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EC Tree
IUBMB 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.
Word Map
3.1.3.36
endocytosis
phosphatases
synaptic
domain-containing
actin
pten
3-kinase
endocytic
x-linked
ptdins3,4,5p3
cataract
clathrin
dynamin
cilia
clathrin-mediated
tensin
polyphosphoinositide
dent
clathrin-coated
endophilins
voltage-sensing
joubert
amphiphysins
ciliopathies
ptdins3,4p2
ptdins4p
1,3,4,5-tetrakisphosphate
itims
fcgammariib
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: Drosophila melanogaster The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ship2, ship1, ocrl1, synaptojanin, inpp5e, synj1, phosphoinositide phosphatase, inositol polyphosphate 5-phosphatase, inositol 5-phosphatase, ci-vsp,
more
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diphosphoinositide phosphatase
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dOCRL
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orthologue of the human oculocerebrorenal syndrome of Lowe 1, i.e. OCRL1
inositol 5-phosphatase
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inositol triphosphate 5-phosphomonoesterase
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Lowe's oculocerebrorenal syndrome protein
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phosphatase, triphosphoinositide
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phosphatidyl 4,5-bisphosphate-specific phosphomonoesterase
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phosphatidyl bisphosphate phosphatase
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phosphatidyl-inositol 4,5-bisphosphate 5-phosphatase
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phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase
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phosphatidyl-myo-inositol-4,5-bisphosphate phosphohydrolase
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phosphatidylinositol 4,5-bisphosphate phosphatase
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phosphatidylinositol-bisphosphatase
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Phosphoinositide 5-phosphatase
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PtdIns(4,5)P2 5-phosphatase
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triphosphoinositide phosphatase
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triphosphoinositide phosphomonoesterase
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PIP2 phosphatase
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hydrolysis of phosphoric ester
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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.
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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
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1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
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1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate is required for formation, polarization, and elongation of spermatid cysts, overview
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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
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1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate
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1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate is required for formation, polarization, and elongation of spermatid cysts, overview
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brenda
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brenda
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dOCRL is associated with endosomes
brenda
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dOCRL dephosphorylates PI(4,5)P2 on internal membranes
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brenda
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physiological function
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dOCRL is essential for cytokinesis and cell division, it dephosphorylates phosphatidylinositol-4,5-bisphosphate on internal membranes to restrict this phosphoinositide at the plasma membrane and thereby regulates cleavage furrow formation and ingression. dOCRL is required for proper furrowing of the contractile ring and proper assembly
malfunction
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in absence of dOCRL, several essential components of the cleavage furrow are found to be incorrectly localized on giant cytoplasmic vacuoles rich in PI(4,5)P2 and in endocytic markers
malfunction
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reduction of plasma membrane phosphatidylinositol 4,5-bisphosphate by low-level expression of the PIP2 phosphatase SigD or mutation of the PIP2 biosynthetic enzyme Skittles results in dramatic defects in spermatid cysts, which become bipolar and fail to fully elongate
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INP5E_DROME
747
0
82590
Swiss-Prot
other Location (Reliability: 4 )
O46094_DROME
850
0
97530
TrEMBL
other Location (Reliability: 2 )
Q5U0V7_DROME
1218
0
134599
TrEMBL
other Location (Reliability: 3 )
A0A0B4K7D8_DROME
348
0
39669
TrEMBL
Secretory Pathway (Reliability: 1 )
Q8MR94_DROME
959
0
105687
TrEMBL
other Location (Reliability: 4 )
M9PHS8_DROME
519
0
60183
TrEMBL
other Location (Reliability: 1 )
Q7K161_DROME
357
0
40498
TrEMBL
Secretory Pathway (Reliability: 1 )
Q9VXE7_DROME
508
0
58973
TrEMBL
other Location (Reliability: 1 )
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Ben El Kadhi, K.; Roubinet, C.; Solinet, S.; Emery, G.; Carreno, S.
The inositol 5-phosphatase dOCRL controls PI(4,5)P2 homeostasis and is necessary for cytokinesis
Curr. Biol.
21
1074-1079
2011
Drosophila melanogaster
brenda
Fabian, L.; Wei, H.; Rollins, J.; Noguchi, T.; Blankenship, J.; Bellamkonda, K.; Polevoy, G.; Gervais, L.; Guichet, A.; Fuller, M.; Brill, J.
Phosphatidylinositol 4,5-bisphosphate directs spermatid cell polarity and exocyst localization in Drosophila
Mol. Biol. Cell
21
1546-1555
2010
Drosophila melanogaster
brenda