|PROSITE documentation PDOC00930 [for PROSITE entry PS01210]|
Caveolins [1,2] are a family of integral membrane proteins which are the principal components of caveolae membranes. Cavoleae are flask-shaped plasma membrane invaginations whose exact cellular function is not yet clear. Caveolins may act as scaffolding proteins within caveolar membranes. They interact directly with G-protein α subunits and can functionally regulate their activity.
Currently, three different forms of caveolins are known: caveolin-1 (or VIP21), caveolin-2 and caveolin-3 (or M-caveolin).
Caveolins are proteins of about 20 Kd, they form high molecular mass homo-oligomers. Structurally they seem to have a N-terminal and C-terminal hydrophilic segments and a long central transmembrane domains that probably forms an hairpin in the membrane. Both extremities are known to face the cytoplasm.
As a signature pattern, we selected a perfectly conseerved octapeptide which is located in the N-terminal section of caveolins.Last update:
December 2001 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Tang Z., Scherer P.E., Okamoto T., Song K., Chu K., Kohtz D.S., Nishimoto I., Lodish H.F., Lisanti M.P.|
|Title||Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle.|
|Source||J. Biol. Chem. 271:2255-2261(1996).|
|2||Authors||Scherer P.E., Okamoto T., Chun M., Nishimoto I., Lodish H.F., Lisanti M.P.|
|Title||Identification, sequence, and expression of caveolin-2 defines a caveolin gene family.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 93:131-135(1996).|