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Information on EC 7.6.2.1 - P-type phospholipid transporter and Organism(s) Homo sapiens and UniProt Accession P98198

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IUBMB Comments
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').
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This record set is specific for:
Homo sapiens
UNIPROT: P98198
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
mg2+-atpase, abcb4, flippase, plscr1, atp8b1, scramblase, aminophospholipid translocase, ala12, tat-2, drs2p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ABCB1
-
-
ABCB4
-
-
aminophospholipid flippase
aminophospholipid flippase 10
-
-
-
-
aminophospholipid flippase 11
-
-
-
-
aminophospholipid flippase 12
-
-
-
-
aminophospholipid scramblase
-
-
aminophospholipid translocase
aminophospholipid translocase VC
-
-
-
-
aminophospholipid transporter
-
aminophosphoplipid translocase
-
-
ATP-dependent specific phospholipid flippase
-
-
ATP-independent flippase
-
-
ATP10A
ATP10B
ATP10D
ATP11A
ATP11C
ATP8A1
Atp8a2
ATP8B1
ATP8B2
-
-
ATP8B3
-
-
ATP8B4
-
-
ATP8B5
-
-
ATP9A
ATPase II
ATPVC
-
-
-
-
ATPVD
-
-
-
-
EpsE
-
-
flippase
HUSSY-20
-
-
-
-
MDR3 P-glycoprotein
-
-
Mg2+-ATPase
-
-
-
-
Mg2+-ATPase A
-
-
-
-
multidrug resistance 3 P-glycoprotein
-
-
P-glycoprotein
-
-
P4-ATPase
PC-flippase
-
phosphatidylserine flippase
-
phosphatidylserine translocase/ATPase
-
-
phospholipid flippase
phospholipid scramblase 1
-
-
phospholipid scramblase 3
-
-
phospholipid scrambling activity
-
-
phospholipid translocase
-
PLS3
-
-
PLSCR1
PS-flippase
-
scramblase
type II secretion ATPase
-
-
type IV P-type ATPase
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + phospholipid [side 1] = ADP + phosphate + phospholipid [side 2]
show the reaction diagram
P-type ATPase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
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').
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + phosphatidylcholine/in
ADP + phosphate + phosphatidylcholine/out
show the reaction diagram
preferred substrate
-
-
?
1-lauroyl-2-(1'-pyrenebutyroyl)-sn-glycero-3-phosphocholine/in
1-lauroyl-2-(1'-pyrenebutyroyl)-sn-glycero-3-phosphocholine/out
show the reaction diagram
-
i.e. pyrene-10-PC, development of a transbilayer lipid flip-flop assay in PLS3 proteoliposomes, overview
-
-
r
acetyl phosphate + H2O
acetate + phosphate
show the reaction diagram
-
translocation of phosphatidylserine from the outer to the inner leaflet of resealed erythrocyte ghosts
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O + 1-palmitoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycero-3-phospho-L-serine/in
ADP + phosphate + 1-palmitoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycero-3-phospho-L-serine/out
show the reaction diagram
-
-
-
?
ATP + H2O + 7-nitrobenz-2-oxa-1,3-diazol-4-yl-phosphatidylserine/in
ADP + phosphate + 7-nitrobenz-2-oxa-1,3-diazol-4-yl-phosphatidylserine/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + asolectin/out
ADP + phosphate + asolectin/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + carboxyfluoresceinyl-phosphatidylserine/in
ADP + phosphate + carboxyfluoresceinyl-phosphatidylserine/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + coumaryl-phosphatidylserine/in
ADP + phosphate + coumaryl-phosphatidylserine/out
show the reaction diagram
-
-
-
-
?
ATP + H2O + galactocerebroside/out
ADP + phosphate + galactocerebroside/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + lactocerebroside/out
ADP + phosphate + lactocerebroside/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + N-methyl-dilauroylphosphatidyl-DL-serine/out
ADP + phosphate + N-methyl-dilauroylphosphatidyl-DL-serine/in
show the reaction diagram
-
rapid change of cell morphology from echinocyte to stomatocyte
-
-
?
ATP + H2O + phosphatidylcholine/in
ADP + phosphate + phosphatidylcholine/out
show the reaction diagram
ATP + H2O + phosphatidylcholine[side 1]
ADP + phosphate + phosphatidylcholine[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + phosphatidylethanolamine/in
ADP + phosphate + phosphatidylethanolamine/out
show the reaction diagram
ATP + H2O + phosphatidylethanolamine/out
ADP + phosphate + phosphatidylethanolamine/in
show the reaction diagram
ATP + H2O + phosphatidylethanolamine[side 1]
ADP + phosphate + phosphatidylethanolamine[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + phosphatidylserine/in
ADP + phosphate + phosphatidylserine/out
show the reaction diagram
ATP + H2O + phosphatidylserine/out
ADP + phosphate + phosphatidylserine/in
show the reaction diagram
ATP + H2O + phosphatidylserine[side 1]
ADP + phosphate + phosphatidylserine[side 2]
show the reaction diagram
ATP + H2O + phosphoethanolamine/in
ADP + phosphate + phosphoethanolamine/out
show the reaction diagram
-
low activity
-
-
?
ATP + H2O + phospholipid/in
ADP + phosphate + phospholipid/out
show the reaction diagram
-
-
-
?
ATP + H2O + phospholipid[side 1]
ADP + phosphate + phospholipid[side 2]
show the reaction diagram
-
-
-
-
?
ATP + H2O + rhodamine 123/out
ADP + phosphate + rhodamine 123/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + sn-1,2-dilauroylphosphatidyl-D-serine/out
ADP + phosphate + sn-1,2-dilauroylphosphatidyl-D-serine/in
show the reaction diagram
-
rapid change of cell morphology from echinocyte to stomatocyte
-
-
?
ATP + H2O + sn-1,2-dilauroylphosphatidyl-L-serine/out
ADP + phosphate + sn-1,2-dilauroylphosphatidyl-L-serine/in
show the reaction diagram
-
rapid change of cell morphology from echinocyte to stomatocyte
-
-
?
ATP + H2O + sn-2,3-dilauroylphosphatidyl-L-serine/out
ADP + phosphate + sn-2,3-dilauroylphosphatidyl-L-serine/in
show the reaction diagram
-
low activity, slow change of cell morphology from echinocyte to stomatocyte
-
-
?
ATP + H2O + sphingomyelin/out
ADP + phosphate + sphingomyelin/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + verapamil/out
ADP + phosphate + verapamil/in
show the reaction diagram
-
highest activity
-
-
?
dATP + H2O
dADP + H2O
show the reaction diagram
fluorescent labeled phosphatidylserine/outer leaflet + ATP + H2O
fluorescent labeled phosphatidylserine/inner leaflet + ADP + phosphate
show the reaction diagram
-
enzyme specifically transports phosphatidylserine from the outer to the inner leaflet of the plasma membrane
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
at 2 mM, 40% of the activity with 2 mM ATP
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
translocation of phosphatidylserine from the outer to the inner leaflet of resealed erythrocyte ghosts
-
-
?
phosphatidylcholine/out
phosphatidylcholine/in
show the reaction diagram
-
-
-
-
?
phosphatidylserine/in
phosphatidylserine/out
show the reaction diagram
-
-
-
-
?
phosphatidylserine/out
phosphatidylserine/in
show the reaction diagram
phospholipid/in
phospholipid/out
show the reaction diagram
-
unspecific bidirectional transmembrane transport of phospholipids
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O + phosphatidylcholine[side 1]
ADP + phosphate + phosphatidylcholine[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + phosphatidylethanolamine/out
ADP + phosphate + phosphatidylethanolamine/in
show the reaction diagram
ATP + H2O + phosphatidylethanolamine[side 1]
ADP + phosphate + phosphatidylethanolamine[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + phosphatidylserine/in
ADP + phosphate + phosphatidylserine/out
show the reaction diagram
ATP + H2O + phosphatidylserine/out
ADP + phosphate + phosphatidylserine/in
show the reaction diagram
ATP + H2O + phosphatidylserine[side 1]
ADP + phosphate + phosphatidylserine[side 2]
show the reaction diagram
ATP + H2O + phosphoethanolamine/in
ADP + phosphate + phosphoethanolamine/out
show the reaction diagram
-
low activity
-
-
?
ATP + H2O + phospholipid/in
ADP + phosphate + phospholipid/out
show the reaction diagram
-
-
-
?
ATP + H2O + phospholipid[side 1]
ADP + phosphate + phospholipid[side 2]
show the reaction diagram
-
-
-
-
?
phosphatidylcholine/out
phosphatidylcholine/in
show the reaction diagram
-
-
-
-
?
phosphatidylserine/in
phosphatidylserine/out
show the reaction diagram
-
-
-
-
?
phosphatidylserine/out
phosphatidylserine/in
show the reaction diagram
-
bidirectional transport, the enzyme controls the level of phosphatidylserine exposed to the platelet surface antagonizing to the aminophospholipid translocase activity, overview
-
-
r
phospholipid/in
phospholipid/out
show the reaction diagram
-
unspecific bidirectional transmembrane transport of phospholipids
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
addition of Ca2+ to the incubation medium does not cause a significant increase in the scramblase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-monoolein
-
0.5 mM significantly reduce the P-glycoprotein protein expression, 0.1 mM of 1-monoolein does not have any significant effect on the expression of P-glycoprotein
1-monostearin
-
0.5 mM significantly reduce the P-glycoprotein protein expression, 0.1 mM of 1-monostearin does not have any significant effect on the expression of P-glycoprotein
azide
-
-
Bcl-2
-
PLS3 and tBid may form a bidirectional positive feedback loop that is antagonized by Bcl-2
-
Cd2+
-
-
Diamide
-
-
DTNB
-
-
EDTA
-
-
elaiophylin
-
partial inhibition of Mg+-ATPase activity, translocation of phosphatidylserine is almost completely abolished
eosin Y
-
almost complete inhibition of both Mg2+-ATPase activity and translocation
orthovanadate
-
-
pyridyldithioethylamine
-
-
ribavirin
-
prolonged treatment of erythrocytes with ribavirin results in surface exposure of phosphatidylserine, mainly caused by inactivation of the aminophospholipid translocase. Inactivation is due to severe ATP depletion
S-nitroso-L-cysteine-ethyl ester
-
i.e. SNCEE, causes intracellular and extracellular trans-nitrosylation of proteins, respectively. Nitrosative stress inhibits the enzyme, and SNCEE causes significant S-nitrosylation/oxidation of thiols in HL-60 cells. SNCEE also strongly inhibites APLT, activated scramblase, and causes PS externalization, reversible by DTT
suramin
-
competitive inhibitor of ATP towards both Mg2+-ATPase activity and aminophospholipid translocation. Inhibition of translocation occurs at higher inhibitor concentration than the inhibition of Mg2+-ATPase activity
vanadate
vanadyl ion
-
inhibits the enzyme from the extracellular surface
verapamil
-
complete inhibition at 0.05 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-aminonaphthalene-8-sulfonate
-
stimulates
1-heptanesulfonate
-
stimulates
2,4-dinitrophenol
-
stimulates, stimulation is prevented by 0.2-1.0 mM Ca2+
4-Aminosalicylate
-
stimulates
ATP
-
biphasic activation, K0.5 = 0.02 mM and 0.4 mM
benzoate
-
stimulates
Brij
-
stimulates
-
CDC50 proteins
CDC50A and CDC50B, cloning and expression of the abut 60 kDa proteins, required for full translocase activity, 2.5-5fold activition, proteins are pivotal factors in the trafficking of ATP8B1 to the plasma membrane and thus may be essential determinants of ATP8B1-related disease, physical interacion with ATP8B1, overview
-
CDC50A
-
-
-
cholate
dithiothreitol
-
partially stimulates
glycerophosphoserine
-
prevents transport of phosphatidylserine
glycocholate
-
slightly increases the efflux of phospholipids and cholesterol from cells
p-hydroxyphenylacetate
-
stimulates
p-nitrophenol
-
stimulates
phenylacylbromide
-
-
Phenylglyoxal
-
-
salicylate
-
stimulates
SDS
-
stimulates
sulfanilamide
-
stimulates
Sulfanilic acid
-
stimulates
taurocholate
-
increases the efflux of phospholipids and cholesterol from cells, the taurocholate monomer plays an important role in ABCB4-mediated lipid secretion
tBid
-
PLS3 and tBid may form a bidirectional positive feedback loop that is antagonized by Bcl-2
-
Tetradecyltrimethylammonium bromide
-
stimulates
thrombin
-
induces platelet phosphatidylserine exposure, inhibited by c7E3 or SR121566
-
Triton X-100
-
stimulates
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.03 - 1.31
acetyl phosphate
0.211 - 0.704
ATP
1.17 - 1.46
p-nitrophenyl phosphate
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 55
purified lipid-stimulated enzyme, pH 7.5, 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
flippase assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
below 4°C transport of phospholipids is inhibited in both erythrocytes and fibroblasts, warming to 7°C activates transport in fibroblasts
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the predominant P4 ATPases in pure pancreatic beta cells and pancreatic islets are ATP8B1, ATP8B2, and ATP9A
Manually annotated by BRENDA team
-
promyelocytic leukemia cells
Manually annotated by BRENDA team
outer segment disc membranes of rod and cone photoreceptor cells, high expression of atp8a2
Manually annotated by BRENDA team
high expression of atp8a2
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
ATP9A localizes to endosomes and the trans-Golgi network, whereas ATP9B localizes exclusively to the trans-Golgi network. The N-terminal cytoplasmic region ofATP9B is required for its Golgi localization
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
gene silencing of individual P4 ATPases and CDC50A inhibits glucose-stimulated insulin release in pure beta cells and in human pancreatic islets
evolution
-
type IV P-type ATPases, P4-ATPases, are putative phospholipid flippases that translocate phospholipids from the exoplasmic (lumenal) to the cytoplasmic leaflet of lipid bilayers and function in complex with CDC50 proteins. Class 5, ATP10A, ATP10B, and ATP10D, and class 6, ATP11A, ATP11B, and ATP11C, P4-ATPases require CDC50 proteins, primarily CDC50A, for their exit from the endoplasmic reticulum and final subcellular localization. In contrast, class 2 P4-ATPases, ATP9A and ATP9B, are able to exit the endoplasmic reticulum in the absence of exogenous CDC50 expression: ATP9B, but not ATP11B, was able to exit the ER despite depletion of CDC50 proteins
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AT8B2_HUMAN
1209
9
137440
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
x * 110000, SDS-PAGE
115000
-
-
132000
x * 132000, about, recombinant enzyme, SDS-PAGE
140000
-
x * 140000, recombinant ABCB4, SDS-PAGE
170000
-
SDS-PAGE
37000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
analysis of glycosylation of ABCB4, cleavage by endoglycosidase H or peptide N-glycosidase F, overview
lipoprotein
phosphoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E203Q
the mutant lacks ATPase activity
F258V
-
site-directed mutagenesis, mutation of the calcium binding motif abolishes the lipid flip-flop activity of PLS3, a dominant negative mutant of PLS3, expression of the PLS3(F258V) mutant in HEK-293 cells results in a phenotype still consistent with low PLS3 activity despite the presence of normal PLS3 in these cells due to spontaneous rate of flip-flop
I376M
missense mutation identified in a patient with cerebellar ataxia, mental retardation and dysequilibrium syndrome. The mutation lies in a highly conserved C-terminal transmembrane region of E1 E2 ATPase domain
K1075M
-
site-directed mutagenesis in the Walker A motif results in an inactive mutant
K435M
-
site-directed mutagenesis in the Walker A motif results in an inactive mutant
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is very instable and rapidly degenerated during purification
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 35 days, stored erythrocytes show nearly no enzyme activity, but the activity can be restored, overview
-
4°C, 35 days, stored erythrocytes show pH-dependently reduced flippase activity and ATP depletion, upon ATP supply the activity can be restored, overview
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
-
partially from erythrocytes
-
recombinant enzyme from HEK-293 cells by immunoaffinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence analysis, PLSCR1, PLSCR2 and PLSCR4 are closely clustered on the small arm of chromosome 3q23
DNA and amino acid sequence analysis, PLSCR1, PLSCR2 and PLSCR4 are closely clustered on the small arm of chromosome 3q23. The region comprising residues M86-E118 in PLSCR1 interacts with the promoter of inositol 1,4,5-triphosphate receptor type 1
DNA and amino acid sequence analysis, PLSCR3 is localized to chromosome 17
expressed in HeLa cells
gene atp8a2, DNA and amino acid sequence determination and analysis, expression in HEK-293 cells
isolated stable expression of N-terminally GFP-tagged ATP8B1 in UPS-1 cells, a nonpolarized CHO-K1 mutant cell line with a defect in the nonendocytic uptake of the NBD-PS analogue, by lentiviral transduction leading to protein localization in the endoplasmic reticulum, co-expression with N-terminally HA-tagged CDC50 proteins results in relocalization of ATP8B1 from the endoplasmic reticulum to the plasma membrane, natural phosphatidylserine exposure in the outer leaflet of the plasma membrane was reduced by 17%-25% in cells coexpressing ATP8B1 and CDC50 proteins in comparison with cells expressing ATP8B1 alone, coexpression of ATP8B1 and CDC50A in WIF-B9 cells resulted in colocalization of both proteins in the canalicular membrane, overview
PLSCR1 DNA and amino acid sequence determination and analysis, co-expression of PLSCR1 as maltose-binding-protein fusion protein and GST-tagged DNA topoisomerase II in Escherichia coli strain BL21(DE3), expression of a human B lymphocyte library, ATCC 87003, and DNA topoisomerase II from HeLa cells in the yeast two hybrid system, interaction analysis, identification of PLSCR1 as binding protein, overview
-
stable expression of ABCB4 in HEK-293 cells
-
transient expression of of different combinations of C-terminally HA-tagged P4-ATPase ATP9A or ATP9B and an N-terminally FLAG-tagged CDC50 construct in HeLa cells, overview. Neither ATP9A nor ATP9B forms a stable complex with CDC50 proteins in the cell
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
coexpression of CDC50A increased the total cellular expression level of flippase ATP8A1
phospholipid flippase ATP11C is endocytosed and downregulated following Ca2+-mediated protein kinase C activation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
assay for phospholipid flippase activities of plasma membrane-localized P4-ATPases using human cell lines stably expressing isoforms ATP8B1, ATP8B2, ATP11A, and ATP11C
analysis
assay for phospholipid flippase activities of plasma membrane-localized P4-ATPases using human cell lines stably expressing isoforms ATP8B1, ATP8B2, ATP11A, and ATP11C
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vermeulen, W.P.; Briede, J.J.; Roelofsen, B.
Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg-ATPase activity
Mol. Membr. Biol.
13
95-102
1996
Homo sapiens
Manually annotated by BRENDA team
Morris, M.B.; Auland, M.E.; Xu, Y.H.; Roufogalis, B.D.
Characterization of the Mg2+-ATPase activity of the human erythrocyte membrane
Biochem. Mol. Biol. Int.
31
823-832
1993
Homo sapiens
Manually annotated by BRENDA team
Beleznay, Z.; Zachowski, A.; Devaux, P.F.; Ott, P.
Characterization of the correlation between ATP-dependent aminophospholipid translocation and Mg2+-ATPase activity in red blood cell membranes
Eur. J. Biochem.
243
58-65
1997
Homo sapiens
Manually annotated by BRENDA team
Bartosz, G.; Batosz, M.; Sokal, A.; Gebicki, J.M.
Stimulation of erythrocyte membrane Mg2+-ATPase activity by dinitrophenol and other membrane-disturbing agents
Biochem. Mol. Biol. Int.
34
521-529
1994
Homo sapiens
Manually annotated by BRENDA team
Daleke, D.L.; Lyles, J.V.
Identification and purification of aminophospholipid flippases
Biochim. Biophys. Acta
1486
108-127
2000
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Beleznay, Z.; Zachowski, A.; Devaux, P.F.; Navazo, M.P.; Ott, P.
ATP-dependent aminophospholipid translocation in erythrocyte vesicles: stoichiometry of transport
Biochemistry
32
3146-3152
1993
Homo sapiens
Manually annotated by BRENDA team
Devaux, P.F.; Zachowski, A.; Morrot, G.; Cribier, S.; Fellmann, P.; Geldwerth, D.; Bitbol, M.; Herve, P.
Control of the transmembrane phospholipid distribution in eukaryotic cells by aminophospholipid translocase
Biotechnol. Appl. Biochem.
12
517-522
1990
Bos taurus, Cavia porcellus, Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Auland, M.E.; Morris, M.B.; Roufogalis, B.D.
Separation and characterization of two Mg2+-ATpase activities from human erythrocyte membrane
Arch. Biochem. Biophys.
312
272-277
1994
Homo sapiens
Manually annotated by BRENDA team
Auland, M.E.; Roufogalis, B.D.; Devaux, P.F.; Zachowski, A.
Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes
Proc. Natl. Acad. Sci. USA
91
10938-10942
1994
Homo sapiens
Manually annotated by BRENDA team
Middelkoop, E.; van der Hoek, E.E.; Bevers, E.M.; Comfurius, P.; Slotboom, A.J.; op den Kamp, J.A.F.; Lubin, B.H.; Zwaal, R.F.A.; Roelofsen, B.
Involvement of ATP-dependent aminophospholipid translocation in maintaining phospholipid asymmetry in diamide-treated human erythrocytes
Biochim. Biophys. Acta
981
151-160
1989
Homo sapiens
Manually annotated by BRENDA team
Connor, J.; Schroit, A.J.
Transbilayer, movement of phosphatidylserine in erythrocytes. Inhibitors of aminophospholipid transport block the association of photolabeled lipid to its transporter
Biochim. Biophys. Acta
1066
37-42
1991
Homo sapiens
Manually annotated by BRENDA team
Herzing, L.B.; Kim, S.J.; Cook, E.H., Jr.; Ledbetter, D.H.
The human aminophospholipid-transporting ATPase gene ATP10C maps adjacent to UBE3A and exhibits similar imprinted expression
Am. J. Hum. Genet.
68
1501-1505
2001
Homo sapiens (O60312)
Manually annotated by BRENDA team
Wolfs, J.L.; Comfurius, P.; Rasmussen, J.T.; Keuren, J.F.; Lindhout, T.; Zwaal, R.F.; Bevers, E.M.
Activated scramblase and inhibited aminophospholipid translocase cause phosphatidylserine exposure in a distinct platelet fraction
Cell. Mol. Life Sci.
62
1514-1525
2005
Homo sapiens
Manually annotated by BRENDA team
Devaux, P.F.; Lopez-MOntero, I.; Bryde, S.
Proteins involved in lipid translocation in eukaryotic cells
Chem. Phys. Lipids
141
119-132
2006
Bos taurus, Saccharomyces cerevisiae, Homo sapiens, Leishmania infantum, Rattus norvegicus
Manually annotated by BRENDA team
Camberg, J.L.; Sandkvist, M.
Molecular analysis of the Vibrio cholerae type II secretion ATPase EpsE
J. Bacteriol.
187
249-256
2005
Homo sapiens
Manually annotated by BRENDA team
Verhoeven, A.J.; Hilarius, P.M.; Dekkers, D.W.; Lagerberg, J.W.; de Korte, D.
Prolonged storage of red blood cells affects aminophospholipid translocase activity
Vox Sang.
91
244-251
2006
Homo sapiens
Manually annotated by BRENDA team
Sahu, S.K.; Gummadi, S.N.; Manoj, N.; Aradhyam, G.K.
Phospholipid scramblases: an overview
Arch. Biochem. Biophys.
462
103-114
2007
Homo sapiens (O15162), Homo sapiens (Q9NRQ2), Homo sapiens (Q9NRY6), Homo sapiens (Q9NRY7), Mus musculus (P58196), Mus musculus (Q9JJ00), Caenorhabditis elegans (Q21318)
Manually annotated by BRENDA team
Smriti, T.; Nemergut, E.C.; Daleke, D.L.
ATP-dependent transport of phosphatidylserine analogues in human erythrocytes
Biochemistry
46
2249-2259
2007
Homo sapiens
Manually annotated by BRENDA team
Liu, J.; Epand, R.F.; Durrant, D.; Grossman, D.; Chi, N.W.; Epand, R.M.; Lee, R.M.
Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis
Biochemistry
47
4518-4529
2008
Homo sapiens
Manually annotated by BRENDA team
Razmara, M.; Hu, H.; Masquelier, M.; Li, N.
Glycoprotein IIb/IIIa blockade inhibits platelet aminophospholipid exposure by potentiating translocase and attenuating scramblase activity
Cell. Mol. Life Sci.
64
999-1008
2007
Homo sapiens
Manually annotated by BRENDA team
Regev, R.; Katzir, H.; Yeheskely-Hayon, D.; Eytan, G.D.
Modulation of P-glycoprotein-mediated multidrug resistance by acceleration of passive drug permeation across the plasma membrane
FEBS J.
274
6204-6214
2007
Homo sapiens (O43520)
Manually annotated by BRENDA team
Morita, S.Y.; Kobayashi, A.; Takanezawa, Y.; Kioka, N.; Handa, T.; Arai, H.; Matsuo, M.; Ueda, K.
Bile salt-dependent efflux of cellular phospholipids mediated by ATP binding cassette protein B4
Hepatology
46
188-199
2007
Homo sapiens
Manually annotated by BRENDA team
Tyurina, Y.Y.; Basova, L.V.; Konduru, N.V.; Tyurin, V.A.; Potapovich, A.I.; Cai, P.; Bayir, H.; Stoyanovsky, D.; Pitt, B.R.; Shvedova, A.A.; Fadeel, B.; Kagan, V.E.
Nitrosative stress inhibits the aminophospholipid translocase resulting in phosphatidylserine externalization and macrophage engulfment: implications for the resolution of inflammation
J. Biol. Chem.
282
8498-8509
2007
Homo sapiens
Manually annotated by BRENDA team
Leung, R.; Gwozdz, A.M.; Wang, H.; Bang, K.W.; Packham, M.A.; Freedman, J.; Rand, M.L.
Persistence of procoagulant surface expression on activated human platelets: involvement of apoptosis and aminophospholipid translocase activity
J. Thromb. Haemost.
5
560-570
2007
Homo sapiens
Manually annotated by BRENDA team
Wyles, J.P.; Wu, Z.; Mirski, S.E.; Cole, S.P.
Nuclear interactions of topoisomerase II alpha and beta with phospholipid scramblase 1
Nucleic Acids Res.
35
4076-4085
2007
Homo sapiens
Manually annotated by BRENDA team
Masuda, M.; Nakai, E.; Mizutani, T.
Study of oxidized lipids as endogenous substrates of P-gp (ABCB1)
Drug Metab. Lett.
2
238-244
2008
Homo sapiens
Manually annotated by BRENDA team
Barta, C.A.; Sachs-Barrable, K.; Feng, F.; Wasan, K.M.
Effects of monoglycerides on P-glycoprotein: modulation of the activity and expression in Caco-2 cell monolayers
Mol. Pharm.
5
863-875
2008
Homo sapiens
Manually annotated by BRENDA team
Barber, L.A.; Palascak, M.B.; Joiner, C.H.; Franco, R.S.
Aminophospholipid translocase and phospholipid scramblase activities in sickle erythrocyte subpopulations
Br. J. Haematol.
146
447-455
2009
Homo sapiens
Manually annotated by BRENDA team
Coleman, J.A.; Kwok, M.C.; Molday, R.S.
Localization, purification, and functional reconstitution of the P4-ATPase Atp8a2, a phosphatidylserine flippase in photoreceptor disc membranes
J. Biol. Chem.
284
32670-32679
2009
Bos taurus (C7EXK4), Mus musculus (P98200), Homo sapiens (Q9NTI2)
Manually annotated by BRENDA team
Sebastian, T.T.; Baldridge, R.D.; Xu, P.; Graham, T.R.
Phospholipid flippases: Building asymmetric membranes and transport vesicles
Biochim. Biophys. Acta
1821
1068-1077
2012
Arabidopsis thaliana, Saccharomyces cerevisiae, Saccharomyces cerevisiae (P32660), Saccharomyces cerevisiae (P39524), Saccharomyces cerevisiae (Q12674), Homo sapiens, Caenorhabditis elegans (C7U324), Caenorhabditis elegans (G5EBH1), Caenorhabditis elegans (O18182), Caenorhabditis elegans (P91203), Caenorhabditis elegans (Q7YXV5)
Manually annotated by BRENDA team
van der Velden, L.M.; Wichers, C.G.; van Breevoort, A.E.; Coleman, J.A.; Molday, R.S.; Berger, R.; Klomp, L.W.; van de Graaf, S.F.
Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases
J. Biol. Chem.
285
40088-40096
2010
Homo sapiens (Q9Y2Q0), Homo sapiens
Manually annotated by BRENDA team
Takatsu, H.; Baba, K.; Shima, T.; Umino, H.; Kato, U.; Umeda, M.; Nakayama, K.; Shin, H.W.
ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes to the trans-Golgi network in a CDC50 protein-independent manner
J. Biol. Chem.
286
38159-38167
2011
Homo sapiens
Manually annotated by BRENDA team
Smith, B.A.; ONeil, E.J.; Lampkins, A.J.; Johnson, J.R.; Lee, J.J.; Cole, E.L.; Smith, B.D.
Evaluation of fluorescent phosphatidylserine substrates for the aminophospholipid flippase in mammalian cells
J. Fluoresc.
22
93-101
2012
Cricetulus griseus, Homo sapiens
Manually annotated by BRENDA team
Kim, J.E.; Han, M.; Hanl, K.S.; Kim, H.K.
Vitamin E inhibition on platelet procoagulant activity: involvement of aminophospholipid translocase activity
Thromb. Res.
127
435-442
2011
Homo sapiens
Manually annotated by BRENDA team
Lee, S.; Uchida, Y.; Wang, J.; Matsudaira, T.; Nakagawa, T.; Kishimoto, T.; Mukai, K.; Inaba, T.; Kobayashi, T.; Molday, R.S.; Taguchi, T.; Arai, H.
Transport through recycling endosomes requires EHD1 recruitment by a phosphatidylserine translocase
EMBO J.
34
669-688
2015
Homo sapiens (Q9NTI2), Homo sapiens (Q9Y2Q0)
Manually annotated by BRENDA team
Onat, O.E.; Gulsuner, S.; Bilguvar, K.; Nazli Basak, A.; Topaloglu, H.; Tan, M.; Tan, U.; Gunel, M.; Ozcelik, T.
Missense mutation in the ATPase, aminophospholipid transporter protein ATP8A2 is associated with cerebellar atrophy and quadrupedal locomotion
Eur. J. Hum. Genet.
21
281-285
2013
Homo sapiens (Q9NTI2), Homo sapiens
Manually annotated by BRENDA team
Kleinegris, M.C.; Koek, G.H.; Mast, K.; Mestrom, E.H.; Wolfs, J.L.; Bevers, E.M.
Ribavirin-induced externalization of phosphatidylserine in erythrocytes is predominantly caused by inhibition of aminophospholipid translocase activity
Eur. J. Pharmacol.
693
1-6
2012
Homo sapiens
Manually annotated by BRENDA team
Takatsu, H.; Tanaka, G.; Segawa, K.; Suzuki, J.; Nagata, S.; Nakayama, K.; Shin, H.W.
Phospholipid flippase activities and substrate specificities of human type IV P-type ATPases localized to the plasma membrane
J. Biol. Chem.
289
33543-33556
2014
Homo sapiens (O43520), Homo sapiens (P98196), Homo sapiens (P98198), Homo sapiens (Q8NB49), Homo sapiens
Manually annotated by BRENDA team
Naito, T.; Takatsu, H.; Miyano, R.; Takada, N.; Nakayama, K.; Shin, H.W.
Phospholipid flippase ATP10A translocates phosphatidylcholine and is involved in plasma membrane dynamics
J. Biol. Chem.
290
15004-15017
2015
Homo sapiens (O60312), Homo sapiens (O94823), Homo sapiens (Q9P241)
Manually annotated by BRENDA team
Ansari, I.U.; Longacre, M.J.; Paulusma, C.C.; Stoker, S.W.; Kendrick, M.A.; MacDonald, M.J.
Characterization of P4 ATPase phospholipid translocases (flippases) in human and rat pancreatic beta cells: their gene silencing inhibits insulin secretion
J. Biol. Chem.
290
23110-23123
2015
Rattus norvegicus (D4AA47), Homo sapiens (O43520), Homo sapiens (P98198), Homo sapiens (Q2NLD0), Homo sapiens
Manually annotated by BRENDA team
van der Mark, V.A.; de Jonge, H.R.; Chang, J.C.; Ho-Mok, K.S.; Duijst, S.; Vidovic, D.; Carlon, M.S.; Oude Elferink, R.P.; Paulusma, C.C.
The phospholipid flippase ATP8B1 mediates apical localization of the cystic fibrosis transmembrane regulator
Biochim. Biophys. Acta
1863
2280-2288
2016
Homo sapiens (O43520), Homo sapiens
Manually annotated by BRENDA team
Takada, N.; Naito, T.; Inoue, T.; Nakayama, K.; Takatsu, H.; Shin, H.W.
Phospholipid-flipping activity of P4-ATPase drives membrane curvature
EMBO J.
37
pii: e97705
2018
Homo sapiens (O60312)
Manually annotated by BRENDA team
Tanaka, Y.; Ono, N.; Shima, T.; Tanaka, G.; Katoh, Y.; Nakayama, K.; Takatsu, H.; Shin, H.W.
The phospholipid flippase ATP9A is required for the recycling pathway from the endosomes to the plasma membrane
Mol. Biol. Cell
27
3883-3893
2016
Homo sapiens (O75110), Homo sapiens
Manually annotated by BRENDA team
Takatsu, H.; Takayama, M.; Naito, T.; Takada, N.; Tsumagari, K.; Ishihama, Y.; Nakayama, K.; Shin, H.W.
Phospholipid flippase ATP11C is endocytosed and downregulated following Ca2+-mediated protein kinase C activation
Nat. Commun.
8
1423
2017
Homo sapiens (Q8NB49)
Manually annotated by BRENDA team
Zachowski, A.; Henry, J.P.; Devaux, P.F.
Control of transmembrane lipid asymmetry in chromaffin granules by an ATP-dependent protein
Nature
340
75-76
1989
Homo sapiens
Manually annotated by BRENDA team