Information on EC 3.6.3.B6 - aminophospholipid translocase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.3.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
aminophospholipid translocase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene tat-1C
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
inability of tat-1 mutants to take up 1-oleoyl-2-{6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl}-sn-glycero-3-phosphoserine
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
fluorescent labeled phosphatidylserine/outer leaflet + ATP + H2O
fluorescent labeled phosphatidylserine/inner leaflet + ADP + phosphate
show the reaction diagram
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enzyme specifically transports phosphatidylserine from the outer to the inner leaflet of the plasma membrane
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O-[[(2R)-2-[(9-[5-[7-(diethylamino)-2-oxo-2H-1-benzopyran-3-yl]-1H-1,2,3-triazol-4-yl]nonanoyl)oxy]-3-(hexadecanoyloxy)propoxy](hydroxy)phosphoryl]-L-serine/outer leaflet + ?
O-[[(2R)-2-[(9-[5-[7-(diethylamino)-2-oxo-2H-1-benzopyran-3-yl]-1H-1,2,3-triazol-4-yl]nonanoyl)oxy]-3-(hexadecanoyloxy)propoxy](hydroxy)phosphoryl]-L-serine/cytoplasmic leaflet + ?
show the reaction diagram
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coumarin-derivative of phosphatidylserine
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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C7U324
Tat-1 binds specifically NUM-1A, which regulates endocytic recycling in Caenorhabditis elegans
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ribavirin
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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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
TAT-1 is differentially spliced during development, isozyme TAT-1C-specific splicing occurs in the intestine
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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ATP9A localizes to endosomes and the trans-Golgi network
Manually annotated by BRENDA team
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endomembrane localization of class 2 and 6 P4-ATPases, overview. ATP9A is localized to the early/recycling endosomes but not late endosomes and to the trans-Golgi network rather than the cis-Golgi. Unlike ATP9A, ATP9B is localized exclusively to the perinuclear region but not on EEA1-positive early endosomes
Manually annotated by BRENDA team
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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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene tat-1, expression in Saccharomyces cerevisiae. Ability of NUM-1A to inhibit transport of phosphatidylserine is suppressed by multiple copies of tat-1C
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
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of a chimeric ATP9 protein by replacement of the N-terminal cytoplasmic region of ATP9A with the corresponding region of ATP9B, the mutant chimera is localized exclusively to the Golgi apparatus. The mutant ATP9B(53-126) construct retains the ability to localize to the Golgi
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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phosphatidylserine-coumarin O-[[(2R)-2-[(9-[5-[7-(diethylamino)-2-oxo-2H-1-benzopyran-3-yl]-1H-1,2,3-triazol-4-yl]nonanoyl)oxy]-3-(hexadecanoyloxy)propoxy](hydroxy)phosphoryl]-L-serine exhibits bright fluorescence and good photostability. It should be useful as a blue-emitting fluorescent translocation substrate for extended imaging studies of flippase action in living cells using laser confocal microscopy
medicine
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spontaneous loss of lipid asymmetry, not corrected by aminophospholipid translocase activity, is the mechanism for ribavirin-induced phosphatidylserine exposure that may contribute to ribavirin-induced anemia