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Information on EC 3.1.3.36 - phosphoinositide 5-phosphatase and Organism(s) Arabidopsis thaliana and UniProt Accession Q84W55
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3.1.3.36 phosphoinositide 5-phosphataseIUBMB Comments
These enzymes can also remove the 5-phosphate from Ins(1,4,5)P3 and/or Ins(1,3,4,5)P4. They are a diverse family of enzymes, with differing abilities to catalyse two or more of the four reactions listed. They are thought to use inositol lipids rather than inositol phosphates as substrates in vivo. All of them can use either or both of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 as substrates; this is the main property that distinguishes them from EC 3.1.3.56, inositol-polyphosphate 5-phosphatase.
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Word Map
- 3.1.3.36
-
endocytosis
- phosphatases
- synaptic
-
domain-containing
- actin
- pten
- 3-kinase
-
endocytic
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x-linked
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ptdins3,4,5p3
- cataract
- clathrin
- dynamin
- cilia
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clathrin-mediated
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tensin
-
polyphosphoinositide
- dent
-
clathrin-coated
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endophilins
-
voltage-sensing
-
joubert
- amphiphysins
- ciliopathies
-
ptdins3,4p2
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ptdins4p
- 1,3,4,5-tetrakisphosphate
-
itims
-
fcgammariib
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tubulopathy
-
pleckstrin
-
tyrosine-based
-
immunoreceptor
- ship-1
- 3,4-bisphosphate
-
nephrocalcinosis
- eps15
-
ciliogenesis
-
microrna-155
-
arl13b
- phosphatidylinositol-3,4,5-trisphosphate
- 3,4,5-triphosphate
-
4-phosphatase
- myotubularins
-
hypercalciuria
- inpp4b
-
intersectin
-
n-wasp
- phosphatidylinositol-4-phosphate
-
myotubular
- molecular biology
- medicine
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
ship2, ship1, ocrl1, synaptojanin, inpp5e, synj1, phosphoinositide phosphatase, inositol polyphosphate 5-phosphatase, inositol 5-phosphatase, ci-vsp, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5PTase
diphosphoinositide phosphatase
-
-
-
-
inositol polyphosphate 5-phosphatase
inositol triphosphate 5-phosphomonoesterase
-
-
-
-
Lowe's oculocerebrorenal syndrome protein
-
-
-
-
OCRL protein
-
-
-
-
p150
-
-
-
-
phosphatase, triphosphoinositide
-
-
-
-
phosphatidyl 4,5-bisphosphate-specific phosphomonoesterase
-
-
-
-
phosphatidyl bisphosphate phosphatase
-
-
-
-
phosphatidyl-inositol 4,5-bisphosphate 5-phosphatase
-
-
-
-
phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase
-
-
-
-
phosphatidyl-myo-inositol-4,5-bisphosphate phosphohydrolase
-
-
-
-
phosphatidylinositol 4,5-bisphosphate phosphatase
-
-
-
-
phosphatidylinositol-bisphosphatase
-
-
-
-
Phosphoinositide 5-phosphatase
-
-
-
-
PIP2 phosphatase
-
-
-
-
PtdIns(4,5)P2 5-phosphatase
-
-
-
-
Synaptojanin
-
-
-
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triphosphoinositide phosphatase
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-
-
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triphosphoinositide phosphomonoesterase
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-
-
-
additional information
5PTase
-
-
-
-
additional information
cf. EC 3.1.3.56, inositol polyphosphate 5-phosphatase
additional information
-
the enzyme belongs to the endonuclease/exonuclease/phosphatase family
additional information
cf. EC 3.1.3.56, inositol polyphosphate 5-phosphatase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphatidyl-myo-inositol-4,5-bisphosphate 4-phosphohydrolase
These enzymes can also remove the 5-phosphate from Ins(1,4,5)P3 and/or Ins(1,3,4,5)P4. They are a diverse family of enzymes, with differing abilities to catalyse two or more of the four reactions listed. They are thought to use inositol lipids rather than inositol phosphates as substrates in vivo. All of them can use either or both of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 as substrates; this is the main property that distinguishes them from EC 3.1.3.56, inositol-polyphosphate 5-phosphatase.
CAS REGISTRY NUMBER
COMMENTARY
9036-01-5
-
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 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
recombinant enzyme
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
recombinant enzyme
-
-
?
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O
1D-myo-inositol 1,3,4-trisphosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
the enzyme is involved in regulation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate levels in stem
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
preferred substrate of the recombinant enzyme
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
best substrate
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
-
-
?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
-
-
?
additional information
?
-
the enzyme is essential in secondary cell wall synthesis in fiber cells and xylem vessels, enzyme deficiency causes a high reduction in secondary cell wall thickness and stem stability due to altered actin organization in fiber cells
-
-
?
additional information
?
-
-
the enzyme is essential in secondary cell wall synthesis in fiber cells and xylem vessels, enzyme deficiency causes a high reduction in secondary cell wall thickness and stem stability due to altered actin organization in fiber cells
-
-
?
additional information
?
-
substrate specificity, no activity with 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
-
-
?
additional information
?
-
-
substrate specificity, no activity with 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
-
-
?
additional information
?
-
substrate specificity, no activity with 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
-
-
?
additional information
?
-
-
substrate specificity, no activity with 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
-
-
?
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
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
the enzyme is involved in regulation of 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate levels in stem
-
-
?
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
-
-
-
?
additional information
?
-
the enzyme is essential in secondary cell wall synthesis in fiber cells and xylem vessels, enzyme deficiency causes a high reduction in secondary cell wall thickness and stem stability due to altered actin organization in fiber cells
-
-
?
additional information
?
-
-
the enzyme is essential in secondary cell wall synthesis in fiber cells and xylem vessels, enzyme deficiency causes a high reduction in secondary cell wall thickness and stem stability due to altered actin organization in fiber cells
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
growth kinetics of wild-type and sac9 mutant primary roots, phenotype and tissue organization, overview
additional information
expression of 5PTase13 is suppressed by blue light irradiation. Expression level of 5PTase13 is significantly enhanced in phototropin1 single or phototropin1 phototropin2 double mutants under blue light
additional information
-
expression of 5PTase13 is suppressed by blue light irradiation. Expression level of 5PTase13 is significantly enhanced in phototropin1 single or phototropin1 phototropin2 double mutants under blue light
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
-
nonredundant function of At5PTase7 in salt stress response by regulating ROS production and gene expression, involvement of the At5PTases in Arabidopsis salt tolerance, overview
malfunction
-
At5PTase7 mutants show reduced salt tolerance and increased salt stress response, phenotype, overview
malfunction
-
mutant sac9-1 plants have a constitutively stressed phenotype with shorter roots which notably accumulate phosphatidylinositol 4,5-bisphosphate and its hydrolysis product inositol trisphosphate, phenotype with extreme abnormalities of cell wall and membrane structures in sac9-1 primary root cells, regardless of cell type, position within the meristematic area, and plane of section, overview
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). IP5PF_ARATH
1101
0
121711
Swiss-Prot
other Location (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme is composed of two domains, an N-terminal WD-repeat domain and a C-terminal catalytic domain
additional information
-
the enzyme is composed of two domains, an N-terminal WD-repeat domain and a C-terminal catalytic domain
additional information
the enzyme contains a WD-repeat domain and a 5PTase catalytic domain, domain organization
additional information
-
the enzyme contains a WD-repeat domain and a 5PTase catalytic domain, domain organization
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of catalytically inactive fra3 missense mutants with an amino acid substitution in the conserved motif II of the catalytic domain, FRA3 overexpressing transgenic plants do not show a phenotype
additional information
-
construction of catalytically inactive fra3 missense mutants with an amino acid substitution in the conserved motif II of the catalytic domain, FRA3 overexpressing transgenic plants do not show a phenotype
additional information
disruption of the gene 5PTase13 results in shortened hypocotyls and expanded cotyledons. Suppression of 5PTase13 expression rescues the elongated hypocotyls in the phototropin1 or phototropin1 phototropin2 mutants. Further analysis shows that the blue light-induced elevation of cytosolic Ca2+ is inhibited in the phot1 mutant but enhanced in the 5pt13 mutant, suggesting that 5PTase13 antagonizes phototropin1-mediated effects on calcium signaling under blue light
additional information
-
disruption of the gene 5PTase13 results in shortened hypocotyls and expanded cotyledons. Suppression of 5PTase13 expression rescues the elongated hypocotyls in the phototropin1 or phototropin1 phototropin2 mutants. Further analysis shows that the blue light-induced elevation of cytosolic Ca2+ is inhibited in the phot1 mutant but enhanced in the 5pt13 mutant, suggesting that 5PTase13 antagonizes phototropin1-mediated effects on calcium signaling under blue light
additional information
-
random mutagensis and identification of mutant At5ptase7, that shows increased sensitivity, which is improved by overexpression. At5ptase7 mutants demonstrate reduced production of reactive oxygen species, phenotype, overview. Supplementation of mutants with exogenous PtdIns dephosphorylated at the D5' position restores ROS production, while PtdIns(4,5)P2, PtdIns(3,5)P2, or PtdIns(3,4,5)P3 are ineffective
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from yeast by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene fra3, expression pattern, DNA and amino acid sequence determination and analysis, complementation of an enzyme-deficient mutant
full-length 5PTase13-encoding sequence is N-terminally fused to a polyhistidinetag and a T7-tag and expressed in Escherichia coli cells
gene 5PTase14, DNA and amino acid sequence determination and analysis, genetic organization, expression of His-tagged full length enzyme in yeast
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhong, R.; Burk, D.H.; Morrison, W.H., 3rd; Ye, Z.H.
FRAGILE FIBER3, an Arabidopsis gene encoding a type II inositol polyphosphate 5-phosphatase, is required for secondary wall synthesis and actin organization in fiber cells
Plant Cell
16
3242-3259
2004
Arabidopsis thaliana (Q84W55), Arabidopsis thaliana
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 (Q9SKB7), Arabidopsis thaliana
Chen, X.; Lin, W.H.; Wang, Y.; Luan, S.; Xue, H.W.
An inositol polyphosphate 5-phosphatase functions in PHOTOTROPIN1 signaling in Arabidopis by altering cytosolic Ca2+
Plant Cell
20
353-366
2008
Arabidopsis thaliana (Q9SYK4), Arabidopsis thaliana
Kaye, Y.; Golani, Y.; Singer, Y.; Leshem, Y.; Cohen, G.; Ercetin, M.; Gillaspy, G.; Levine, A.
Inositol polyphosphate 5-phosphatase7 regulates the production of reactive oxygen species and salt tolerance in Arabidopsis
Plant Physiol.
157
229-241
2011
Arabidopsis thaliana
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