UniProt ID: Q7ZZ56 |
FUNCTION: Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5- trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. {ECO:0000256|PIRNR:PIRNR038025}. CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo- inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero- 3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43560, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83420, ChEBI:CHEBI:83423; Evidence={ECO:0000256|ARBA:ARBA00034256}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43561; Evidence={ECO:0000256|ARBA:ARBA00034256}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5- trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo- inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43552, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416, ChEBI:CHEBI:83419; Evidence={ECO:0000256|ARBA:ARBA00034268}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43553; Evidence={ECO:0000256|ARBA:ARBA00034268}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000256|ARBA:ARBA00001512, ECO:0000256|PIRNR:PIRNR038025}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000256|ARBA:ARBA00001482, ECO:0000256|PIRNR:PIRNR038025}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000256|ARBA:ARBA00001490, ECO:0000256|PIRNR:PIRNR038025}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5- trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456; EC=3.1.3.67; Evidence={ECO:0000256|ARBA:ARBA00000536, ECO:0000256|PIRNR:PIRNR038025}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946}; SUBCELLULAR LOCATION: Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}. Cytoplasm {ECO:0000256|PIRNR:PIRNR038025}. Nucleus {ECO:0000256|PIRNR:PIRNR038025}. Nucleus, PML body {ECO:0000256|PIRNR:PIRNR038025}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}. SIMILARITY: Belongs to the PTEN phosphatase protein family. {ECO:0000256|ARBA:ARBA00007881, ECO:0000256|PIRNR:PIRNR038025}. |
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