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cGMP-inhibited 3',5'-cyclic phosphodiesterase A (EC 3.1.4.17) (Cyclic GMP-inhibited phosphodiesterase A) (CGI-PDE A)

 PDE3A_RAT               Reviewed;        1141 AA.
Q62865;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 127.
RecName: Full=cGMP-inhibited 3',5'-cyclic phosphodiesterase A;
EC=3.1.4.17;
AltName: Full=Cyclic GMP-inhibited phosphodiesterase A;
Short=CGI-PDE A;
Name=Pde3a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adipose tissue;
PubMed=9631240; DOI=10.1007/BF02737830;
He R., Komas N., Ekholm D., Murata T., Taira M., Hockman S.C.,
Degerman E., Manganiello V.C.;
"Expression and characterization of deletion recombinants of two cGMP-
inhibited cyclic nucleotide phosphodiesterases (PDE-3).";
Cell Biochem. Biophys. 29:89-111(1998).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-
specificity for the second messengers cAMP and cGMP, which are key
regulators of many important physiological processes.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
nucleoside 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=Binds 2 divalent metal cations per subunit. Site 1 may
preferentially bind zinc ions, while site 2 has a preference for
magnesium and/or manganese ions. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by cGMP.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE3 subfamily. {ECO:0000305}.
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EMBL; U38179; AAA84964.1; -; mRNA.
RefSeq; NP_059033.1; NM_017337.1.
UniGene; Rn.44403; -.
ProteinModelPortal; Q62865; -.
SMR; Q62865; -.
STRING; 10116.ENSRNOP00000032282; -.
PhosphoSitePlus; Q62865; -.
PaxDb; Q62865; -.
PRIDE; Q62865; -.
Ensembl; ENSRNOT00000032843; ENSRNOP00000032282; ENSRNOG00000025042.
GeneID; 50678; -.
KEGG; rno:50678; -.
UCSC; RGD:61942; rat.
CTD; 5139; -.
RGD; 61942; Pde3a.
eggNOG; ENOG410IEGG; Eukaryota.
eggNOG; ENOG410XT2V; LUCA.
GeneTree; ENSGT00760000119066; -.
HOGENOM; HOG000060144; -.
HOVERGEN; HBG053541; -.
InParanoid; Q62865; -.
KO; K19021; -.
OMA; PNEEETC; -.
OrthoDB; EOG091G0BTI; -.
PhylomeDB; Q62865; -.
TreeFam; TF329631; -.
Reactome; R-RNO-418457; cGMP effects.
Reactome; R-RNO-418555; G alpha (s) signalling events.
SABIO-RK; Q62865; -.
PRO; PR:Q62865; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000025042; -.
Genevisible; Q62865; RN.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:RGD.
GO; GO:0030552; F:cAMP binding; IDA:RGD.
GO; GO:0004119; F:cGMP-inhibited cyclic-nucleotide phosphodiesterase activity; IDA:RGD.
GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; TAS:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IDA:RGD.
GO; GO:0019933; P:cAMP-mediated signaling; ISO:RGD.
GO; GO:0071321; P:cellular response to cGMP; ISO:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
GO; GO:0019934; P:cGMP-mediated signaling; ISO:RGD.
GO; GO:0016101; P:diterpenoid metabolic process; IEP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0043116; P:negative regulation of vascular permeability; ISO:RGD.
GO; GO:0001556; P:oocyte maturation; IEP:RGD.
GO; GO:0060282; P:positive regulation of oocyte development; ISO:RGD.
GO; GO:0043117; P:positive regulation of vascular permeability; ISO:RGD.
GO; GO:0040020; P:regulation of meiotic nuclear division; ISO:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0042493; P:response to drug; ISO:RGD.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF00233; PDEase_I; 1.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
cAMP; cGMP; Complete proteome; Hydrolase; Isopeptide bond; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 1141 cGMP-inhibited 3',5'-cyclic
phosphodiesterase A.
/FTId=PRO_0000198801.
TRANSMEM 62 82 Helical. {ECO:0000255}.
TRANSMEM 127 147 Helical. {ECO:0000255}.
TRANSMEM 157 177 Helical. {ECO:0000255}.
TRANSMEM 182 202 Helical. {ECO:0000255}.
TRANSMEM 207 227 Helical. {ECO:0000255}.
TRANSMEM 229 249 Helical. {ECO:0000255}.
REGION 728 1086 Catalytic. {ECO:0000250}.
ACT_SITE 752 752 Proton donor. {ECO:0000250}.
METAL 756 756 Divalent metal cation 1. {ECO:0000250}.
METAL 836 836 Divalent metal cation 1. {ECO:0000250}.
METAL 837 837 Divalent metal cation 1. {ECO:0000250}.
METAL 837 837 Divalent metal cation 2. {ECO:0000250}.
METAL 950 950 Divalent metal cation 1. {ECO:0000250}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:Q14432}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000250|UniProtKB:Q14432}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000250|UniProtKB:Q14432}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0X4}.
MOD_RES 533 533 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0X4}.
MOD_RES 1033 1033 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0X4}.
MOD_RES 1036 1036 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z0X4}.
CROSSLNK 1120 1120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q14432}.
SEQUENCE 1141 AA; 124301 MW; A333DFB44F6F33F3 CRC64;
MAVRGEAAQD WAKPGLRGPS PAPVARGDHR CRGGSPSSPR GSGCCWRALA LQPLRRSPQL
SSALCAGSLS VLLALLVRLV GGEVGGELES SQEAAAEEEE EEGARGGVFP GPRGGAPGGG
AQLSPWLQPA ALLFSLLCAF FWMGLCLLRA GVRLPLAVAL LAACCAGEAL VQLSLGVGDG
RLLSLPAAGV LLSCLGGATW LVLRLRLGVL MVALTSALRT VALVSLERFK VAWRPYLAYL
AAVLGLLLAR YAEQLLPQCS GPAPPRERFG SQSSARTKEE IPGWKRRRRS SSVVAGEMSG
CGGKSHRRTS LPCIPREQLM GHSEWDHKRG SRGSQSGTSV TVDIAVMGEA HGLITDLLAD
PSLPPNVCTS LRAVSNLLST QLTFQAIHKP RVNPTVTFSE NYTCSDSEEG LEKDKLAIPK
RLRRSLPPGL LRRVSSTWTT TTSATGLPTL EPAPVRRDRS ASIKPHEAPS PSAVNPDSWN
APVLMTLTKS RSFTSSYAVS AANHVKAKKQ NRPGGLDKIS PVPSPSSSPP QGSPTSSPVS
GIASVQFPES PEVTTKRGPG SHRALTYTQS APDLSPQIPP SPVICSSCGR PYSQGNPADG
PSERSGPAMQ KPNRTDDTSQ VTSDYETNNN SDSSDILQND EEAECQREPL RKASACGTYT
PQTMIFLDKP ILAPEPLVMD NLDSIMDQLN TWNFPIFDLV ENIGRKCGRI LSQVSYRLFE
DMGLFEAFKI PVREFMNYFH ALEIGYRDIP YHNRIHATDV LHAVWYLTTQ PIPGLPSVIG
DHGSASDSDS DSGFTHGHMG YVFSKAYHVP DDKYGCLSGN IPALELMALY VAAAMHDYDH
PGRTNAFLVA TSAPQAVLYN DRSVLENHHA AAAWNLFMSR PEYNFLVNLD HVEFKHFRFL
VIEAILATDL KKHFDFVAKF NAKVNDDVGI DWTNENDRLL VCQMCIKLAD INGPAKCKDL
HLRWTEGIAS EFYEQGDEEA SLGLPISPFM DRSAPQLANL QESFISHIVG PLCHSYDSAG
LMPGKWVDDS DDSGDTDDPE EEEEEAETPH EEETCENSEA PRKKSFKRRR IYCQITQHLL
QNHMMWKKVI EEEQCLSGTE NQAPDQAPLQ HSSEQIQAIK EEEEEKGKPR AEETLAPQPD
L


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