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Literature summary extracted from

  • Sebastian, T.T.; Baldridge, R.D.; Xu, P.; Graham, T.R.
    Phospholipid flippases: Building asymmetric membranes and transport vesicles (2012), Biochim. Biophys. Acta, 1821, 1068-1077.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.6.2.1 ALIS protein
-
Arabidopsis thaliana
7.6.2.1 CDC50A
-
Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.6.2.1 endosome
-
Homo sapiens 5768
-
7.6.2.1 endosome
-
Saccharomyces cerevisiae 5768
-
7.6.2.1 endosome
-
Arabidopsis thaliana 5768
-
7.6.2.1 endosome
-
Caenorhabditis elegans 5768
-
7.6.2.1 Golgi apparatus
-
Homo sapiens 5794
-
7.6.2.1 Golgi apparatus
-
Saccharomyces cerevisiae 5794
-
7.6.2.1 Golgi apparatus
-
Arabidopsis thaliana 5794
-
7.6.2.1 Golgi apparatus
-
Caenorhabditis elegans 5794
-
7.6.2.1 plasma membrane
-
Homo sapiens 5886
-
7.6.2.1 plasma membrane
-
Saccharomyces cerevisiae 5886
-
7.6.2.1 plasma membrane
-
Arabidopsis thaliana 5886
-
7.6.2.1 plasma membrane
-
Caenorhabditis elegans 5886
-

Organism

EC Number Organism UniProt Comment Textmining
7.6.2.1 Arabidopsis thaliana
-
-
-
7.6.2.1 Caenorhabditis elegans C7U324
-
-
7.6.2.1 Caenorhabditis elegans G5EBH1
-
-
7.6.2.1 Caenorhabditis elegans O18182
-
-
7.6.2.1 Caenorhabditis elegans P91203
-
-
7.6.2.1 Caenorhabditis elegans Q7YXV5
-
-
7.6.2.1 Homo sapiens
-
-
-
7.6.2.1 Saccharomyces cerevisiae
-
-
-
7.6.2.1 Saccharomyces cerevisiae P32660
-
-
7.6.2.1 Saccharomyces cerevisiae P39524
-
-
7.6.2.1 Saccharomyces cerevisiae Q12674
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.6.2.1 blood platelet
-
Homo sapiens
-
7.6.2.1 erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.6.2.1 ATP + H2O + phosphatidylethanolamine/in
-
Homo sapiens ADP + phosphate + phosphatidylethanolamine/out
-
?
7.6.2.1 ATP + H2O + phosphatidylethanolamine/in
-
Saccharomyces cerevisiae ADP + phosphate + phosphatidylethanolamine/out
-
?
7.6.2.1 ATP + H2O + phosphatidylethanolamine/in
-
Arabidopsis thaliana ADP + phosphate + phosphatidylethanolamine/out
-
?
7.6.2.1 ATP + H2O + phosphatidylethanolamine/in
-
Caenorhabditis elegans ADP + phosphate + phosphatidylethanolamine/out
-
?
7.6.2.1 ATP + H2O + phosphatidylserine/in
-
Homo sapiens ADP + phosphate + phosphatidylserine/out
-
?
7.6.2.1 ATP + H2O + phosphatidylserine/in
-
Saccharomyces cerevisiae ADP + phosphate + phosphatidylserine/out
-
?
7.6.2.1 ATP + H2O + phosphatidylserine/in
-
Arabidopsis thaliana ADP + phosphate + phosphatidylserine/out
-
?
7.6.2.1 ATP + H2O + phosphatidylserine/in
-
Caenorhabditis elegans ADP + phosphate + phosphatidylserine/out
-
?

Subunits

EC Number Subunits Comment Organism
7.6.2.1 heterodimer
-
Homo sapiens
7.6.2.1 heterodimer
-
Saccharomyces cerevisiae
7.6.2.1 heterodimer
-
Arabidopsis thaliana
7.6.2.1 heterodimer
-
Caenorhabditis elegans

Synonyms

EC Number Synonyms Comment Organism
7.6.2.1 ALA1
-
Arabidopsis thaliana
7.6.2.1 ALA10
-
Arabidopsis thaliana
7.6.2.1 ALA11
-
Arabidopsis thaliana
7.6.2.1 ALA12
-
Arabidopsis thaliana
7.6.2.1 ALA2
-
Arabidopsis thaliana
7.6.2.1 ALA3
-
Arabidopsis thaliana
7.6.2.1 ALA4
-
Arabidopsis thaliana
7.6.2.1 ALA5
-
Arabidopsis thaliana
7.6.2.1 ALA7
-
Arabidopsis thaliana
7.6.2.1 ALA8
-
Arabidopsis thaliana
7.6.2.1 ALA9
-
Arabidopsis thaliana
7.6.2.1 aminophospholipid ATPase
-
Arabidopsis thaliana
7.6.2.1 aminophospholipid translocase
-
Homo sapiens
7.6.2.1 APLT
-
Homo sapiens
7.6.2.1 ATP10A
-
Homo sapiens
7.6.2.1 ATP10B
-
Homo sapiens
7.6.2.1 ATP10D
-
Homo sapiens
7.6.2.1 ATP11A
-
Homo sapiens
7.6.2.1 ATP11B
-
Homo sapiens
7.6.2.1 ATP11C
-
Homo sapiens
7.6.2.1 ATP8A1
-
Homo sapiens
7.6.2.1 Atp8a2
-
Homo sapiens
7.6.2.1 ATP8B1
-
Homo sapiens
7.6.2.1 ATP8B2
-
Homo sapiens
7.6.2.1 ATP8B3
-
Homo sapiens
7.6.2.1 ATP8B4
-
Homo sapiens
7.6.2.1 ATP8B5
-
Homo sapiens
7.6.2.1 ATP9A
-
Homo sapiens
7.6.2.1 ATP9B
-
Homo sapiens
7.6.2.1 Dnf1 | Drs2 Neo1 family ATPase 1 Saccharomyces cerevisiae
7.6.2.1 Dnf2 Drs2 Neo1 family ATPase 2 Saccharomyces cerevisiae
7.6.2.1 Dnf3 Drs2 Neo1 family ATPase 3 Saccharomyces cerevisiae
7.6.2.1 Drs2 defect in ribosome synthesis 2 Saccharomyces cerevisiae
7.6.2.1 Neo1 neomycin resistance 1 Saccharomyces cerevisiae
7.6.2.1 P4-ATPase
-
Homo sapiens
7.6.2.1 P4-ATPase
-
Saccharomyces cerevisiae
7.6.2.1 P4-ATPase
-
Arabidopsis thaliana
7.6.2.1 P4-ATPase
-
Caenorhabditis elegans
7.6.2.1 phospholipid flippase
-
Homo sapiens
7.6.2.1 phospholipid flippase
-
Saccharomyces cerevisiae
7.6.2.1 phospholipid flippase
-
Arabidopsis thaliana
7.6.2.1 phospholipid flippase
-
Caenorhabditis elegans
7.6.2.1 TAT-2
-
Caenorhabditis elegans
7.6.2.1 TAT-3
-
Caenorhabditis elegans
7.6.2.1 TAT-4
-
Caenorhabditis elegans
7.6.2.1 TAT-5
-
Caenorhabditis elegans
7.6.2.1 TAT-6
-
Caenorhabditis elegans
7.6.2.1 transbilayer amphipath transporter
-
Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
7.6.2.1 malfunction knockdown of ALA1 expression causes a cold-sensitive growth defect in plants Arabidopsis thaliana
7.6.2.1 malfunction P4-ATPase deficiencies are linked to liver disease, obesity, diabetes, hearing loss, neurological deficits, immune deficiency, and reduced fertility Homo sapiens
7.6.2.1 physiological function the enzyme flips phospholipid across the bilayer to create an asymmetric membrane structure with substrate phospholipids, such as phosphatidylserine and phosphatidylethanolamine, enriched within the cytosolic leaflet. Fippase helps to form transport vesicles that bud from Golgi and endosomal membranes Homo sapiens
7.6.2.1 physiological function the enzyme flips phospholipid across the bilayer to create an asymmetric membrane structure with substrate phospholipids, such as phosphatidylserine and phosphatidylethanolamine, enriched within the cytosolic leaflet. Fippase helps to form transport vesicles that bud from Golgi and endosomal membranes Caenorhabditis elegans
7.6.2.1 physiological function the enzyme flips phospholipid across the bilayer to create an asymmetric membrane structure with substrate phospholipids, such as phosphatidylserine and phosphatidylethanolamine, enriched within the cytosolic leaflet. Flippase helps to form transport vesicles that bud from Golgi and endosomal membranes Saccharomyces cerevisiae
7.6.2.1 physiological function the enzyme flips phospholipid across the bilayer to create an asymmetric membrane structure with substrate phospholipids, such as phosphatidylserine and phosphatidylethanolamine, enriched within the cytosolic leaflet. Flippase helps to form transport vesicles that bud from Golgi and endosomal membranes Arabidopsis thaliana