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Information on EC 7.6.2.1 - P-type phospholipid transporter and Organism(s) Saccharomyces cerevisiae and UniProt Accession P39524

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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:
Saccharomyces cerevisiae
UNIPROT: P39524
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
Dnf2
Drs2 Neo1 family ATPase 2
phospholipid flippase
-
type IV P-type ATPase
-
aminophospholipid flippase
aminophospholipid flippase 10
-
-
-
-
aminophospholipid flippase 11
-
-
-
-
aminophospholipid flippase 12
-
-
-
-
aminophospholipid translocase
aminophospholipid translocase VC
-
-
-
-
ATPase II
ATPVC
-
-
-
-
ATPVD
-
-
-
-
Cdc50p-Drs2p
-
-
Dnf1 |
Drs2 Neo1 family ATPase 1
Dnf1p
Dnf1p and Dnf2p
-
-
Dnf2p
Dnf3
Drs2 Neo1 family ATPase 3
Dnf3p
Drs2
-
defect in ribosome synthesis 2
Drs2-dependent phosphatidylserine translocase
-
-
Drs2p
energy-dependent lipid flippase
-
-
energy-independent lipid flippase
-
-
flippase
HUSSY-20
-
-
-
-
inward-directed phospholipid translocase
-
-
M5-DLO flippase
-
-
Man5GlcNAc2-PP-dolichol flippase
-
-
Mg2+-ATPase
-
-
-
-
Mg2+-ATPase A
-
-
-
-
Neo1
-
neomycin resistance 1
Neo1p
P4-ATPase
phosphatidylserine flippase
-
-
phosphatidylserine translocase
-
-
phospholipid flippase
phospholipid translocase
-
-
phospholipid-translocase
-
-
PS translocase
-
-
sphingomyelin flippase
-
-
type 4 P-type ATPas
-
-
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
The Cdc50p/Lem3p family comprises a set of subunits specific to phospholipid-translocating P-type ATPases. Cdc50p physically associates with Drs2p. Cds50p forms a complex with Drs2p, whereas Lem3p forms a complex with Dnf1p in vivo. The Cdc50p-Drs2p complex possesses aminophospholipid translocase activity, which translocates aminophospholipids more efficiently than phosphatidylcholine.
-
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
-
-
-
?
ATP + H2O + phosphatidylethanolamine/in
ADP + phosphate + phosphatidylethanolamine/out
show the reaction diagram
-
-
-
?
ATP + H2O + phosphatidylserine/in
ADP + phosphate + phosphatidylserine/out
show the reaction diagram
ATP + H2O + 1-palmitoyl-2-(6-(7-nitro-2-1,3-benzoxadiazole)-aminocaproyl)-phosphatidylcholine/out
ADP + phosphate + 1-palmitoyl-2-(6-(7-nitro-2-1,3-benzoxadiazole)-aminocaproyl)-phosphatidylcholine/in
show the reaction diagram
-
internalization through the plasma membrane by the Dnf1p-Lem3p complex
-
-
?
ATP + H2O + 1-palmitoyl-2-(6-(7-nitro-2-1,3-benzoxadiazole)-aminocaproyl)-phosphatidylethanolamine/out
ADP + phosphate + 1-palmitoyl-2-(6-(7-nitro-2-1,3-benzoxadiazole)-aminocaproyl)-phosphatidylethanolamine/in
show the reaction diagram
-
internalization through the plasma membrane by the Dnf1p-Lem3p complex
-
-
?
ATP + H2O + aminophospholipid[side 1]
ADP + phosphate + aminophospholipid[side 2]
show the reaction diagram
-
-
-
-
?
ATP + H2O + glycerophospholipid[side 1]
ADP + phosphate + glycerophospholipid[side 2]
show the reaction diagram
-
-
-
-
?
ATP + H2O + lysophosphatidylcholine/out
ADP + phosphate + lysophosphatidylcholine/in
show the reaction diagram
-
lysophosphatidylcholine is a bona fide biological substrate transported by the yeast plasma membrane ATPases, Dnf1p and Dnf2p, in consort with a second protein Lem3p
-
-
?
ATP + H2O + lysophosphatidylethanolamine/out
ADP + phosphate + lysophosphatidylethanolamine/in
show the reaction diagram
-
lysophosphatidylethanolamine is a bona fide biological substrate transported by the yeast plasma membrane ATPases, Dnf1p and Dnf2p, in consort with a second protein Lem3p
-
-
?
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 + 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 + sphingomyelin[side 1]
ADP + phosphate + sphingomyelin[side 2]
show the reaction diagram
-
low activity
-
-
?
Man5GlcNAc2-diphosphate-dolichol/out
Man5GlcNAc2-diphosphate-dolichol/in
show the reaction diagram
-
-
-
-
?
phospholipid/in
phospholipid/out
show the reaction diagram
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 + aminophospholipid[side 1]
ADP + phosphate + aminophospholipid[side 2]
show the reaction diagram
-
-
-
-
?
ATP + H2O + glycerophospholipid[side 1]
ADP + phosphate + glycerophospholipid[side 2]
show the reaction diagram
-
-
-
-
?
ATP + H2O + phosphatidylethanolamine/in
ADP + phosphate + phosphatidylethanolamine/out
show the reaction diagram
-
selective ATP-dependent transport/flip of phosphatidylethanolamine from the outer to the inner monolayer of the cell membrane and post-Golgi secretory vesicles to maintain lipid asymmetry
-
-
?
ATP + H2O + phosphatidylethanolamine/out
ADP + phosphate + phosphatidylethanolamine/in
show the reaction diagram
ATP + H2O + phosphatidylserine/in
ADP + phosphate + phosphatidylserine/out
show the reaction diagram
-
selective ATP-dependent transport/flip of phosphatidylserine from the outer to the inner monolayer of the cell membrane and post-Golgi secretory vesicles to maintain lipid asymmetry
-
-
?
ATP + H2O + phosphatidylserine/out
ADP + phosphate + phosphatidylserine/in
show the reaction diagram
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
-
-
-
-
?
phospholipid/in
phospholipid/out
show the reaction diagram
-
transbilayer movement of phospholipids in an unidirectional fashion in biological membranes is mediated by energy-dependent and energy-independent flippases
-
-
ir
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Kes1p
-
Kes1p represses the flippase activity of Drs2p in trans-Golgi network membranes
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
protein Drs2p
-
coupled to the enzyme, required for the translocation of phospholipids from the luminal leaflet of the membrane to the cytosolic leaflet in the trans-Golgi network, overview
-
additional information
-
Lem3p interacts and sustains functionality of isozymes Dnf1p and Dnf2p
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
flippase activity detected with unlabeled lipids by shape changes of giant unilamellar vesicles
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
AP-1 is required, and GGA proteins, Golgi localized, gamma-ear containing, Arf-binding proteins acting as chlatrin adaptos, are dispensable, for efficient exclusion of Drs2p from exocytic vesicles targeted to the plasma membrane
Manually annotated by BRENDA team
-
post-Golgi, Drs2p is incorporated into the low-density class of secretory vesicles
Manually annotated by BRENDA team
-
Cdc50p and Drs2p are localized to the trans-Golgi network and late endosome
Manually annotated by BRENDA team
-
proteoliposome
Manually annotated by BRENDA team
additional information
-
P4-ATPases Drs2p and Dnf1p cycle between the exocytic and endocytic pathways, and maintain a steady-state localization to internal organelles requiring endocytosis
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
malfunction
metabolism
physiological function
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F511L
the mutant has a specific activity that is 35% that of wild type Drs2
F511Y
the mutant retains wild type activity, the substitution in Drs2 specifically abrogates phosphatidylserine recognition by this flippase causing phosphatidylserine exposure on the outer leaflet of the plasma membrane without disrupting phospatidylethanolamine asymmetry
D256E
-
the mutant shows reduced activity with phosphatidylcholine, increased activity with phosphatidylserine, and increased activity with sphingomyelin compared to the wild type enzyme
F213S
-
the mutant shows increased activity with phosphatidylcholine, phosphatidylserine, and sphingomyelin compared to the wild type enzyme
I1235F
mutation increases the overall activity of Dnf1 for all substrates and causes partial loss of specificity for glycerophospholipid
I615M
-
the mutant shows about wild type activity
I615S
-
the mutation significantly increases sphingomyelin and phosphatidylserine transport compared to the wild type enzyme
I615T
-
the mutant shows about wild type activity
L242S
-
the mutant shows reduced activity with phosphatidylcholine and wild type activity with sphingomyelin
N220C
-
the mutant shows wild type activity with phosphatidylcholine and increased activity with sphingomyelin
N220S
-
the mutant shows reduced activity with phosphatidylcholine and increased activity with sphingomyelin compared to the wild type enzyme
N220S/L242S
-
the mutant shows reduced activity with phosphatidylcholine and increased activity with sphingomyelin compared to the wild type enzyme
N220T
-
the mutant shows increased activity with phosphatidylcholine and increased activity with sphingomyelin compared to the wild type enzyme
N550S
-
the mutant shows reduced activity with phosphatidylcholine, increased activity with phosphatidylserine, and increased activity with sphingomyelin compared to the wild type enzyme
T254A
-
the mutant shows reduced activity with phosphatidylcholine, increased activity with phosphatidylserine, and increased activity with sphingomyelin compared to the wild type enzyme
Y618F
acquisition of the phosphatidylserine substrate maps to a Tyr618Phe substitution in transmembrane segment 4 of Dnf1. The rate of 7-nitrobenz-2–oxa-1,3-diazol-4-yl phospholipid uptake by Dnf1 Y618F is comparable to wild type Dnf1
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from chromaffin granules
-
native enzymes partially by subcellular fractionation
-
partially by microsome preparation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Creation and study of strains lacking Dnf1, Dnf2 or both Dnf1 and Dnf2. The double mutant is defective in the inward translocalisation of NBD-labeled phosphatidylethanolamine, phosphatidylserine and phosphatidylcholine across the plasmamembrane. The loss of both Dnf1 and Dnf2 leads to an increased cell surface exposure of endogenous aminophospholipids. The double mutant is sensitive to low concentrations of Co2+, Ni2+, Zn2+, and Mn2+
-
expressed in HeLa cells
-
expression of GFP-tagged Drs2p and HA-tagged Drf1p wild-type and mutant enzymes in Saccharomyces cerevisiae, subcloning in Escherichia coli strains XL1-Blue and DH5alpha
-
gene swa4, DNA and amino acid sequence determination and anaylsis, comparison to the allelic gene cdc50
-
genes DNF1 and DNF2, expression of EGFP-tagged Dnf1p and Dnf2p in Saccharomyces cerevisiae deletion mutant strains vps51DELTA, vps52DELTA, vps53DELTA, and vps54DELTA
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genes DRS2, DNF1 and DNF2, and DNF3, expression of wild-type and mutant enzymes, overview
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
preparation of proteoliposomes for enzyme reconstitution using microsome and liposomes, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Drs2p deficiency causes a markedly increased rate of cholesterol transport from the plasma membrane to the endoplasmic reticulum and redistribution of endogenous ergosterol to intracellular membranes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pomorski, T.; Lombardi, R.; Riezman, H.; Devaux, P.F.; van Meer, G.; Holthuis, J.C.M.
Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis
Mol. Biol. Cell
14
1240-1254
2003
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Saito, K.; Fujimura-Kamada, K.; Furuta, N.; Kato, U.; Umeda, M.; Tanaka, K.
Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae
Mol. Biol. Cell
15
3418-3432
2004
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Noji, T.; Yamamoto, T.; Saito, K.; Fujimura-Kamada, K.; Kondo, S.; Tanaka, K.
Mutational analysis of the Lem3p-Dnf1p putative phospholipid-translocating P-type ATPase reveals novel regulatory roles for Lem3p and a carboxyl-terminal region of Dnf1p independent of the phospholipid-translocating activity of Dnf1p in yeast
Biochem. Biophys. Res. Commun.
344
323-331
2006
Saccharomyces cerevisiae
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
Natarajan, P.; Wang, J.; Hua, Z.; Graham, T.R.
Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function
Proc. Natl. Acad. Sci. USA
101
10614-10619
2004
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Papadopulos, A.; Vehring, S.; Lopez-Montero, I.; Kutschenko, L.; Stoeckl, M.; Devaux, P.F.; Kozlov, M.; Pomorski, T.; Herrmann, A.
Flippase activity detected with unlabeled lipids by shape changes of giant unilamellar vesicles
J. Biol. Chem.
282
15559-15568
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae sec61
Manually annotated by BRENDA team
Stevens, H.C.; Nichols, J.W.
The proton electrochemical gradient across the plasma membrane of yeast is necessary for phospholipid flip
J. Biol. Chem.
282
17563-17567
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae LMY65
Manually annotated by BRENDA team
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
Saccharomyces cerevisiae, Saccharomyces cerevisiae EHY227
Manually annotated by BRENDA team
Furuta, N.; Fujimura-Kamada, K.; Saito, K.; Yamamoto, T.; Tanaka, K.
Endocytic recycling in yeast is regulated by putative phospholipid translocases and the Ypt31p/32p-Rcy1p pathway
Mol. Biol. Cell
18
295-312
2007
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Liu, K.; Hua, Z.; Nepute, J.A.; Graham, T.R.
Yeast P4-ATPases Drs2p and Dnf1p are essential cargos of the NPFXD/Sla1p endocytic pathway
Mol. Biol. Cell
18
487-500
2007
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Liu, K.; Surendhran, K.; Nothwehr, S.F.; Graham, T.R.
P4-ATPase requirement for AP-1/clathrin function in protein transport from the trans-Golgi network and early endosomes
Mol. Biol. Cell
19
3525-3535
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Chen, S.; Wang, J.; Muthusamy, B.; Liu, K.; Zare, S.; Andersen, R.J.; Graham, T.R.
Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane
Traffic
7
1503-1517
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae CCY 2811
Manually annotated by BRENDA team
Sanyal, S.; Frank, C.G.; Menon, A.K.
Distinct flippases translocate glycerophospholipids and oligosaccharide diphosphate dolichols across the endoplasmic reticulum
Biochemistry
47
7937-7946
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae YCF40
Manually annotated by BRENDA team
Riekhof, W.R.; Voelker, D.R.
The yeast plasma membrane P4-ATPases are major transporters for lysophospholipids
Biochim. Biophys. Acta
179
620-627
2009
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Poulsen, L.R.; Lopez-Marques, R.L.; Palmgren, M.G.
Flippases: still more questions than answers
Cell. Mol. Life Sci.
65
3119-3125
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Muthusamy, B.P.; Raychaudhuri, S.; Natarajan, P.; Abe, F.; Liu, K.; Prinz, W.A.; Graham, T.R.
Control of protein and sterol trafficking by antagonistic activities of a P4-ATPase and oxysterol binding protein homologue
Mol. Biol. Cell
20
2920-2931
2009
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Takagi, K.; Iwamoto, K.; Kobayashi, S.; Horiuchi, H.; Fukuda, R.; Ohta, A.
Involvement of Golgi-associated retrograde protein complex in the recycling of the putative Dnf aminophospholipid flippases in yeast
Biochem. Biophys. Res. Commun.
417
490-494
2012
Saccharomyces cerevisiae
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
Baldridge, R.D.; Graham, T.R.
Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases
Proc. Natl. Acad. Sci. USA
109
E290-E298
2012
Saccharomyces cerevisiae (P32660), Saccharomyces cerevisiae (P39524), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Baldridge, R.D.; Graham, T.R.
Two-gate mechanism for phospholipid selection and transport by type IV P-type ATPases
Proc. Natl. Acad. Sci. USA
110
E358-E367
2013
Saccharomyces cerevisiae (P32660), Saccharomyces cerevisiae (P39524)
Manually annotated by BRENDA team
Roland, B.; Graham, T.
Decoding P4-ATPase substrate interactions
Crit. Rev. Biochem. Mol. Biol.
51
513-527
2016
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Yamamoto, T.; Fujimura-Kamada, K.; Shioji, E.; Suzuki, R.; Tanaka, K.
Cfs1p, a novel membrane protein in the PQ-loop family, is involved in phospholipid flippase functions in yeast
G3 (Bethesda)
7
179-192
2017
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Takatsu, H.; Baba, K.; Shima, T.; Umino, H.; Kato, U.; Umeda, M.; Nakayama, K.; Shin, H.
ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes to the trans-Golgi network in a CDC50 protein-independent
J. Biol. Chem.
286
38159-38167
2015
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Yamagami, K.; Yamamoto, T.; Sakai, S.; Mioka, T.; Sano, T.; Igarashi, Y.; Tanaka, K.
Inositol depletion restores vesicle transport in yeast phospholipid flippase mutants
PLoS ONE
10
e0120108
2015
Saccharomyces cerevisiae, Saccharomyces cerevisiae YEF473
Manually annotated by BRENDA team
Roland, B.P.; Graham, T.R.
Directed evolution of a sphingomyelin flippase reveals mechanism of substrate backbone discrimination by a P4-ATPase
Proc. Natl. Acad. Sci. USA
113
E4460-E4466
2016
Saccharomyces cerevisiae
Manually annotated by BRENDA team