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Information on EC 3.1.3.56 - inositol-polyphosphate 5-phosphatase and Organism(s) Arabidopsis thaliana and UniProt Accession O80560
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3.1.3.56 inositol-polyphosphate 5-phosphataseIUBMB Comments
One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids.
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Word Map
- 3.1.3.56
- phosphatidylinositol
- 1,4-bisphosphate
- 5ptases
-
oculocerebrorenal
- 3,4,5-trisphosphate
-
ptdins4,5p2
-
3hinositol
- 2,3-bisphosphoglycerate
- inpp5f
-
ptdins3,4,5p3
- medicine
- molecular biology
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
inpp5k, ins(1,4,5)p3 5-phosphatase, inositol polyphosphate-5-phosphatase, inpp5a, insp 5-ptase, insp3 5-phosphatase, pip3 phosphatase, at5ptase1, inositol polyphosphatase, 5pt13, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5PTase
D-myo-inositol 1,4,5-triphosphate 5-phosphatase
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D-myo-inositol 1,4,5-trisphosphate 5-phosphatase
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D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase
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inosine triphosphatase
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inositol 1,4,5-triphosphate 5-phosphatase
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inositol 1,4,5-trisphosphate 5-monophosphatase
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inositol 1,4,5-trisphosphate 5-phosphatase
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inositol 1,4,5-trisphosphate phosphatase
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inositol phosphate 5-phosphomonoesterase
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inositol polyphosphate 5-phosphatase
inositol polyphosphate-5-phosphatase
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inositol trisphosphate phosphomonoesterase
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inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase
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Ins(1,4,5)P3 5-phosphatase
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Ins(1,4,5)P3/Ins(1,3,4,5)P4 5-phosphatase
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L-myo-inositol 1,4,5-trisphosphate-monoesterase
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myo-inositol-1,4,5-trisphosphate 5-phosphatase
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phosphatase, inosine tri-5PTASE
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
1D-myo-inositol-1,4,5-trisphosphate 5-phosphohydrolase
One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids.
CAS REGISTRY NUMBER
COMMENTARY
106283-14-1
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9082-57-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
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-
-
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?
1D-myo-inositol 1,4,5-trisphosphate + H2O
myo-inositol 1,4-bisphosphate + phosphate
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-
-
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?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
specific for
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-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
absolutely specific for
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-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
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-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
specific for
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-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
absolutely specific for
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-
?
additional information
?
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substrate specificity, no activity with 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate, 1D-myo-inositol 1,3,4,5-tetrakisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate, 1-phosphatidyl-1D-myo-inositol 5-phosphate, 1-phosphatidyl-1D-myo-inositol 4-phosphate, and 1-phosphatidyl-1D-myo-inositol 3-phosphate
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-
?
additional information
?
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substrate specificity, no activity with 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate, 1D-myo-inositol 1,3,4,5-tetrakisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate, 1-phosphatidyl-1D-myo-inositol 5-phosphate, 1-phosphatidyl-1D-myo-inositol 4-phosphate, and 1-phosphatidyl-1D-myo-inositol 3-phosphate
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?
additional information
?
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substrate specificity, no activity with 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate, 1D-myo-inositol 1,3,4,5-tetrakisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate, 1-phosphatidyl-1D-myo-inositol 5-phosphate, 1-phosphatidyl-1D-myo-inositol 4-phosphate, and 1-phosphatidyl-1D-myo-inositol 3-phosphate
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?
additional information
?
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substrate specificity, no activity with 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate, 1D-myo-inositol 1,3,4,5-tetrakisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate, 1-phosphatidyl-1D-myo-inositol 5-phosphate, 1-phosphatidyl-1D-myo-inositol 4-phosphate, and 1-phosphatidyl-1D-myo-inositol 3-phosphate
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
specific for
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
specific for
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-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
myo-inositol 1,4-bisphosphate + phosphate
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-
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
wounding and abscisic acid induce the enzyme
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additional information
wounding and abscisic acid induce the enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
expression of At5pTase1 is weaker than At5Ptase2
additional information
expression of At5pTase1 is weaker than At5Ptase2
additional information
-
expression of At5pTase1 is weaker than At5Ptase2
additional information
expression of At5pTase2 is generally stronger than At5Ptase1
additional information
expression of At5pTase2 is generally stronger than At5Ptase1
additional information
-
expression of At5pTase2 is generally stronger than At5Ptase1
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
using a GFP-fusion construct it is shown that in most cells, the GFP fluorescence retracts from the cell wall, and is most concentrated in a ring, consistent with a cell surface or plasma membrane location
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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the increase in the levels of 1D-myo-inositol 1,4,5-trisphosphate/Ca2+ caused by deficiency of inositol polyphosphate 5-phosphatases is sufficient to break pollen dormancy and to trigger early germination
physiological function
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the enzyme is crucial for maintaining pollen dormancy
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). IP5PC_ARATH
1316
0
144731
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme contains a WD-repeat domain and a 5PTase catalytic domain
additional information
the enzyme contains a WD-repeat domain and a 5PTase catalytic domain
additional information
the enzyme contains a WD-repeat domain and a 5PTase catalytic domain
additional information
the enzyme contains a WD-repeat domain and a 5PTase catalytic domain
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wild-type seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wild-type seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
-
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wild-type seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wildtype seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wildtype seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
additional information
-
T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wildtype seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from yeast by nickel affinity chromatography
recombinant His-tagged enzyme from yeast by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene 5PTase12, expression of His-tagged full length enzyme in yeast
gene 5PTase13, expression of His-tagged full length enzyme in yeast
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform 5PT12 is preferentially expressed in leaf and mature pollen grains at floral stages 12-14
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
At5PTase1 and At5PTase2 genes have nonredundant roles in hydrolyzing inositol second-messenger substrates and regulation of Ins(1,4,5)P3 levels is important during germination and early seedling development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhong, R.; Ye, Z.H.
Molecular and biochemical characterization of three WD-repeat-domain-containing inositol polyphosphate 5-phosphatases in Arabidopsis thaliana
Plant Cell Physiol.
45
1720-1728
2004
Arabidopsis thaliana (O80560), Arabidopsis thaliana (Q9SYK4)
Gunesekera, B.; Torabinejad, J.; Robinson, J.; Gillaspy, G.E.
Inositol polyphosphate 5-phosphatases 1 and 2 are required for regulating seedling growth
Plant Physiol.
143
1408-1417
2007
Arabidopsis thaliana (Q84MA2), Arabidopsis thaliana (Q9FUR2), Arabidopsis thaliana
Ercetin, M.E.; Ananieva, E.A.; Safaee, N.M.; Torabinejad, J.; Robinson, J.Y.; Gillaspy, G.E.
A phosphatidylinositol phosphate-specific myo-inositol polyphosphate 5-phosphatase required for seedling growth
Plant Mol. Biol.
67
375-388
2008
Arabidopsis thaliana
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (Q84MA2), Arabidopsis thaliana (Q9FUR2)
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