3294-3354}
MOTIF: cysteine residue {C3296}
MODIFICATION: cysteine residue {C3339}
cysteine residue {C3325}
MODIFICATION: cysteine residue {C3352}
cysteine residue {C3339}
MODIFICATION: cysteine residue {C3296}
cysteine residue {C3352}
MODIFICATION: cysteine residue {C3325}
N-glycosylation site {N3369}
N-glycosylation site {N3379}
Database Correlations
OMIM correlations
UniProt P13611
PFAM correlations
Entrez Gene 1462
Kegg hsa:1462
References
- UniProt :accession P13611
- Functional glycomics gateway - glycan binding - Note: versican
http://www.functionalglycomics.org/glycomics/GBPServlet?&operationtype=view&cbpId=cbp_hum_Ctlect_214
- Ruoslahti E, Yamaguchi Y.
Proteoglycans as modulators of growth factor activities.
Cell. 1991 Mar 8;64(5):867-9. Review.
PMID: 2001586