ASAP1
Domain
The PH domain most probably contributes to the phosphoinositide-dependent regulation of ADP ribosylation factors.
Function
Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Part of the ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which direct preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:25673879).
Post-translational modifications
Phosphorylated on tyrosine residues by SRC.
Cellular localization
- Cytoplasm
- Membrane
- Golgi apparatus
- Golgi apparatus
- trans-Golgi network
- Predominantly cytoplasmic. Partially membrane-associated. Localized to the Golgi, TGN and rhodopsin transport carriers (RTC) when interacting with RHO in photoreceptors (PubMed:25673879). Localized to RTC when interacting with RAB11A and RAB11FIP3 in photoreceptors (PubMed:25673879).
Alternative names
DDEF1, KIAA1249, PAG2, ASAP1, ADP-ribosylation factor-directed GTPase-activating protein 1, Development and differentiation-enhancing factor 1, PIP2-dependent ARF1 GAP, ARF GTPase-activating protein 1, DEF-1, Differentiation-enhancing factor 1