May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. May also regulate voltage-gated potassium channels. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity). Mediates the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae (PubMed:19262564). Homooligomer. Interacts with DLG1 and KCNA5; forms a ternary complex. Interacts with TRIM72. Interacts with MUSK; may regulate MUSK signaling. Interacts with DAG1 (via its C-terminal); the interaction prevents binding of DAG1 with DMD (PubMed:10988290). Interacts with DYSF (PubMed:11532985). Interacts with BVES (By similarity). Interacts with CAVIN1 and CAVIN2 (PubMed:24567387). Interacts with CAVIN4 (PubMed:24567387, PubMed:11251997). Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). Expressed predominantly in muscle. Sumoylation with SUMO3 by PIAS4 may reduce agonist-induced internalization and desensitization of adrenergic receptor ABRD2. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Disease susceptibility is associated with variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Belongs to the caveolin family. It is uncertain whether Met-1 or Met-2 is the initiator. Extended N-terminus. Truncated N-terminus. Caveolin-3/LGMD-1C page Caveolin entry