Based on limited published evidence, ADPRM is a manganese-dependent phosphohydrolase that hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-choline, and CDP-ethanolamine. The enzyme contains signature metal-dependent phosphatase domains and is localized to the cytosol 1. ADPRM displays phosphohydrolytic activity on cyclic ADP-ribose and 2',3'-cAMP, with substrate specificity conferred by residues Phe37, Arg43, and Cys253 in the active site region 1. The protein is preferentially expressed in immune cells and may function in immune signaling through ADP-ribose metabolism, which can activate TRPM2 channels as a mediator of oxidative/nitrosative stress.