Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
Also known as: PDE1A
Function
Calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cGMP and cAMP, which are key regulators of many important physiological processes. Has a higher efficiency with cGMP compared to cAMP.
Classification
- Family (Pfam)
- PF00233 PDEase_I, PF08499 PDEase_I_N
- InterPro
- HD/PDEase_dom, PDE1_N, PDEase, PDEase_catalytic_dom, PDEase_catalytic_dom_sf, PDEase_CS
- Functional cluster
- Mixed Regulatory & Membrane Proteins
Gene Ontology · 11
- GO:0005829 cytosol
- GO:0043025 neuronal cell body
- GO:0005516 calmodulin binding
- GO:0048101 calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity
- GO:0004117 calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity
- GO:0046872 metal ion binding
- GO:0046069 cGMP catabolic process
- GO:0141162 negative regulation of cAMP/PKA signal transduction
- GO:0034391 regulation of smooth muscle cell apoptotic process
- GO:0048660 regulation of smooth muscle cell proliferation
- GO:0007165 signal transduction
Drugs targeting this protein · 2
- PENTOXIFYLLINE inhibitor
- DIPYRIDAMOLE inhibitor
Related proteins · sequence + function similarity
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A 0.99
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A 0.99
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B 0.96
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B 0.95
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B 0.95
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B 0.95
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B 0.95
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C 0.89
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C 0.89
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C 0.88
- Probable 3',5'-cyclic phosphodiesterase pde-1 0.80
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1 0.71
Co-cited proteins · studied together in the literature
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C 1 shared papers
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B 1 shared papers
- Adenylate kinase isoenzyme 5 1 shared papers
- Adenylate kinase isoenzyme 5 1 shared papers
- LIM domain-binding protein 1 1 shared papers
- Rho guanine nucleotide exchange factor 7 1 shared papers
- MAP kinase-activating death domain protein 1 shared papers
- 14-3-3 protein zeta/delta 1 shared papers
- MAP/microtubule affinity-regulating kinase 4 1 shared papers
- MAP/microtubule affinity-regulating kinase 3 1 shared papers
- ARF GTPase-activating protein GIT1 1 shared papers
- 14-3-3 protein zeta/delta 1 shared papers
Literature · 6 cited papers
- The full-ORF clone resource of the German cDNA consortium. BMC Genomics · 2007
- Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling. Mol. Cell. Proteomics · 2006
- The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. · 2004
- Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants. Cell. Signal. · 2002
- Human Ca2+/calmodulin-dependent phosphodiesterase PDE1A: novel splice variants, their specific expression, genomic organization, and chromosomal localization. Biochim. Biophys. Acta · 2001
- Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J. Biol. Chem. · 1996
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