TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*8.A.26.1.1









Calveolin-1 of 178 aas and 2 TMSs.  Caveolae are membrane-budding structures in vertebrate cells, and calveolin-1 forms membrane curvature and endocytic vesicles. Caveolae-like structures can form in E. coli through the expression of caveolin-1.  These caveolae are ~100 nm in diameter and can harbor both animal and bacterial transmembrane proteins (Shin et al. 2015). Molecules from the outside can be taken up into these structures. Transport of fatty acids across the plasma membrane is modulated by caveolin-1 and cholesterol and is not dependent on the putative fatty acid transport proteins, CD36 and FATP (Meshulam et al. 2006).

Eukaryota
Metazoa
Caveolin-1 of Homo sapiens (Q03135)
*8.A.26.1.2









Caveolin-1 (219 aas)

Eukaryota
Metazoa
Caveolin-1 of Xenopus laevis (Q8JHX1)
*8.A.26.1.3









Caveolin-2 (160 aas)

Eukaryota
Metazoa
Caveolin-2 of Xenopus laevis (Q8JHX0)
*8.A.26.1.4









Caveolin-3 (141 aas)

Eukaryota
Metazoa
Caveolin-3 of Xenopus laevis (Q8JHW9)
*8.A.26.1.5









Caveolin-1 of 224 aas.  May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and transport proteins, and can functionally regulate their activities (Li et al. 2014).

Eukaryota
Metazoa
Caveolin-1 of Artemia sinica
*8.A.26.1.6









Caveolin-1, CAV1, of 127 aas and 2 TMSs.  It plays a central role in signal transduction, substrate transport, and membrane trafficking in various cell types. CAV1 also plays an important rolein embryogenesis and host immune defense in disk abalone (Udayantha et al. 2017).

 

Eukaryota
Metazoa
Caveolin-1 of Haliotis discus discus (the disc abalone)