function:Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDC2 to switch off endocytosis, One of its substrates would be EPN1/Epsin.,similarity:Contains 1 Rho-GAP domain.,subunit:Interacts with the GTP-bound form of RALA, RALB, CDC42 and RAC1. Interacts with REPS1 and REPS2 and this does not affect the Ral-binding activity. Interacts with DAB2IP. Interacts with catalytically active CCNB1 and CDC2 during mitosis. Interacts with EPN1, NUMB and TFAP2A during interphase and mitosis.,tissue specificity:Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes.,
Cell membrane ; Peripheral membrane protein . Cytoplasm, cytosol . Cytoplasm, cytoskeleton, spindle pole . Nucleus . Mitochondrion . Cytosolic protein that transiently associates with the mitotic spindle poles in early prophase, and dissociates from them after completion of mitosis (By similarity). Targeted to the plasma membrane through its interaction with RALB, directed by FGF signaling. Docking on the membrane is required to transduce the Ral signal (By similarity). Recruited by RALA to the mitochondrion during mitosis where it regulates mitochondrial fission (PubMed:21822277). Nuclear localization is cell cycle dependent while membrane localization is seen in adherent cells (PubMed:22319010). The region involved in membrane association could form transmembrane domains and expose a part of the protein extracellularly (Probable). .
Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes.
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