Abstract
The appearance of phosphatidylserine on the surface of animal cells triggers phagocytosis and blood coagulation. Normally, phosphatidylserine is confined to the inner leaflet of the plasma membrane by an aminophospholipid translocase, which has now been cloned and sequenced. The bovine enzyme is a member of a previously unrecognized subfamily of P-type adenosine triphosphatases (ATPases) that may have diverged from the primordial enzyme before the separation of the known families of ion-translocating ATPases. Studies in Saccharomyces cerevisiae suggest that aminophospholipid translocation is a general function of members of this family.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / isolation & purification
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Adenosine Triphosphatases / metabolism*
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Animals
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Biological Transport
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Cattle
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Cell Membrane / metabolism
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Chromaffin Granules / enzymology
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Cloning, Molecular
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Molecular Sequence Data
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Molecular Weight
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Phosphatidylcholines / metabolism
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Phosphatidylethanolamines / metabolism
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Phosphatidylserines / metabolism
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Phospholipids / metabolism*
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Sequence Homology, Amino Acid
Substances
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Phosphatidylcholines
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Phosphatidylethanolamines
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Phosphatidylserines
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Phospholipids
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Adenosine Triphosphate
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Adenosine Triphosphatases