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High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (EC 3.1.4.35)

 PDE9A_MOUSE             Reviewed;         534 AA.
O70628;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
25-OCT-2017, entry version 138.
RecName: Full=High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A {ECO:0000305};
EC=3.1.4.35 {ECO:0000269|PubMed:9624145};
Name=Pde9a; Synonyms=Pde8b;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, AND TISSUE SPECIFICITY.
PubMed=9624145; DOI=10.1074/jbc.273.25.15553;
Soderling S.H., Bayuga S.J., Beavo J.A.;
"Identification and characterization of a novel family of cyclic
nucleotide phosphodiesterases.";
J. Biol. Chem. 273:15553-15558(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9856478; DOI=10.1007/s004390050838;
Guipponi M., Scott H.S., Kudoh J., Kawasaki K., Shibuya K.,
Shintani A., Asakawa S., Chen H., Lalioti M.D., Rossier C.,
Minoshima S., Shimizu N., Antonarakis S.E.;
"Identification and characterization of a novel cyclic nucleotide
phosphodiesterase gene (PDE9A) that maps to 21q22.3: alternative
splicing of mRNA transcripts, genomic structure and sequence.";
Hum. Genet. 103:386-392(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[4]
TISSUE SPECIFICITY.
PubMed=14501210; DOI=10.1023/A:1025704031210;
van Staveren W.C., Glick J., Markerink-van Ittersum M., Shimizu M.,
Beavo J.A., Steinbusch H.W., de Vente J.;
"Cloning and localization of the cGMP-specific phosphodiesterase type
9 in the rat brain.";
J. Neurocytol. 31:729-741(2002).
[5]
FUNCTION, AND ENZYME REGULATION.
PubMed=22328573; DOI=10.1124/jpet.111.191353;
Kleiman R.J., Chapin D.S., Christoffersen C., Freeman J.,
Fonseca K.R., Geoghegan K.F., Grimwood S., Guanowsky V., Hajos M.,
Harms J.F., Helal C.J., Hoffmann W.E., Kocan G.P., Majchrzak M.J.,
McGinnis D., McLean S., Menniti F.S., Nelson F., Roof R.,
Schmidt A.W., Seymour P.A., Stephenson D.T., Tingley F.D.,
Vanase-Frawley M., Verhoest P.R., Schmidt C.J.;
"Phosphodiesterase 9A regulates central cGMP and modulates responses
to cholinergic and monoaminergic perturbation in vivo.";
J. Pharmacol. Exp. Ther. 341:396-409(2012).
[6]
FUNCTION.
PubMed=24746365; DOI=10.1016/j.neurobiolaging.2014.03.023;
Kroker K.S., Mathis C., Marti A., Cassel J.C., Rosenbrock H.,
Dorner-Ciossek C.;
"PDE9A inhibition rescues amyloid beta-induced deficits in synaptic
plasticity and cognition.";
Neurobiol. Aging 35:2072-2078(2014).
[7]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=25799991; DOI=10.1038/nature14332;
Lee D.I., Zhu G., Sasaki T., Cho G.S., Hamdani N., Holewinski R.,
Jo S.H., Danner T., Zhang M., Rainer P.P., Bedja D., Kirk J.A.,
Ranek M.J., Dostmann W.R., Kwon C., Margulies K.B., Van Eyk J.E.,
Paulus W.J., Takimoto E., Kass D.A.;
"Phosphodiesterase 9A controls nitric-oxide-independent cGMP and
hypertrophic heart disease.";
Nature 519:472-476(2015).
-!- FUNCTION: Specifically hydrolyzes the second messenger cGMP, which
is a key regulator of many important physiological processes
(PubMed:9624145). Highly specific: compared to other members of
the cyclic nucleotide phosphodiesterase family, has the highest
affinity and selectivity for cGMP. Specifically regulates
natriuretic-peptide-dependent cGMP signaling in heart, acting as a
regulator of cardiac hypertrophy in myocytes and muscle. Does not
regulate nitric oxide-dependent cGMP in heart (PubMed:25799991).
Additional experiments are required to confirm whether its ability
to hydrolyze natriuretic-peptide-dependent cGMP is specific to
heart or is a general feature of the protein (Probable). In brain,
involved in cognitive function, such as learning and long-term
memory (PubMed:22328573, PubMed:24746365).
{ECO:0000269|PubMed:22328573, ECO:0000269|PubMed:24746365,
ECO:0000269|PubMed:25799991, ECO:0000269|PubMed:9624145,
ECO:0000305}.
-!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
guanosine 5'-phosphate. {ECO:0000269|PubMed:9624145}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:O76083};
Note=Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal
cations per subunit: site 1 preferentially binds zinc, while site
2 has a preference for magnesium. Tightly binds zinc.
{ECO:0000250|UniProtKB:O76083};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:O76083};
Note=Binds 1 Mg(2+) ions per subunit. Binds 2 divalent metal
cations per subunit: site 1 preferentially binds zinc, while site
2 has a preference for magnesium. Binds magnesium less tightly
than zinc. {ECO:0000250|UniProtKB:O76083};
-!- ENZYME REGULATION: Inhibited by SCH 51866 and moderately, by
zaprinast. Specifically inhibited by PF-04447943 (6-[(3S,4S)-4-
methyl-1-(pyrimidin-2-ylmethyl)pyrrolidin-3-yl]-1-(tetrahydro-2H-
pyran-4-yl)-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one)
(PubMed:22328573). {ECO:0000269|PubMed:22328573,
ECO:0000269|PubMed:9624145}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.07 mM for cGMP {ECO:0000269|PubMed:9624145};
-!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
3',5'-cyclic GMP: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O76083}.
-!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:O76083}. Golgi apparatus
{ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:O76083}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced.;
Name=1;
IsoId=O70628-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Highly expressed in kidney. Lower levels in
liver, lung and brain (PubMed:9624145). Widely expressed in brain,
with highest expression in cerebellar Purkinje cells
(PubMed:14501210). Present in heart (at protein level)
(PubMed:25799991). {ECO:0000269|PubMed:14501210,
ECO:0000269|PubMed:25799991, ECO:0000269|PubMed:9624145}.
-!- DISRUPTION PHENOTYPE: Mice hearts develop less dilation and
dysfunction when exposed to sustained pressure overload.
{ECO:0000269|PubMed:25799991}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE9 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF031147; AAC24344.1; -; mRNA.
EMBL; AF068247; AAC23996.1; -; mRNA.
EMBL; BC061163; AAH61163.1; -; mRNA.
CCDS; CCDS28605.1; -. [O70628-1]
RefSeq; NP_001157220.1; NM_001163748.1. [O70628-1]
RefSeq; NP_032830.3; NM_008804.4. [O70628-1]
UniGene; Mm.10812; -.
ProteinModelPortal; O70628; -.
SMR; O70628; -.
STRING; 10090.ENSMUSP00000038005; -.
iPTMnet; O70628; -.
PhosphoSitePlus; O70628; -.
MaxQB; O70628; -.
PaxDb; O70628; -.
PRIDE; O70628; -.
Ensembl; ENSMUST00000047168; ENSMUSP00000038005; ENSMUSG00000041119. [O70628-1]
Ensembl; ENSMUST00000127929; ENSMUSP00000117611; ENSMUSG00000041119. [O70628-1]
GeneID; 18585; -.
KEGG; mmu:18585; -.
UCSC; uc008buz.2; mouse. [O70628-1]
CTD; 5152; -.
MGI; MGI:1277179; Pde9a.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000119066; -.
HOGENOM; HOG000008058; -.
HOVERGEN; HBG053545; -.
InParanoid; O70628; -.
KO; K13761; -.
OMA; TQMMYSM; -.
OrthoDB; EOG091G082I; -.
PhylomeDB; O70628; -.
TreeFam; TF314638; -.
BRENDA; 3.1.4.35; 3474.
Reactome; R-MMU-418457; cGMP effects.
UniPathway; UPA00763; UER00748.
PRO; PR:O70628; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000041119; -.
CleanEx; MM_PDE9A; -.
ExpressionAtlas; O70628; baseline and differential.
Genevisible; O70628; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046069; P:cGMP catabolic process; IDA:UniProtKB.
GO; GO:0046068; P:cGMP metabolic process; ISO:MGI.
GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:UniProtKB.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Cell projection; cGMP;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
Hydrolase; Magnesium; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Zinc.
CHAIN 1 534 High affinity cGMP-specific 3',5'-cyclic
phosphodiesterase 9A.
/FTId=PRO_0000198842.
NP_BIND 251 255 cGMP. {ECO:0000250|UniProtKB:O76083}.
NP_BIND 451 452 cGMP. {ECO:0000250|UniProtKB:O76083}.
REGION 227 489 Catalytic. {ECO:0000250}.
ACT_SITE 251 251 Proton donor.
{ECO:0000250|UniProtKB:O76083}.
METAL 255 255 Zinc; via tele nitrogen.
{ECO:0000250|UniProtKB:O76083}.
METAL 291 291 Zinc; via tele nitrogen.
{ECO:0000250|UniProtKB:O76083}.
METAL 292 292 Magnesium.
{ECO:0000250|UniProtKB:O76083}.
METAL 292 292 Zinc. {ECO:0000250|UniProtKB:O76083}.
METAL 401 401 Zinc. {ECO:0000250|UniProtKB:O76083}.
BINDING 292 292 cGMP. {ECO:0000250|UniProtKB:O76083}.
BINDING 401 401 cGMP. {ECO:0000250|UniProtKB:O76083}.
BINDING 423 423 cGMP. {ECO:0000250|UniProtKB:O76083}.
BINDING 423 423 Inhibitor specific to Pde9a.
{ECO:0000250|UniProtKB:O76083}.
BINDING 452 452 Inhibitor.
{ECO:0000250|UniProtKB:O76083}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:Q8QZV1}.
SEQUENCE 534 AA; 61636 MW; 28126C7BB7375241 CRC64;
MGAGSSSYRP KAIYLDIDGR IQKVVFSKYC NSSDIMDLFC IATGLPRNTT ISLLTTDDAM
VSIDPTMPAN SERTPYKVRP VAVKQVSERE ELIQGVLAQV AEQFSRAFKI NELKAEVANH
LAVLEKRVEL EGLKVVEIEK CKSDIKKMRE ELAARNSRTN CPCKYSFLDN KKLTPRRDVP
TYPKYLLSPE TIEALRKPTF DVWLWEPNEM LSCLEHMYHD LGLVRDFSIN PITLRRWLLC
VHDNYRNNPF HNFRHCFCVT QMMYSMVWLC GLQEKFSQMD ILVLMTAAIC HDLDHPGYNN
TYQINARTEL AVRYNDISPL ENHHCAIAFQ ILARPECNIF ASVPPEGFRQ IRQGMITLIL
ATDMARHAEI MDSFKEKMEN FDYSNEEHLT LLKMILIKCC DISNEVRPME VAEPWVDCLL
EEYFMQSDRE KSEGLPVAPF MDRDKVTKAT AQIGFIKFVL IPMFETVTKL FPVVEETMLR
PLWESREHYE ELKQLDDAMK ELQKKTESLT SGAPENTTEK NRDAKDSEGH SPPN


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