UniProt ID: Q2I6J0 |
FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin. Regulates cell adhesion and cell spreading. Acts as a negative regulator of the FC- gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6 (By similarity). {ECO:0000250|UniProtKB:O15357}. 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-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658, ChEBI:CHEBI:57836; EC=3.1.3.86; Evidence={ECO:0000250|UniProtKB:O15357}; SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9WVR3}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q9WVR3}; Peripheral membrane protein {ECO:0000250}. Cell projection, filopodium {ECO:0000250|UniProtKB:O15357}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O15357}. Nucleus {ECO:0000250|UniProtKB:D7PF45}. Nucleus speckle {ECO:0000250|UniProtKB:D7PF45}. Note=Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. {ECO:0000250}. DOMAIN: The SH2 domain interacts with tyrosine phosphorylated forms of proteins. {ECO:0000250|UniProtKB:O15357}. DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. {ECO:0000250|UniProtKB:O15357}. PTM: Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli. SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family. {ECO:0000305}. |
UniProt ID: A0A8M1N8H7 |
SUBCELLULAR LOCATION: Cell projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}. SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family. {ECO:0000256|ARBA:ARBA00008734}. |
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