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

 PDE2A_MOUSE             Reviewed;         916 AA.
Q922S4; Q8K2U1;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
30-AUG-2017, entry version 132.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 805-814, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[4]
X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 183-549 IN COMPLEX WITH
CGMP, DOMAIN GAF 1, AND SUBUNIT.
PubMed=12271124; DOI=10.1073/pnas.192374899;
Martinez S.E., Wu A.Y., Glavas N.A., Tang X.-B., Turley S.,
Hol W.G.J., Beavo J.A.;
"The two GAF domains in phosphodiesterase 2A have distinct roles in
dimerization and in cGMP binding.";
Proc. Natl. Acad. Sci. U.S.A. 99:13260-13265(2002).
-!- 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};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12271124}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}.
-!- DOMAIN: GAF 1 functions as a dimerization domain, whereas GAF 2
binds cGMP, which causes activation of the catalytic activity of
the enzyme. {ECO:0000269|PubMed:12271124}.
-!- MISCELLANEOUS: cGMP binds at an allosteric activator site.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE2 subfamily. {ECO:0000305}.
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EMBL; AC129079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC129609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006845; AAH06845.1; -; mRNA.
EMBL; BC029810; AAH29810.1; -; mRNA.
EMBL; BC057029; -; NOT_ANNOTATED_CDS; mRNA.
UniGene; Mm.247564; -.
PDB; 1MC0; X-ray; 2.86 A; A=190-549.
PDBsum; 1MC0; -.
ProteinModelPortal; Q922S4; -.
SMR; Q922S4; -.
IntAct; Q922S4; 2.
STRING; 10090.ENSMUSP00000131553; -.
iPTMnet; Q922S4; -.
PhosphoSitePlus; Q922S4; -.
SwissPalm; Q922S4; -.
MaxQB; Q922S4; -.
PaxDb; Q922S4; -.
PeptideAtlas; Q922S4; -.
PRIDE; Q922S4; -.
UCSC; uc009ioq.3; mouse.
MGI; MGI:2446107; Pde2a.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
HOGENOM; HOG000007068; -.
HOVERGEN; HBG053540; -.
InParanoid; Q922S4; -.
EvolutionaryTrace; Q922S4; -.
PRO; PR:Q922S4; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_PDE2A; -.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0030552; F:cAMP binding; IMP:UniProtKB.
GO; GO:0030553; F:cGMP binding; IDA: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:0036004; F:GAF domain binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030911; F:TPR domain binding; ISO:MGI.
GO; GO:0035904; P:aorta development; IMP:MGI.
GO; GO:0006198; P:cAMP catabolic process; IMP:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB.
GO; GO:0003279; P:cardiac septum development; IMP:MGI.
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:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:UniProtKB.
GO; GO:0046069; P:cGMP catabolic process; IMP:UniProtKB.
GO; GO:0019934; P:cGMP-mediated signaling; ISS:UniProtKB.
GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0003170; P:heart valve development; IMP:MGI.
GO; GO:0008152; P:metabolic process; IDA:UniProtKB.
GO; GO:0030818; P:negative regulation of cAMP biosynthetic process; IMP: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:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:UniProtKB.
GO; GO:0043117; P:positive regulation of vascular permeability; ISS:UniProtKB.
GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
GO; GO:0030823; P:regulation of cGMP metabolic process; IGI:MGI.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
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; 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; cAMP; cGMP; cGMP-binding;
Complete proteome; Direct protein sequencing; Hydrolase; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Repeat.
CHAIN 1 916 cGMP-dependent 3',5'-cyclic
phosphodiesterase.
/FTId=PRO_0000198797.
DOMAIN 216 353 GAF 1.
DOMAIN 385 524 GAF 2.
REGION 609 867 Catalytic. {ECO:0000250}.
REGION 632 636 Substrate binding. {ECO:0000250}.
ACT_SITE 632 632 Proton donor. {ECO:0000250}.
METAL 636 636 Divalent metal cation 1. {ECO:0000250}.
METAL 672 672 Divalent metal cation 1. {ECO:0000250}.
METAL 673 673 Divalent metal cation 1. {ECO:0000250}.
METAL 673 673 Divalent metal cation 2. {ECO:0000250}.
METAL 784 784 Divalent metal cation 1. {ECO:0000250}.
BINDING 407 407 cGMP. {ECO:0000269|PubMed:12271124}.
BINDING 422 422 cGMP. {ECO:0000269|PubMed:12271124}.
BINDING 475 475 cGMP. {ECO:0000269|PubMed:12271124}.
BINDING 673 673 Substrate. {ECO:0000250}.
BINDING 784 784 Substrate. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P14099}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:Q01062}.
CONFLICT 4 5 VS -> QP (in Ref. 2; BC057029).
{ECO:0000305}.
HELIX 199 210 {ECO:0000244|PDB:1MC0}.
HELIX 217 231 {ECO:0000244|PDB:1MC0}.
STRAND 234 242 {ECO:0000244|PDB:1MC0}.
STRAND 244 246 {ECO:0000244|PDB:1MC0}.
STRAND 248 254 {ECO:0000244|PDB:1MC0}.
STRAND 257 271 {ECO:0000244|PDB:1MC0}.
HELIX 272 278 {ECO:0000244|PDB:1MC0}.
HELIX 284 286 {ECO:0000244|PDB:1MC0}.
HELIX 289 299 {ECO:0000244|PDB:1MC0}.
STRAND 306 312 {ECO:0000244|PDB:1MC0}.
TURN 314 316 {ECO:0000244|PDB:1MC0}.
STRAND 318 330 {ECO:0000244|PDB:1MC0}.
HELIX 337 381 {ECO:0000244|PDB:1MC0}.
TURN 382 384 {ECO:0000244|PDB:1MC0}.
TURN 386 388 {ECO:0000244|PDB:1MC0}.
HELIX 389 401 {ECO:0000244|PDB:1MC0}.
STRAND 403 411 {ECO:0000244|PDB:1MC0}.
STRAND 413 421 {ECO:0000244|PDB:1MC0}.
HELIX 440 448 {ECO:0000244|PDB:1MC0}.
STRAND 452 455 {ECO:0000244|PDB:1MC0}.
HELIX 468 471 {ECO:0000244|PDB:1MC0}.
STRAND 478 484 {ECO:0000244|PDB:1MC0}.
STRAND 490 499 {ECO:0000244|PDB:1MC0}.
STRAND 502 504 {ECO:0000244|PDB:1MC0}.
HELIX 507 535 {ECO:0000244|PDB:1MC0}.
SEQUENCE 916 AA; 103249 MW; A386C6773CC4F5B4 CRC64;
MRRVSAASQD PLAQKPEPPG SRDDRLEDAL LSLGAVIDIA GLRQAARDAL SAVLPKVETV
YTYLLDGESR LVCEDPPHEL PQEGKIREAV ISQKRLSCNG LGPSDLLGKP LARLVAPLAP
DMQVLVIPLL DKETGSVAAV ILVHCGQLSD SEEQSLQVVE KHALVALRRV QALQQRRPEA
VQNTSVDASE DQKDEKGYTD HDRKILQLCG ELFDLDATSL QLKVLQYLQQ ETQATHCCLL
LVSEDNLQLS CKVIGDKVLG EEVSFPLTMG RLGQVVEDKQ CIQLKDLTSD DVQQLQNMLG
CELQAMLCVP VISRATDQVV ALACAFNKLG GDFFTDEDEH VIQHCFHYTG TVLTSTLAFQ
KEQKLKCECQ ALLQVAKNLF THLDDVSVLL QEIITEARNL SNAEICSVFL LDQNELVAKV
FDGGVVDDES YEIRIPADQG IAGHVATTGQ ILNIPDAYAH PLFYRGVDDS TGFRTRNILC
FPIKNENQEV IGVAELVNKI NGPWFSKFDE DLATAFSIYC GISIAHSLLY KKVNEAQYRS
HLANEMMMYH MKVSDDEYTK LLHDGIQPVA AIDSNFANFT YTPRSLPEDD TSMAILSMLQ
DMNFINNYKI DCPTLARFCL MVKKGYRDPP YHNWMHAFSV SHFCYLLYKN LELSNYLEDI
EIFALFISCM CHDLDHRGTN NSFQVASKSV LAALYSSEGS VMERHHFAQA IAILNTHGCN
IFDHFSRKDY QRMLDLMRDI ILATDLAHHL RIFKDLQKMA EVGYDRNNRQ HHRLLLCLLM
TSCDLSDQTK GWKTTRKIAE LIYKEFFSQG DLEKAMGNRP MEMMDREKAY IPELQISFME
HIAMPIYKLL QDLFPKAAEL YERVASNREH WTKVSHKFTI RGLPSNNSLD FLDEEYEVPD
LDGTRAPVNG CCSLEG


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