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GRP1 (general receptor for phosphoinositides-1) contains a Pleckstrin homology (PH) domain as well as a Sec7 domain. The PH domain has high binding affinity for phosphatidylinositol 3,4,5-trisphosphate Ptdlns(3,4,5)P3), while the Sec7 homology domain is responsible for catalyzing guanine nucleotide exchange of ADP-ribosylation factor (ARF) proteins. GRP1 co-localizes with ARF6 and catalyzes GTP/GDP exchange on ARF6. It is known to interact with Ptdlns(3,4,5)P3 localized to the plasma membrane in vitro and may also be a Ptdlns(3,4,5)P3 receptor. Additionally, GRP1 may regulate protein sorting and membrane trafficking through interaction with the guanosine triphosphate ARF, and may control cell adhesion through interaction with integrins.
AI648983; ARF nucleotide-binding site opener 3; ARNO3; CLM3; CYTH3; cytohesin 3; cytohesin-3; General receptor of phosphoinositides 1; GRP1; mSec7-3; PH, SEC7 and coiled-coil domain-containing protein 3; pleckstrin homology, Sec7 and coiled/coil domains 3; pleckstrin homology, Sec7 and coiled-coil domains 3; Protein ARNO3; PSCD3; rSec7-3; Sec7; SEC7 homolog C; Sec7C
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