Recombinant Human Caveolin-3 (CAV3)

Uniprot Id

P56539

Target Species

Human

Target Name

CAV3

Target Full Name

Caveolin-3

Target Function

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. Mediates the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae.

Target Involvement

Limb-girdle muscular dystrophy 1C (LGMD1C); HyperCKmia (HYPCK); Rippling muscle disease 2 (RMD2); Cardiomyopathy, familial hypertrophic (CMH); Long QT syndrome 9 (LQT9); Sudden infant death syndrome (SIDS); Myopathy, distal, Tateyama type (MPDT)

Target Subcellular Location

Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Cell membrane, sarcolemma.

Target Protein Families

Caveolin family

Target Tissue Specificity

Expressed predominantly in muscle.

Target Research Area

Signal Transduction

Target Synonyms

CAV3; CAV3_HUMAN; Caveolin 3; Caveolin-3; LGMD1C; LQT9; M-caveolin; MGC126100; MGC126101; MGC126129; OTTHUMP00000115603; OTTHUMP00000207105; VIP 21; VIP21

Target Background

This gene encodes a caveolin family member, which functions as a component of the caveolae plasma membranes found in most cell types. Caveolin proteins are proposed to be scaffolding proteins for organizing and concentrating certain caveolin-interacting molecules. Mutations identified in this gene lead to interference with protein oligomerization or intra-cellular routing, disrupting caveolae formation and resulting in Limb-Girdle muscular dystrophy type-1C (LGMD-1C), hyperCKemia or rippling muscle disease (RMD). Alternative splicing has been identified for this locus, with inclusion or exclusion of a differentially spliced intron. In addition, transcripts utilize multiple polyA sites and contain two potential translation initiation sites.