EC - Phospholipid-translocating ATPase

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IntEnz Enzyme Nomenclature


Accepted name:
phospholipid-translocating ATPase
Other names:
aminophospholipid-transporting ATPase
phospholipid-transporting ATPase
Systematic name:
ATP phosphohydrolase (phospholipid-flipping)




A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme apparently has several activities, one of them being the movement of phospholipids from one membrane face to the other ('flippase').

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00139
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004012
UniProtKB/Swiss-Prot: (57) [show] [UniProt]


  1. Morris, M.B., Auland, M.E., Xu, Y.H. and Roufogalis, B.D.
    Characterization of the Mg2+-ATPase activity of the human erythrocyte membrane.
    Biochem. Mol. Biol. Int. 31: 823-832 (1993). [PMID: 8136700]
  2. Vermeulen, W.P., Briede, J.J. and Rolofsen, B.
    Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity.
    Mol. Membr. Biol. 13: 95-102 (1996). [PMID: 8839453]
  3. Suzuki, H., Kamakura, M., Morii, M. and Takeguchi, N.
    The phospholipid flippase activity of gastric vesicles.
    J. Biol. Chem. 272: 10429-10434 (1997). [PMID: 9099684]
  4. Auland ME, Roufogalis BD, Devaux PF, Zachowski A.
    Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes.
    Proc. Natl. Acad. Sci. USA 91: 10938-10942 (1994). [PMID: 7971987]
  5. Alder-Baerens, N., Lisman, Q., Luong, L., Pomorski, T., Holthuis, J. C.
    Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles.
    Mol. Biol. Cell 17: 1632-1642 (2006). [PMID: 16452632]
  6. Lopez-Marques, R. L., Poulsen, L. R., Hanisch, S., Meffert, K., Buch-Pedersen, M. J., Jakobsen, M. K., Pomorski, T. G., Palmgren, M. G.
    Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA alpha-subunit.
    Mol. Biol. Cell 21: 791-801 (2010). [PMID: 20053675]

[EC created 2000 (EC created 2000, incorporated 2001)]