Calcium-binding protein 7 (CABP7)

Calcium-binding protein 7 (CABP7) is a member of the calmodulin-related family of small calcium-binding proteins characterized by four EF-hand motifs and a unique C-terminal transmembrane domain. CABP7 and its close homolog CaBP8 form a distinct subfamily (sometimes called calneurons), localizing predominantly to the Golgi and trans-Golgi network via a tail-anchor mechanism rather than N-myristoylation. The primary known function of CABP7 is to negatively regulate Golgi-to-plasma membrane trafficking by directly inhibiting the lipid kinase PI4KIIIβ in a calcium-dependent manner, thereby influencing the production of phosphatidylinositol 4-phosphate (PI4P) and vesicle transport. CABP7 is also implicated in essential cell processes such as cytokinesis. While structurally and functionally related to calmodulin, CABP7 is not known to directly regulate ion channels or serve as a classic drug target at present, and its roles in human disease are still emerging.

Other names

CaBP7CALN2Calneuron IICalneuron-2MGC57793calneuron 2calneuron II