Secretory carrier membrane protein 1 (SCAMP1)

Secretory carrier membrane protein 1 (SCAMP1) is a member of the SCAMP family, integral membrane proteins found in secretory and endocytic carrier vesicles, highly conserved across metazoans and plants. SCAMP1 is characterized by a core domain containing four transmembrane spans and three conserved amphiphilic segments, making it structurally similar to tetraspanins. The N- and C-terminal domains are cytoplasmically oriented, and the protein is involved in key processes of membrane trafficking, particularly in the formation and function of secretory granules and vesicles. SCAMP1 is not significantly exposed on the protein ectodomain and instead operates through cytoplasmic interfaces[1][2]. Research indicates its involvement is largely in basic cell biology rather than specific disease mechanisms or as a pharmacological target[1][2].

Other names

Secretory carrier-associated membrane protein 1SCAMPSCAMP37secretory carrier membrane protein 1

Not applicable; no drugs target SCAMP1, so mechanisms of pharmacological action are unknown.