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. By dephosphorylating PtdIns(3,4,5)P3 antagonizes PtdIns(3,4,5)P3 production by age-1/PI3K and thus, negatively regulates daf-2-mediated processes including dauer formation, longevity, fat metabolism, chemotaxis towards salt, thermotolerance and axon guidance. Similarly, promotes apoptosis during embryonic development by suppressing the recruitment of the prosurvival kinases akt-1/2 to the plasma membrane. In addition, regulates Z2/Z3 germline precursor cell cycle by maintaining them arrested at the G2 stage and by controlling their growth during L1 diapause. After sperm depletion in larvae and adult hermaphrodites, promotes germline stem cell quiescence and oocyte accumulation. By dephosphorylating ephrin-like receptor vab-1 on tyrosine residues, negatively regulates oocyte maturation downstream of vab-1 and upstream of mpk-1, independently of daf-2. Plays a role in postembryonic muscle arm extensions. Required for neurite outgrowth during AIY interneuron embryonic development. Mainly independently of daf-2, negatively regulates vulva induction probably by inhibiting mpk-1 phosphorylation. Both lipid and protein phosphatase activities are required for the regulation of vulva induction.