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Information on EC 7.6.2.1 - P-type phospholipid transporter and Organism(s) Arabidopsis thaliana and UniProt Accession P98204

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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:
Arabidopsis thaliana
UNIPROT: P98204
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
aminophospholipid flippase
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aminophospholipid ATPase
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aminophospholipid flippase
aminophospholipid flippase 10
-
-
-
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aminophospholipid flippase 11
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-
-
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aminophospholipid flippase 12
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-
-
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aminophospholipid translocase
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-
-
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aminophospholipid translocase VC
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-
-
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ATPase II
-
-
-
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ATPVC
-
-
-
-
ATPVD
-
-
-
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flippase
-
-
-
-
HUSSY-20
-
-
-
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Mg2+-ATPase
-
-
-
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Mg2+-ATPase A
-
-
-
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P4 ATPase ALA1
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phospholipid flippase
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-
additional information
ALA3 is a member of the P4-ATPase subfamily
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
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transmembrane transport
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-
-
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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[side 1]
ADP + phosphate + phosphatidylcholine[side 2]
show the reaction diagram
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-
-
-
?
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 + phospholipid[side 1]
ADP + phosphate + phospholipid[side 2]
show the reaction diagram
-
-
-
-
?
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 + phospholipid[side 1]
ADP + phosphate + phospholipid[side 2]
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ALIS protein
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-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme localizes to the plant plasma membrane and has a strict requirement for an ALIS protein beta-subunit to exit the endoplasmic reticulum
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
ATP-dependent aminophospholipid translocases constitute a subfamily, P4 ATPases, in the superfamily of P-type ATPase pumps
malfunction
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knockdown of ALA1 expression causes a cold-sensitive growth defect in plants
metabolism
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the enzyme controls fatty acid desaturase 2/3 desaturation of phosphatidylcholine in the endoplasmic reticulum and affects chloroplast lipid composition in Arabidopsis thaliana
physiological function
additional information
the loss of ITB2/ALA3 function leads to aberrant trichome expansion, reduced primary root growth and longer root hairs
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALA1_ARATH
1158
10
130329
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 120000, SDS-PAGE
heterodimer
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-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
phenotypic and genetic analyses of multiple itb2 alleles, including the T-DNA insertion alleles, shows that the loss of ITB2/ALA3 function leads to aberrant trichome expansion, reduced primary root growth and longer root hairs, but has no effect on plant growth, phenotype, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain w303-1a
gene ITB2, DNA and amino acid sequence determination and analysis, phenotypic and genetic analyses of multiple itb2 alleles, including the T-DNA insertion alleles, ITB2 gene structure, intron positions, and ITB2 fine mapping and mutation mapping, overview
heterologous expression of ALA1 in a enzyme-deficient Ddrs2Ddnf1Ddnf2 Saccharomyces cerevisiae mutant strain. Transient expression of N-terminally GFP-tagged ALA1 in tobacco leaves in the presence of untagged versions of three different ALIS proteins ALIS1, ALIS3, ALIS5, co-expression with any ALIS protein results in localization of GFP-ALA1 in membranes resembling either the plasma membrane or the tonoplast. Expression of GFP­-tagged ALA1 lacking its beta-subunit localizes to the endoplasmic reticulum in tobacco epidermal cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is overexpressed in plants treated with 0.1 mM galvestine-1
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, X.; Oppenheimer, D.G.
IRREGULAR TRICHOME BRANCH 2 (ITB2) encodes a putative aminophospholipid translocase that regulates trichome branch elongation in Arabidopsis
Plant J.
60
195-206
2009
Arabidopsis thaliana (Q9XIE6)
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
Lopez-Marques, R.L.; Poulsen, L.R.; Palmgren, M.G.
A putative plant aminophospholipid flippase, the Arabidopsis P4 ATPase ALA1, localizes to the plasma membrane following association with a beta-subunit
PLoS ONE
7
e33042
2012
Arabidopsis thaliana, Arabidopsis thaliana (P98204)
Manually annotated by BRENDA team
Botella, C.; Sautron, E.; Boudiere, L.; Michaud, M.; Dubots, E.; Yamaryo-Botte, Y.; Albrieux, C.; Marechal, E.; Block, M.A.; Jouhet, J.
ALA10, a phospholipid flippase, controls FAD2/FAD3 desaturation of phosphatidylcholine in the ER and affects chloroplast lipid composition in Arabidopsis thaliana
Plant Physiol.
170
1300-1314
2016
Arabidopsis thaliana
Manually annotated by BRENDA team