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Information on EC 3.1.3.56 - inositol-polyphosphate 5-phosphatase and Organism(s) Mus musculus
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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
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ptdins4,5p2
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3hinositol
- 2,3-bisphosphoglycerate
- inpp5f
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ptdins3,4,5p3
- medicine
- molecular biology
The taxonomic range for the selected organisms is: Mus musculus
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, 5pt13, inpp5j, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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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 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
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additional information
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the enzyme binds to PRIP-1, a Ins(1,4,5)P3-binding protein, via the protein's PH-domain, which inhibits the enzyme activity
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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
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the enzyme is involved in Ins(1,4,5)P3-mediated Ca2+ signaling associated to PRIP-1, a Ins(1,4,5)P3-binding protein, overview
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?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
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?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
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regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
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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
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
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?
1D-myo-inositol 1,4,5-trisphosphate + H2O
1D-myo-inositol 1,4-bisphosphate + phosphate
-
the enzyme is involved in Ins(1,4,5)P3-mediated Ca2+ signaling associated to PRIP-1, a Ins(1,4,5)P3-binding protein, overview
-
-
?
D-myo-inositol 1,4,5-trisphosphate + H2O
D-myo-inositol 1,4-bisphosphate + phosphate
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regulation of intracellular Ca2+ level by degradation of intracellular Ca2+ releasing second messenger D-myo-inositol 1,4,5-trisphosphate
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protein PRIP-1
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binding to PRIP-1, a Ins(1,4,5)P3-binding protein, inhibits the enzyme in vitro, in vivo binding of Ins(1,4,5)P3 to PRIP-1 prevents it from being hydrolyzed by the enzyme, PRIP-1 has a domain organization similar to phospholipase C-delta1, interaction analysis, overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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the enzyme links endoplasmic reticulum stress to insulin resistance in skeletal muscle
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). PI5PA_MOUSE
1003
0
107544
Swiss-Prot
other Location (Reliability: 4)
SHIP1_MOUSE
1191
0
133542
Swiss-Prot
other Location (Reliability: 3)
OCRL_MOUSE
900
0
104285
Swiss-Prot
other Location (Reliability: 2)
I5P1_MOUSE
412
0
47622
Swiss-Prot
Secretory Pathway (Reliability: 4)
INP5K_MOUSE
468
0
54159
Swiss-Prot
other Location (Reliability: 4)
Q3TZT4_MOUSE
420
0
48960
TrEMBL
Secretory Pathway (Reliability: 2)
V9GXL7_MOUSE
548
0
60904
TrEMBL
Mitochondrion (Reliability: 5)
A0A075B6D7_MOUSE
899
0
96807
TrEMBL
other Location (Reliability: 4)
Q3TBW1_MOUSE
1003
0
107514
TrEMBL
other Location (Reliability: 4)
A0PJC0_MOUSE
905
0
97576
TrEMBL
other Location (Reliability: 4)
Q5ND43_MOUSE
468
0
54159
TrEMBL
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D232A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is increased due to endoplasmic reticulum stress and is higher in the skeletal muscle isolated from high-fat-diet-fed mice and db/db mice than in that from wild type mice. Enzyme protein expression is increased by the expression of transcription factors ATF6alpha and XBP1
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Whisstock, J.C.; Romero, S.; Gurung, R.; Nandurkar, H.; Ooms, L.M.; Bottomley, S.P.; Mitchell, C.A.
The inositol polyphosphate 5-phosphatases and the apurinic/apyrimidinic base excision repair endonucleases share a common mechanism for catalysis
J. Biol. Chem.
275
37055-37061
2000
Mus musculus, Saccharomyces cerevisiae
Harada, K.; Takeuchi, H.; Oike, M.; Matsuda, M.; Kanematsu, T.; Yagisawa, H.; Nakayama, K.I.; Maeda, K.; Erneux, C.; Hirata, M.
Role of PRIP-1, a novel Ins(1,4,5)P3 binding protein, in Ins(1,4,5)P3-mediated Ca2+ signaling
J. Cell. Physiol.
202
422-433
2005
Mus musculus
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