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Information on EC 2.7.1.150 - 1-phosphatidylinositol-3-phosphate 5-kinase and Organism(s) Mus musculus and UniProt Accession Q9Z1T6

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Mus musculus
UNIPROT: Q9Z1T6 not found.
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
pikfyve, ste12, fab1p, pip5k3, fab1/pikfyve, phosphatidylinositol 3-phosphate 5-kinase, ppk-3, phosphatidylinositol-3-phosphate-5-kinase pikfyve, ptdins3p 5-kinase, cgfab1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PtdIns 3-phosphate 5-kinase
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Fab1p
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kinase (phosphorylating), phosphatidylinositol 3-phosphate 5-
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phosphatidylinositol 3-phosphate 5-kinase
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phosphatidylinositol 5-OH kinase
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Phosphatidylinositol-3-phosphate 5-kinase
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PI(3)P-5-kinase
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PIKfyve
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PtdIns(3) 5-kinase
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PtdIns3P 5-OH kinase
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type III PIP kinase
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additional information
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the enzyme belongs to the type III PIPkin family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho-group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP:1-phosphatidyl-1D-myo-inositol-3-phosphate 5-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
190606-24-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
show the reaction diagram
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?
ATP + 1-phosphatidyl-1D-myo-inositol
ADP + 1-phosphatidyl-1D-myo-inositol 5-phosphate
show the reaction diagram
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recombinant enzyme
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-
?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
show the reaction diagram
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
show the reaction diagram
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recombinant enzyme
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?
additional information
?
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substrate specificity in descending order: 1-phosphatidyl-1D-myo-inositol 3-phosphate, 1-phosphatidyl-1D-myo-inositol 4-phosphate, and 1-phosphatidyl-1D-myo-inositol, the enzyme also shows lipid kinase activity
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
show the reaction diagram
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?
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
show the reaction diagram
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regulation of 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate synthesis involving osmotic stress, interleukins, UV radiation, and autophosphorylation, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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enzyme synthesis is stimulated by a hyperosmotic shock and UV radiation
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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enzyme is not localized in the Golgi apparatus, recycling endosomes, or lysosomes
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the vacuolation phenotype in cultured Vps34 (EC 2.7.1.137)-deficient podocytes is caused by the absence of a substrate for the Vps34 downstream effector PtdIns 3-phosphate 5-kinase, which phosphorylates Vps34-generated 1-phosphatidyl-1D-myo-inositol 3-phosphate to produce + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate. PtdIns 3-phosphate 5-kinase perturbation and 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate reduction result in massive membrane vacuolation along the endosomal system. Genetic deletion of the enzyme in endocytically active proximal tubular cells results in the development of large cytoplasmic vacuoles caused by arrested endocytic traffic progression at a late-endosome stage, while deletion of the enzyme in glomerular podocytes does not significantly alter the endosomal morphology, even in age 18-month-old mice
physiological function
in Xenopus oocytes expressing mammalian excitatory amino acid transporter EAAT4, glutamate induces a current which is significantly enhanced by coexpression of isoform PIKfyve and glucocorticoid inducible kinase SGK1. This glutamate-induced current is significantly larger than the current in Xenopus oocytes expressing EAAT4 together with either kinase alone. Coexpression of the inactive SGK1 mutant K127N does not significantly alter glutamate-induced current in EAAT4-expressing Xenopus oocytes and abolishes the stimulation of glutamate-induced current by coexpression of isoform PIKfyve. The stimulating effect of PIKfyve is abrogated by mutation S318A in the SGK consensus sequence of PIKfyve. Coexpression of PIKfyve S318A mutant significantly blunts the stimulating effect of SGK1 on EAAT4 activity
physiological function
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PIKFYVE knockdown produces a 36% reduction in phosphatidylinositol 3,5-bisphosphate and a 13% increase in phosphatidylinositol 3-phosphate. PIKFYVE and class II phosphatidylinositol 3-kinase PI3K-C2alpha are necessary for activation of the kinase complex mechanistic target of rapamycin mTORC1 and its translocation to the plasma membrane in 3T3-L1 adipocytes. The mTORC1 component Raptor directly interacts with phosphatidylinositol 3,5-bisphosphate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FYV1_MOUSE
2097
0
236877
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the PIPkin type III family enzyme consists of 4 typical domains: the FYVE RING Zn-finger domain, the TCP-I/chaperone-like domain, the PIPkin domain, and the cysteine-rich domain, the mouse enzyme contains additionally a DEP domain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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the enzyme downregulates its own activity by autophosphorylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S318A
in Xenopus oocytes expressing mammalian excitatory amino acid transporter EAAT4, glutamate induces a current which is significantly enhanced by coexpression of isoform PIKfyve and glucocorticoid inducible kinase SGK1. The stimulating effect of PIKfyve is abrogated by mutation S318A in the SGK consensus sequence of PIKfyve. Coexpression of PIKfyve S318A mutant significantly blunts the stimulating effect of SGK1 on EAAT4 activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of the enzmye fused to EGFP in COS-7 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cooke, F.T.
Phosphatidylinositol 3,5-bisphosphate: metabolism and function
Arch. Biochem. Biophys.
407
143-151
2002
Arabidopsis thaliana, Caenorhabditis elegans, Candida albicans, Drosophila melanogaster, Homo sapiens, Mus musculus, Oryza sativa, Schizosaccharomyces pombe, Saccharomyces cerevisiae (P34756)
Manually annotated by BRENDA team
Alesutan, I.S.; Ureche, O.N.; Laufer, J.; Klaus, F.; Zuern, A.; Lindner, R.; Strutz-Seebohm, N.; Tavare, J.M.; Boehmer, C.; Palmada, M.; Lang, U.E.; Seebohm, G.; Lang, F.
Regulation of the glutamate transporter EAAT4 by PIKfyve
Cell. Physiol. Biochem.
25
187-194
2010
Mus musculus (Q9Z1T6)
Manually annotated by BRENDA team
Bridges, D.; Ma, J.T.; Park, S.; Inoki, K.; Weisman, L.S.; Saltiel, A.R.
Phosphatidylinositol 3,5-bisphosphate plays a role in the activation and subcellular localization of mechanistic target of rapamycin 1
Mol. Biol. Cell
23
2955-2962
2012
Mus musculus
Manually annotated by BRENDA team
Venkatareddy, M.; Verma, R.; Kalinowski, A.; Patel, S.R.; Shisheva, A.; Garg, P.
Distinct requirements for vacuolar protein sorting 34 downstream effector phosphatidylinositol 3-phosphate 5-kinase in podocytes versus proximal tubular cells
J. Am. Soc. Nephrol.
27
2702-2719
2016
Mus musculus (Q9Z1T6)
Manually annotated by BRENDA team