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 (PubMed:9210593, PubMed:29392776, PubMed:15938621). Has a higher efficiency with cGMP compared to cAMP (PubMed:15938621). Plays a role in cell growth and migration (PubMed:24705027). 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. kcat is 0.6 sec(-1) with 3',5'-cyclic GMP as substrate (PubMed:15938621). kcat is 0.12 sec(-1) with 3',5'-cyclic AMP as substrate (PubMed:15938621). Homodimer. Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms. Widely expressed (PubMed:9210593, PubMed:29392776). Expressed in brain, with high expression observed in the corpus striatum (PubMed:29392776). Also expressed in heart, placenta, lung, skeletal muscle, kidney and pancreas (PubMed:9210593, PubMed:29392776). The GAF 1 domain functions as a dimerization domain. The GAF 2 domains binds cGMP, which acts as an allosteric activator. The disease is caused by variants affecting the gene represented in this entry. Soluble form. Contains a transit peptide at positions 1-17. Belongs to the cyclic nucleotide phosphodiesterase family. PDE2 subfamily.