Polyamine deacetylase (PDAC), which acts preferentially on N(8)-acetylspermidine, and also on acetylcadaverine and acetylputrescine . Exhibits attenuated catalytic activity toward N(1),N(8)-diacetylspermidine and very low activity, if any, toward N(1)-acetylspermidine . Histone deacetylase activity has been observed in vitro ( , ). Has also been shown to be involved in MSH2 deacetylation . The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak . May play a role in the promotion of late stages of autophagy, possibly autophagosome-lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells (, ). May play a role in homologous recombination . May promote DNA mismatch repair .
Subcellular locations: Cytoplasm, Nucleus
Excluded from nucleoli.
Widely expressed with high levels in liver and kidney.