cGMP-activated cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a higher efficiency with cGMP compared to cAMP (By similarity). Plays a role in cell growth and migration (By similarity). Regulates mitochondrial cAMP levels and respiration (By similarity). Involved in the regulation of mitochondria morphology/dynamics and apoptotic cell death via local modulation of cAMP/PKA signaling in the mitochondrion, including the monitoring of local cAMP levels at the outer mitochondrial membrane and of PKA-dependent phosphorylation of Dnm1l (PubMed:28463107). a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+) 3',5'-cyclic GMP + H2O = GMP + H(+) 3',5'-cyclic AMP + H2O = AMP + H(+) Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions. Binds 2 divalent metal cations per subunit. Site 2 has a preference for magnesium ions. The 3',5'-cyclic-AMP phosphodiesterase activity is stimulated by 3',5'-cyclic GMP (By similarity). Specifically inhibited by Bay 60-7550. When repressed, protected from ionomycin- but not staurosporin-induced cell death. Homodimer. Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms. Expressed in brain and liver. The GAF 1 domain functions as a dimerization domain. The GAF 2 domains binds cGMP, which acts as an allosteric activator. Belongs to the cyclic nucleotide phosphodiesterase family. PDE2 subfamily.