|PROSITE documentation PDOC00927 [for PROSITE entry PS01207]|
Glypicans [1,2] are a family of heparan sulfate proteoglycans which are anchored to cell membranes by a glycosylphosphatidylinositol (GPI) linkage. Structurally, these proteins consist of three separate domains:
a) A signal sequence; b) An extracellular domain of about 500 residues that contains 12 conserved cysteines probably involved in disulfide bonds and which also contains the sites of attachment of the heparan sulfate glycosaminoglycan side chains; c) A C-terminal hydrophobic region which is post-translationally removed after formation of the GPI-anchor.
The proteins known to belong to this family are:
The signature pattern that we developed for glypicans is located in the central section of the extracellular domain and contains five of the conserved cysteines.Last update:
April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Weksberg R., Squire J.A., Templeton D.M.|
|Title||Glypicans: a growing trend.|
|Source||Nat. Genet. 12:225-227(1996).|
|2||Authors||Watanabe K., Yamada H., Yamaguchi Y.|
|Title||K-glypican: a novel GPI-anchored heparan sulfate proteoglycan that is highly expressed in developing brain and kidney.|
|Source||J. Cell Biol. 130:1207-1218(1995).|