ATP11C Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. In the cell membrane of erythrocytes, it is required to maintain phosphatidylserine (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 splenic macrophages. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Required for B cell differentiation past the pro-B cell stage. Seems to mediate PS flipping in pro-B cells. May be involved in the transport of cholestatic bile acids. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. Widely expressed. 4 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.3.1; Hydrolase; Membrane protein, integral; Membrane protein, multi-pass; Transporter; Transporter, ion channel
Chromosomal Location of Human Ortholog: Xq27.1
Cellular Component:  endoplasmic reticulum; endoplasmic reticulum membrane; integral component of membrane; plasma membrane
Molecular Function:  ATP binding; magnesium ion binding; protein binding
Biological Process:  ion transmembrane transport; phospholipid translocation; positive regulation of B cell differentiation; pre-B cell differentiation
Disease: Hemolytic Anemia, Congenital, X-linked
Reference #:  Q8NB49 (UniProtKB)
Alt. Names/Synonyms: AT11C; ATP11C; ATPase class VI type 11C; ATPase IQ; ATPase, class VI, type 11C; ATPIG; ATPIQ; Phospholipid-transporting ATPase IG; Probable phospholipid-transporting ATPase IG
Gene Symbols: ATP11C
Molecular weight: 129,477 Da
Basal Isoelectric point: 6.25  Predict pI for various phosphorylation states
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ATP11C

Protein Structure Not Found.


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