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.
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).
Immunodeficiency 62
IMD62
An autosomal recessive, primary immunologic disorder characterized by recurrent severe respiratory tract infections and bronchiectasis, due to antibody deficiency. Affected individuals have an abnormal B cell immunophenotype, with low levels of circulating memory B cells.
None
The disease is caused by variants affecting the gene represented in this entry.
Phosphorylated by PKCA. Angiotensin-2 induced Tyr-738 phosphorylation is mediated by JAK2.
Ubiquitously expressed.
Proteins
102435Da
We found 1 product in 1 category