Pathways & interactions
Short name: Caveolin_1
- Caveolin (IPR001612)
- Caveolin-1 (IPR015504)
Caveolins [PMID: 8567687, PMID: 8552590] are a family of integral membrane proteins that 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 alpha 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 kDa, they form high molecular mass homo-oligomers. Structurally they seem to have N-terminal and C-terminal hydrophilic segments and a long central transmembrane domain that probably forms a hairpin in the membrane. Both extremities are known to face the cytoplasm.
Caveolin-1 (VIP21) was first identified as a tyrosine-phosphorylated protein in Rous sarcoma virus transformed cells that was enriched in both caveolae and vesicles targeted to the apical surface of polarized epithelial cells. Caveolin-1 has a function in intracellular and extracellular lipid transport [PMID: 12189159].
- PTHR10844:SF5 (PTHR10844:SF5)