|PROSITE documentation PDOC00745 [for PROSITE entry PS00964]|
Syndecans [1,2] (from the greek syndein; to bind together) are a family of transmembrane heparan sulfate proteoglycans which are implicated in the binding of extracellular matrix components and growth factors. Syndecans bind a variety of molecules via their heparan sulfate chains and can act as receptors or as co-receptors.
Structurally, these proteins consist of four separate domains:
a) A signal sequence; b) An extracellular domain (ectodomain) of variable length and whose sequence is not evolutionary conserved in the various forms of syndecans. The ectodomain contains the sites of attachment of the heparan sulfate glycosaminoglycan side chains; c) A transmembrane region; d) A highly conserved cytoplasmic domain of about 30 to 35 residues which could interact with cytoskeletal proteins.
The proteins known to belong to this family are:
The signature pattern that we developed for syndecans starts with the last residue of the transmembrane region and includes the first 10 residues of the cytoplasmic domain. This region, which contains four basic residues, could act as a stop transfer site.Expert(s) to contact by email:
November 1997 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Bernfield M. Kokenyesi R. Kato M. Hinkes M.T. Spring J. Gallo R.L. Lose E.J.|
|Title||Biology of the syndecans: a family of transmembrane heparan sulfate proteoglycans.|
|Source||Annu. Rev. Cell Biol. 8:365-393(1992).|
|Title||Integral membrane heparan sulfate proteoglycans.|
|Source||FASEB J. 7:1023-1030(1993).|