LIPID MAPS® Gene/Proteome Database (LMPD)

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LMPD Record

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LMP007276

UniProt Annotations

Entry Information
Gene Namephosphatidylinositol-3,5-bisphosphate 5-phosphatase
Protein EntryFIG4_YEAST
UniProt IDP42837
SpeciesYeast (S288c)
Comments
Comment typeDescription
Catalytic Activity1-phosphatidyl-1D-myo-inositol 3,5- bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate. {ECO:0000269|PubMed:14528018}.
CofactorName=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:14528018};
FunctionThe PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Major enzyme required for hyperosmotic shock- induced turnover of PtdIns(3,5)P2 and requires VAC14 for this function. In vivo, mediates turnover of PtdIns(3,5)P2 at the vacuole membrane necessary for vacuolar size control. In vitro, catalyzes the removal of phosphate from the fifth hydroxyl of the myo-inositol ring of phosphatidylinositol 3,5-bisphosphate. {ECO:0000269|PubMed:11950935, ECO:0000269|PubMed:14528018, ECO:0000269|PubMed:16492811, ECO:0000269|PubMed:19037259}.
InteractionP34756:FAB1; NbExp=4; IntAct=EBI-28407, EBI-6754; Q06708:VAC14; NbExp=7; IntAct=EBI-28407, EBI-27189;
MiscellaneousPresent with 339 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
SimilarityContains 1 SAC domain. {ECO:0000255|PROSITE- ProRule:PRU00183}.
Subcellular LocationVacuole membrane {ECO:0000269|PubMed:11950935, ECO:0000269|PubMed:14528018, ECO:0000269|PubMed:18653468, ECO:0000269|PubMed:19037259}; Peripheral membrane protein {ECO:0000269|PubMed:11950935, ECO:0000269|PubMed:14528018, ECO:0000269|PubMed:18653468, ECO:0000269|PubMed:19037259}. Note=Localized to the limiting membrane of the vacuole. Localization requires VAC14 and FAB1.
SubunitComponent of the PI(3,5)P2 regulatory complex, composed of ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly of the complex and serves as a scaffold. {ECO:0000269|PubMed:18653468, ECO:0000269|PubMed:19037259}.