Copine-1 (CPNE1)

Copine-1 is a highly conserved, calcium-dependent, phospholipid-binding intracellular protein encoded by the CPNE1 gene and found broadly in mammalian tissues[1][2][3][4]. It contains two N-terminal C2 domains, responsible for Ca²⁺-dependent phospholipid-binding, and one C-terminal von Willebrand factor A (VWA) domain, which can mediate protein-protein interactions[1][2][3][4]. Copine-1 plays key regulatory roles at the interface of the cell membrane and cytoplasm, functioning in intracellular events such as signal transduction, membrane trafficking, cell proliferation, apoptosis, immune regulation, neuronal differentiation, autophagy, and gene transcription[1][2][3][4]. High expression and genetic dysregulation of CPNE1 are linked to the development, prognosis, and progression of multiple cancer types—including prostate, lung, breast, liver, thyroid, osteosarcoma, and colorectal cancer—often by regulating AKT, MAPK, TNF-α/NF-κB, and TGF-beta pathways[1][2][4]. Additionally, CPNE1 expression has been proposed as a prognostic or diagnostic biomarker in several cancers and is associated with immune infiltration during hepatocarcinogenesis[2]. There are no known therapeutics directly targeting Copine-1, nor established safety concerns, but its proto-oncogenic role makes it a candidate for future cancer drug development[2][4].

Other names

Copine 1CPN1Chromobindin 17Copine ICOPN1copine-1chromobindin 17copine I