The domain within your query sequence starts at position 15 and ends at position 148; the E-value for the Caveolin domain shown below is 9.5e-61.

KDIHCKEIDLVNRDPKNINEDIVKVDFEDVIAEPEGTYSFDGVWKVSFTTFTVSKYWCYR
LLSTLLGVPLALLWGFLFACISFCHIWAVVPCIKSYLIEIQCISHIYSLCIRTFCNPLFA
ALGQVCSNIKVVLR

Caveolin

Caveolin
PFAM accession number:PF01146
Interpro abstract (IPR001612):

Caveolae are 50-100 nm invaginations located at the plasma membrane of many cell types and are known to transport molecules across endothelial cells [(PUBMED:9759488)]. Caveolae require the caveolin protein for formation. Caveolins may act as scaffolding proteins within caveolar membranes by compartmentalizing and concentrating signalling molecules. Mammals have three caveolin proteins:caveolin-1 (Cav-1, or VIP21), caveolin-2 and caveolin-3 (or M-caveolin). Various classes of signalling molecules, including G-protein subunits, receptor and non-receptor tyrosine kinases, endothelial nitric oxide synthase (eNOS), and small GTPases, bind Cav-1 through its 'caveolin-scaffolding domain' [(PUBMED:23028656)].

Caveolins are proteins of about 20 Kd, 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. Caveolae are enriched with cholesterol and Cav-1 is one of the few proteins that binds cholesterol tightly and specifically.

GO process:caveola assembly (GO:0070836)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Caveolin