Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits (PubMed:9641915, PubMed:9641916). Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase (PubMed:9641915, PubMed:9641916, PubMed:8810315, PubMed:30521495). Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain (PubMed:9641916). This GEF activity is inhibited by binding to activated GNA12 (PubMed:9641916). Mediates angiotensin-2-induced RhoA activation (PubMed:20098430). Interacts with RHOA, GNA12 and GNA13. Homooligomerizes through the coiled coil region. May interact with CCPG1 (By similarity). Interacts with CTNNAL1. Translocated to the membrane by activated GNA13 or LPA stimulation. Ubiquitously expressed. The RGSL domain, also known as rgRGS domain, is necessary but not sufficient for GAP activity. The DH domain is involved in interaction with CCPG1. Phosphorylated by PKCA. Angiotensin-2 induced Tyr-738 phosphorylation is mediated by JAK2. The disease is caused by variants affecting the gene represented in this entry. Contaminating sequence. Sequence of unknown origin in the N-terminal part.