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). A caveolin-1 dependent glucose-6-phosphatase trafficking contributes to hepatic glucose production (Gautier-Stein et al. 2023). In an oxidative stress environment, neovascularization within A tumor occurs with structural deterioration and decreased perfusion capacity. One of the main regulatory mechanisms is the migration of extracellular SPARC from the endothelium to intracellular compartments via Caveolin-1 carriers (Zhao et al. 2023).  

Caveolae are distinctive, flask-shaped structures within the cell membrane that play critical roles in cellular signal transduction, ion homeostasis, and mechanosensation. These structures are composed of the caveolin protein family and are enriched in cholesterol and sphingolipids, creating a unique lipid microdomain. Caveolae contribute to the functional regulation of various ion channels through both physical interactions and involvement in complex signaling networks (Huo et al. 2025). Ion channels localized within caveolae are involved in critical cellular processes such as the generation and propagation of action potentials, cellular responses to mechanical forces, and regulation of metabolism. Dysregulation of caveolae function has been linked to the development of various diseases, including cardiovascular disorders, neurodegenerative diseases, metabolic syndrome, and cancer (Huo et al. 2025).


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









Caveolin-1 of 219 aas with two possible TMSs, N- and C-terminal. Caveolin 1 is required for axonal outgrowth of motor neurons and affects Xenopus neuromuscular development (Breuer et al. 2020).

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









Caveolin-2 (160 aas)

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









Caveolin-3 (141 aas)

Eukaryota
Metazoa, Chordata
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, Arthropoda
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, Mollusca
Caveolin-1 of Haliotis discus discus (the disc abalone)
8.A.26.1.7









A CAV3 microdeletion differentially affects skeletal muscle and the myocardium. Intrafamilial phenotypic heterogeneity is associated with caveolin-3 Phe97 microdeletion. The molecular network interacting with caveolin-3 in skeletal muscle and heart may differ (Cagliani et al. 2003). It may act as a scaffolding protein within caveolar membranes and interacts directly with G-protein alpha subunits and can functionally regulate their activity. It may also regulate voltage-gated potassium channels. It plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress. It mediates the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae (McMahon et al. 2009).

Eukaryota
Metazoa, Chordata
CAV3 of Homo sapiens