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FUNCTION Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate (PubMed:11733541, PubMed:12668758, PubMed:14690594, PubMed:21372139). Regulates the level of these phosphoinositides critical for various biological processes including autophagy initiation and autophagosome maturation (PubMed:35580604).CATALYTIC ACTIVITY a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphateCATALYTIC ACTIVITY a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphateCATALYTIC ACTIVITY 1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphateCATALYTIC ACTIVITY 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphateSUBUNIT Homodimer (via coiled-coil domain) (PubMed:12668758, PubMed:15998640). Heterotetramer consisting of one MTMR2 dimer and one SBF2/MTMR13 dimer; specifically in peripheral nerves stabilizes SBF2/MTMR13 at the membranes and increases MTMR2 catalytic activity towards phosphatidylinositol 3,5-bisphosphate and to a lesser extent towards phosphatidylinositol 3-phosphate (PubMed:15998640, PubMed:34718573). Heterodimer with SBF1/MTMR5; acts as an adapter for the phosphatase MTMR2 to regulate MTMR2 catalytic activity and subcellular location (PubMed:12668758, PubMed:21372139, PubMed:34718573). Heterodimer with MTMR12 (PubMed:12847286).INTERACTION Partly associated with membranes (PubMed:12668758, PubMed:15998640, PubMed:21372139). Localizes to vacuoles in hypo-osmotic conditions (By similarity).ALTERNATIVE PRODUCTS The coiled-coil domain mediates homodimerization (PubMed:12668758, PubMed:15998640). Also mediates interaction with SBF1/MTMR5 (PubMed:12668758). By mediating MTMR2 homodimerization, indirectly involved in SBF2/MTMR13 and MTMR2 heterotetramerization (By similarity).DOMAIN The GRAM domain mediates binding to phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate.PTM Phosphorylation at Ser-58 decreases MTMR2 localization to endocytic vesicular structures.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the protein-tyrosine phosphatase family. Non-receptor class myotubularin subfamily.
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