Arf-GAP with coiled-coil, ankyrin repeat and PH domains 2 (ACAP2)

Arf-GAP with coiled-coil, ankyrin repeat and PH domains 2 (ACAP2) is a multidomain protein encoded by the *ACAP2* gene in humans and is a member of the centaurin beta family. It functions primarily as an enzyme—specifically a GTPase-activating protein (GAP) for the small GTPase ARF6—participating in the inactivation of ARF6 by enhancing its intrinsic GTPase activity. ACAP2 contains a coiled-coil domain (involved in protein-protein interactions and oligomerization), ankyrin repeats (often mediating protein binding), and a PH (pleckstrin homology) domain that binds specific phosphoinositides in membranes[1][3][6][7][9][11]. ACAP2 binds to the plasma membrane and participates in actin cytoskeleton regulation and membrane trafficking; it also directly interacts with RAB35 through its ankyrin repeats but does not have GAP activity for RAB35[2][9][11]. ACAP2 shows pro-apoptotic activity in cancer cell lines, and its down-regulation has been reported in various human cancers, suggesting a tumor suppressor role[4]. No approved drugs directly target ACAP2, and there are no established clinical biomarkers or safety profiles.

Other names

Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2ACAP2CENTB2KIAA0041CNT-B2Centaurin-beta-2