ID PDE3A_MOUSE Reviewed; 1141 AA. AC Q9Z0X4; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 16-JUN-2009, entry version 56. DE RecName: Full=cGMP-inhibited 3',5'-cyclic phosphodiesterase A; DE EC=3.1.4.17; DE AltName: Full=Cyclic GMP-inhibited phosphodiesterase A; DE Short=CGI-PDE A; GN Name=Pde3a; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Ovary; RA Shitsukawa K., Andersen C.B., Richard F.J., Conti M.; RT "Characterization of cGMP-inhibited phosphodiesterase (PDE3A) RT expressed in mouse oocyte."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). CC -!- FUNCTION: Hydrolyzes both cyclic AMP (cAMP) and cyclic GMP (cGMP) CC (By similarity). CC -!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O = CC nucleoside 5'-phosphate. CC -!- ENZYME REGULATION: Inhibited by cGMP (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF099187; AAD16300.1; -; mRNA. DR IPI; IPI00129586; -. DR RefSeq; NP_061249.1; -. DR UniGene; Mm.103728; -. DR UniGene; Mm.393561; -. DR HSSP; Q08499; 1MKD. DR SMR; Q9Z0X4; 677-1049. DR PhosphoSite; Q9Z0X4; -. DR PRIDE; Q9Z0X4; -. DR Ensembl; ENSMUSG00000041741; Mus musculus. DR GeneID; 54611; -. DR KEGG; mmu:54611; -. DR MGI; MGI:1860764; Pde3a. DR HOGENOM; Q9Z0X4; -. DR HOVERGEN; Q9Z0X4; -. DR OMA; Q9Z0X4; DSGFTHG. DR BRENDA; 3.1.4.17; 244. DR NextBio; 311416; -. DR ArrayExpress; Q9Z0X4; -. DR Bgee; Q9Z0X4; -. DR CleanEx; MM_PDE3A; -. DR GO; GO:0005626; C:insoluble fraction; IDA:MGI. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005625; C:soluble fraction; IDA:MGI. DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:MGI. DR GO; GO:0001556; P:oocyte maturation; IDA:MGI. DR GO; GO:0040020; P:regulation of meiosis; IDA:MGI. DR GO; GO:0042493; P:response to drug; IDA:MGI. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR003607; Met-dep_phosphohydro_HD. DR InterPro; IPR002073; PDEase. DR Pfam; PF00233; PDEase_I; 1. DR SMART; SM00471; HDc; 1. DR PROSITE; PS00126; PDEASE_I; 1. PE 1: Evidence at protein level; KW cGMP; Hydrolase; Membrane; Phosphoprotein. FT CHAIN 1 1141 cGMP-inhibited 3',5'-cyclic FT phosphodiesterase A. FT /FTId=PRO_0000198800. FT MOD_RES 310 310 Phosphoserine (By similarity). FT MOD_RES 425 425 Phosphoserine (By similarity). FT MOD_RES 437 437 Phosphothreonine (By similarity). FT MOD_RES 495 495 Phosphoserine. SQ SEQUENCE 1141 AA; 124513 MW; 3D9ACCFF928219D8 CRC64; MAVRGEAAQD LAKPGLGGAS PARVARGNHR HRGESSPSPR GSGCCWRALA LQPLRRSPQL SSALCAGSLS VLLALLVRLV GGEVGGELEK SQEAAAEEEE EEGARGGVFP GPRGGAPGGG AQLSPWLQPA ALLFSLLCAF FWMGLCLLRA GVRLPLAVAL LAACCAGEAL VQLSLGVGDG RLLSLPAAGV LLSCLGGATW LVLRLRLGVL MVAWTSVLRT VALVSLERFK VAWRPYLAYL AAVLGLLLAR YAEQILPQCS GPAPPRERFG SQLSARTKEE IPGWKRRRRS SSVVAGEMSG CSGKSHRRTS LPCIPREQLM GHSEWDHKRG PRGSQSGTSI TVDIAVMGEA HGLITDLLAD PSLPPNVCTS LRAVSNLLST QLTFQAIHKP RVNPTVTFSE NYTCSDSEEG LEKDKQAISK RLRRSLPPGL LRRVSSTWTT TTSATGLPTL EPAPVRRDRS ASIKPHEAPS PSAVNPDSWN APGLTTLTKS RSFTSSYAVS AANHVKAKKQ NRPGGLAKIS PVPSPSSSPP QGSPASSPVS NSASQQFPES PEVTIKRGPG SHRALTYTQS APDLSPQIPP PSVICSSCGR PYSQGNPADG PSERSGPAML KPNRTDDTSQ VTSDYETNNN SDSSDILQNE EEAECQREPQ RKASACGTYT SQTMIFLDKP ILAPEPLVMD NLDSIMDQLN TWNFPIFDLM ENIGRKCGRI LSQVSYRLFE DMGLFEAFKI PVREFMNYFH ALEIGYRDIP YHNRIHATDV LHAVWYLTTQ PIPGLPSVIG DHGSASDSDS DSGFTHGHMG YVFSKMYHVP DDKYGCLSGN IPALELMALY VAAAMHDYDH PGRTNAFLVA TSAPQAVLYN DRSVLENHHA AAAWNLFMSR PEYNFLVNLD HVEFKHFRFL VIEAILATDL KKHFDFVAKF NAKVNDDVGI DWTNENDRLL VCQMCIKLAD INGPAKCKEL HLRWTEGIAS EFYEQGDEEA SLGLPISPFM DRSAPQLANL QESFISHIVG PLCHSYDSAG LMPGKWVDDS DDSGDTDDPE EEEEEAETPH EDEACESSIA PRKKSFKRRR IYCQITQHLL QNHMMWKKVI EEEQCLSGTE NQSLDQVPLQ HPSEQIQAIK EEEEEKGKPR AEETLAPQPD L //