Multifunctional protein that functions as a downstream effector of ralA and ralB (PubMed:15511640). As a GTPase-activating protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase activity. As part of the Ral signaling pathway, may also regulate ligand-dependent EGF and insulin receptors-mediated endocytosis. During mitosis, may act as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase of the cell cycle. During mitosis, also controls mitochondrial fission as an effector of ralA. Recruited to mitochondrion by ralA, acts as a scaffold to foster the mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of DNM1L (By similarity). Acts on the cytoskeleton, to regulate pigment distribution and to regulate gastrulation (PubMed:15511640). Could also function as a primary ATP-dependent active transporter for glutathione conjugates of electrophiles. May also actively catalyze the efflux of a wide range of substrates including xenobiotics like doxorubicin (DOX) contributing to cell multidrug resistance. an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2. ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene C4(out) + phosphate Interacts with the active, GTP-bound form of ralB and ralA. 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 (PubMed:15511640). Nuclear localization is cell cycle dependent while membrane localization is seen in adherent cells (PubMed:22319010). Expressed both maternally and zygotically during oogenesis and early development. The Rho-GAP domain mediates the GTPase activator activity toward CDC42.