Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane (PubMed:25315773, PubMed:32493773, PubMed:24904167, PubMed:26567335). Major PS-flippase in immune cell subsets. In erythrocyte plasma membrane, it is required to maintain PS in the inner leaflet preventing its exposure on the surface. This asymmetric distribution is critical for the survival of erythrocytes in circulation since externalized PS is a phagocytic signal for erythrocyte clearance by splenic macrophages (PubMed:26944472). Required for B cell differentiation past the pro-B cell stage (By similarity). Seems to mediate PS flipping in pro-B cells (By similarity). May be involved in the transport of cholestatic bile acids (By similarity). ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate The flippase activity is inactivated by caspase-mediated cleavage in apoptotic cells, allowing for PS exposure on the cell surface and engulfment of apoptotic cells by macrophages. The ATPase activity is up-regulated by aminophospholipids PS and PE and down-regulated by Increasing intracellular Ca2+ levels. Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit ATP11C and an accessory beta subunit TMEM30A. Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A. Internalized via clathrin-dependent endocytosis in response to ca(2+) signaling induced by G-protein coupled serotonin and histamine receptors. Widely expressed. The di-leucine motif is required for sorting to clathrin-coated endosomes upon ca(2+)-dependent PRKCA activation. Proteolytically cleaved by CASP3, CASP6 and CASP7. Phosphorylated at Ser-1116 likely by PRKCA; this creates a functional di-leucine motif that is sufficient for endocytosis. The disease is caused by variants affecting the gene represented in this entry. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.