A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Different forms of the enzyme move phospholipids such as phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidyglycerol, sphingomyelin and glucosylceramide from one membrane face to the other ('flippase').
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, phospholipid-flipping)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Different forms of the enzyme move phospholipids such as phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidyglycerol, sphingomyelin and glucosylceramide from one membrane face to the other ('flippase').
selective ATP-dependent transport of phosphatidylserine from the outer to the inner monolayer of the cell membrane to maintain lipid asymmetry in the plasma membrane and secretory vesicles
selective ATP-dependent transport of phosphatidylserine from the outer to the inner monolayer of the cell membrane, exposure of PS on the surface of cells serves as a binding site for haemostatic factors, triggers cell-cell interaction and recognition by macrophages and phospholipases. Exposure of PS on the red cell surface plays a significant role in sickle cell pathology
PLSCR1 acts as signaling molecule and is involved in redistribution of plasma membrane phospholipids triggered by increased cytosolic Ca2+. The enzyme plays a role in apoptosis, lipid metabolism, and thrombosis, and is involved in the Scott syndrome, detailed overview
PLSCR1 acts as signaling molecule and is involved in redistribution of plasma membrane phospholipids triggered by increased cytosolic Ca2+. The enzyme plays a role in apoptosis, lipid metabolism, and thrombosis, and is involved in the Scott syndrome, detailed overview
calcium-induced phospholipid scrambling is bidirectional, reversible and insensitive to phospholipid head group, PLSCR1 is neither sufficient nor necessary for the phosphatidylserine externalization
calcium-induced phospholipid scrambling is bidirectional, reversible and insensitive to phospholipid head group, PLSCR1 is neither sufficient nor necessary for the phosphatidylserine externalization
calcium-induced phospholipid scrambling is bidirectional, reversible and insensitive to phospholipid head group, the scramblase catalyzes the externalization of phosphatidylserine to the cell surface
calcium-induced phospholipid scrambling is bidirectional, reversible and insensitive to phospholipid head group, the scramblase catalyzes the externalization of phosphatidylserine to the cell surface
Atp8a2 flipps fluorescent-labeled phosphatidylserine from the inner leaflet of liposomes, equivalent to the exocytoplasmic leaflet of cell membranes, to the outer leaflet, equivalent to cytoplasmic leaflet, in an ATP-dependent manner
selective ATP-dependent transport of phosphatidylserine from the outer to the inner monolayer of the cell membrane to maintain lipid asymmetry in the plasma membrane and secretory vesicles
selective ATP-dependent transport of phosphatidylserine from the outer to the inner monolayer of the cell membrane, exposure of PS on the surface of cells serves as a binding site for haemostatic factors, triggers cell-cell interaction and recognition by macrophages and phospholipases. Exposure of PS on the red cell surface plays a significant role in sickle cell pathology
PLSCR1 acts as signaling molecule and is involved in redistribution of plasma membrane phospholipids triggered by increased cytosolic Ca2+. The enzyme plays a role in apoptosis, lipid metabolism, and thrombosis, and is involved in the Scott syndrome, detailed overview
PLSCR1 acts as signaling molecule and is involved in redistribution of plasma membrane phospholipids triggered by increased cytosolic Ca2+. The enzyme plays a role in apoptosis, lipid metabolism, and thrombosis, and is involved in the Scott syndrome, detailed overview
Atp8a2 flipps fluorescent-labeled phosphatidylserine from the inner leaflet of liposomes, equivalent to the exocytoplasmic leaflet of cell membranes, to the outer leaflet, equivalent to cytoplasmic leaflet, in an ATP-dependent manner
the secretory granule Atp8a1 is activated by phospholipids binding to a specific site whose properties (PS selectivity, dependence upon glycerol but not serine, stereochemistry, and vanadate sensitivity) are similar to, but distinct from, the properties of the substrate binding site of the plasma membrane flippase, no activation by N-methylphosphatidylserine, phosphatidylserine-O-methyl ester, lysophosphatidylserine, glycerophosphoserine, and phosphoserine, Atp8a1 activities are insensitive to the stereochemistry of the serine headgroup of activating phospholipid
P4-ATPases in general are implicated in the energy-dependent translocation of aminophospholipids across cell membranes. Atp8a2 is implicated in the generation and maintenance of phosphatidylserine asymmetry in photoreceptor disc membranes
the P4-type ATPase ATP11C is redundant during B cell development in the fetal liver, yet essential in the context of adult bone marrow, where it is required for optimal responses to interleukin-7 and sustained expression of Ebf1
PLSCR1 contains a palmitoylation motif as the site of palmitoylation by a thioester linkage to the sulfhydryl groups of cysteines that regulates its trafficking either to nucleus or to the plasma membrane
PLSCR4 contains a palmitoylation motif as the site of palmitoylation by a thioester linkage to the sulfhydryl groups of cysteines that regulates its trafficking either to nucleus or to the plasma membrane
Atp8b1 protein is virtually undetectable in G308V mouse liver, the G308V substitution results in an instable protein that cannot exit the endoplasmic reticulum and is broken down by the proteasome
ATP8B1 deficiency leads to reduced PS flipping and impaired farnesoid X receptor signaling via impaired PKCgamma-mediated nuclear translocation of farnesoid X receptor, resulting in reduced bile salt export pump and enhanced apical sodium-dependent bile salt transporter activation