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cGMP-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) (Cyclic GMP-stimulated phosphodiesterase) (CGS-PDE) (cGSPDE)

 PDE2A_BOVIN             Reviewed;         921 AA.
P14099; Q28064;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 2.
25-OCT-2017, entry version 124.
RecName: Full=cGMP-dependent 3',5'-cyclic phosphodiesterase;
EC=3.1.4.17;
AltName: Full=Cyclic GMP-stimulated phosphodiesterase;
Short=CGS-PDE;
Short=cGSPDE;
Name=PDE2A;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A1).
PubMed=1654333;
Sonnenburg W.K., Mullaney P.J., Beavo J.A.;
"Molecular cloning of a cyclic GMP-stimulated cyclic nucleotide
phosphodiesterase cDNA. Identification and distribution of isozyme
variants.";
J. Biol. Chem. 266:17655-17661(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A3).
TISSUE=Brain;
Juilfs D.M., Sonnenburg W.K., Seraji S., Beavo J.A.;
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 592-921, AND ACETYLATION AT MET-1.
TISSUE=Heart;
PubMed=2176866; DOI=10.1021/bi00496a018;
le Trong H., Beier N., Sonnenburg W.K., Stroop S.D., Walsh K.A.,
Beavo J.A., Charbonneau H.;
"Amino acid sequence of the cyclic GMP stimulated cyclic nucleotide
phosphodiesterase from bovine heart.";
Biochemistry 29:10280-10288(1990).
[4]
PROTEIN SEQUENCE OF 613-694 AND 808-868.
TISSUE=Heart;
PubMed=3025833; DOI=10.1073/pnas.83.24.9308;
Charbonneau H., Beier N., Walsh K.A., Beavo J.A.;
"Identification of a conserved domain among cyclic nucleotide
phosphodiesterases from diverse species.";
Proc. Natl. Acad. Sci. U.S.A. 83:9308-9312(1986).
-!- 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}.
-!- FUNCTION: Isoform PDE2A2: Regulates mitochondrial cAMP levels and
respiration. 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.
{ECO:0000250|UniProtKB:Q01062}.
-!- 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};
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Isoform PDE2A3: Cell membrane
{ECO:0000250|UniProtKB:Q01062}; Peripheral membrane protein
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform PDE2A1: Cytoplasm
{ECO:0000250|UniProtKB:Q01062}.
-!- SUBCELLULAR LOCATION: Isoform PDE2A2: Mitochondrion
{ECO:0000250|UniProtKB:Q01062}. Mitochondrion inner membrane
{ECO:0000250|UniProtKB:Q01062}. Mitochondrion outer membrane
{ECO:0000250|UniProtKB:Q01062}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=PDE2A1;
IsoId=P14099-1; Sequence=Displayed;
Name=PDE2A2;
IsoId=P14099-3; Sequence=Not described;
Name=PDE2A3;
IsoId=P14099-2; Sequence=VSP_004555;
-!- DOMAIN: GAF 1 functions as a dimerization domain, whereas GAF 2
binds cGMP, which causes activation of the catalytic activity of
the enzyme. {ECO:0000250}.
-!- MISCELLANEOUS: cGMP binds at an allosteric activator site.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE2 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M73512; AAA74559.1; -; mRNA.
EMBL; L49503; AAA87353.1; -; mRNA.
PIR; A40981; A40981.
RefSeq; NP_001137318.1; NM_001143846.1.
RefSeq; NP_001243202.1; NM_001256273.1. [P14099-1]
UniGene; Bt.4716; -.
PDB; 3JAB; EM; 11.00 A; B/N=367-551.
PDB; 3JBQ; EM; 11.00 A; C/G=367-551.
PDBsum; 3JAB; -.
PDBsum; 3JBQ; -.
ProteinModelPortal; P14099; -.
SMR; P14099; -.
STRING; 9913.ENSBTAP00000011077; -.
BindingDB; P14099; -.
ChEMBL; CHEMBL3477; -.
iPTMnet; P14099; -.
PaxDb; P14099; -.
PRIDE; P14099; -.
GeneID; 281971; -.
KEGG; bta:281971; -.
CTD; 5138; -.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
HOGENOM; HOG000007068; -.
HOVERGEN; HBG053540; -.
InParanoid; P14099; -.
KO; K18283; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0030553; F:cGMP binding; ISS:UniProtKB.
GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IDA:UniProtKB.
GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; ISS:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
GO; GO:0071321; P:cellular response to cGMP; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB.
GO; GO:0046069; P:cGMP catabolic process; ISS:UniProtKB.
GO; GO:0019934; P:cGMP-mediated signaling; ISS:UniProtKB.
GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
GO; GO:0046038; P:GMP catabolic process; TAS:AgBase.
GO; GO:0030818; P:negative regulation of cAMP biosynthetic process; ISS:UniProtKB.
GO; GO:0033159; P:negative regulation of protein import into nucleus, translocation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0043116; P:negative regulation of vascular permeability; ISS:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0043117; P:positive regulation of vascular permeability; ISS:UniProtKB.
GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
GO; GO:0030814; P:regulation of cAMP metabolic process; TAS:AgBase.
GO; GO:0007165; P:signal transduction; NAS:AgBase.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
Gene3D; 3.30.450.40; -; 3.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF_dom-like.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF01590; GAF; 1.
Pfam; PF13185; GAF_2; 1.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00065; GAF; 2.
SMART; SM00471; HDc; 1.
SUPFAM; SSF55781; SSF55781; 3.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; cAMP; Cell membrane;
cGMP; cGMP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Membrane; Metal-binding;
Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
Repeat.
CHAIN 1 921 cGMP-dependent 3',5'-cyclic
phosphodiesterase.
/FTId=PRO_0000198795.
DOMAIN 220 357 GAF 1. {ECO:0000255}.
DOMAIN 389 528 GAF 2. {ECO:0000255}.
REGION 613 871 Catalytic.
REGION 636 640 Substrate binding. {ECO:0000250}.
ACT_SITE 636 636 Proton donor. {ECO:0000250}.
METAL 640 640 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
METAL 676 676 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
METAL 677 677 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
METAL 677 677 Divalent metal cation 2.
{ECO:0000250|UniProtKB:O00408}.
METAL 788 788 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
BINDING 411 411 cGMP. {ECO:0000250|UniProtKB:Q922S4}.
BINDING 426 426 cGMP. {ECO:0000250|UniProtKB:Q922S4}.
BINDING 479 479 cGMP. {ECO:0000250|UniProtKB:Q922S4}.
BINDING 677 677 Substrate. {ECO:0000250}.
BINDING 788 788 Substrate. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:2176866}.
VAR_SEQ 1 25 MRRQPAASRDLFAQEPVPPGSGDGA -> MGQACGHSILCR
SQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADS (in
isoform PDE2A3). {ECO:0000303|Ref.2}.
/FTId=VSP_004555.
CONFLICT 204 204 N -> D (in Ref. 2; AAA87353).
{ECO:0000305}.
CONFLICT 633 633 P -> L (in Ref. 4; AA sequence).
{ECO:0000305}.
SEQUENCE 921 AA; 103228 MW; E29F4C9875E83640 CRC64;
MRRQPAASRD LFAQEPVPPG SGDGALQDAL LSLGSVIDVA GLQQAVKEAL SAVLPKVETV
YTYLLDGESR LVCEEPPHEL PQEGKVREAV ISRKRLGCNG LGPSDLPGKP LARLVAPLAP
DTQVLVIPLV DKEAGAVAAV ILVHCGQLSD NEEWSLQAVE KHTLVALKRV QALQQRESSV
APEATQNPPE EAAGDQKGGV AYTNQDRKIL QLCGELYDLD ASSLQLKVLQ YLQQETQASR
CCLLLVSEDN LQLSCKVIGD KVLEEEISFP LTTGRLGQVV EDKKSIQLKD LTSEDMQQLQ
SMLGCEVQAM LCVPVISRAT DQVVALACAF NKLGGDLFTD QDEHVIQHCF HYTSTVLTST
LAFQKEQKLK CECQALLQVA KNLFTHLDDV SVLLQEIITE ARNLSNAEIC SVFLLDQNEL
VAKVFDGGVV EDESYEIRIP ADQGIAGHVA TTGQILNIPD AYAHPLFYRG VDDSTGFRTR
NILCFPIKNE NQEVIGVAEL VNKINGPWFS KFDEDLATAF SIYCGISIAH SLLYKKVNEA
QYRSHLANEM MMYHMKVSDD EYTKLLHDGI QPVAAIDSNF ASFTYTPRSL PEDDTSMAIL
SMLQDMNFIN NYKIDCPTLA RFCLMVKKGY RDPPYHNWMH AFSVSHFCYL LYKNLELTNY
LEDMEIFALF ISCMCHDLDH RGTNNSFQVA SKSVLAALYS SEGSVMERHH FAQAIAILNT
HGCNIFDHFS RKDYQRMLDL MRDIILATDL AHHLRIFKDL QKMAEVGYDR TNKQHHSLLL
CLLMTSCDLS DQTKGWKTTR KIAELIYKEF FSQGDLEKAM GNRPMEMMDR EKAYIPELQI
SFMEHIAMPI YKLLQDLFPK AAELYERVAS NREHWTKVSH KFTIRGLPSN NSLDFLDEEY
EVPDLDGARA PINGCCSLDA E


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