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

 PDE9A_RAT               Reviewed;         534 AA.
Q8QZV1; F1LRG6;
27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
22-NOV-2017, entry version 110.
RecName: Full=High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A {ECO:0000305};
EC=3.1.4.35 {ECO:0000250|UniProtKB:O76083};
Name=Pde9a {ECO:0000312|RGD:621035};
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], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=11698617;
Andreeva S.G., Dikkes P., Epstein P.M., Rosenberg P.A.;
"Expression of cGMP-specific phosphodiesterase 9A mRNA in the rat
brain.";
J. Neurosci. 21:9068-9076(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[6]
FUNCTION, AND ENZYME REGULATION.
PubMed=18674549; DOI=10.1016/j.neuropharm.2008.07.005;
van der Staay F.J., Rutten K., Baerfacker L., Devry J., Erb C.,
Heckroth H., Karthaus D., Tersteegen A., van Kampen M., Blokland A.,
Prickaerts J., Reymann K.G., Schroeder U.H., Hendrix M.;
"The novel selective PDE9 inhibitor BAY 73-6691 improves learning and
memory in rodents.";
Neuropharmacology 55:908-918(2008).
[7]
FUNCTION, AND ENZYME REGULATION.
PubMed=22070409; DOI=10.3109/01677063.2011.630494;
Vardigan J.D., Converso A., Hutson P.H., Uslaner J.M.;
"The selective phosphodiesterase 9 (PDE9) inhibitor PF-04447943
attenuates a scopolamine-induced deficit in a novel rodent attention
task.";
J. Neurogenet. 25:120-126(2011).
[8]
FUNCTION.
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).
-!- FUNCTION: Specifically hydrolyzes the second messenger cGMP, which
is a key regulator of many important physiological processes.
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. 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 (By similarity). In brain, involved in
cognitive function, such as learning and long-term memory
(PubMed:18674549, PubMed:22070409, PubMed:22328573).
{ECO:0000250|UniProtKB:O76083, ECO:0000269|PubMed:18674549,
ECO:0000269|PubMed:22070409, ECO:0000269|PubMed:22328573}.
-!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
guanosine 5'-phosphate. {ECO:0000250|UniProtKB:O76083}.
-!- 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: Specifically inhibited by BAY-73-6691 (1-(2-
chlorophenyl)-6-((2R)-3,3,3- trifluoro-2-methylpropyl)-1,5-
dihydro-4H-pyrazolo(3,4-d)pyrimidine-4-one) (PubMed:18674549).
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:22070409). {ECO:0000269|PubMed:18674549,
ECO:0000269|PubMed:22070409}.
-!- 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}.
-!- TISSUE SPECIFICITY: Widely expressed in brain: highly expressed in
the basal forebrain, cerebellum and olfactory bulb
(PubMed:11698617, PubMed:14501210). Expressed at highest level in
cerebellar Purkinje cells (PubMed:14501210).
{ECO:0000269|PubMed:11698617, ECO:0000269|PubMed:14501210}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE9 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF372654; AAL99404.1; -; mRNA.
EMBL; AY145898; AAN64274.1; -; mRNA.
EMBL; AABR06100132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06100133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06100134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06100135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC161837; AAI61837.1; -; mRNA.
RefSeq; NP_612552.1; NM_138543.1.
RefSeq; XP_008771015.1; XM_008772793.2.
RefSeq; XP_008771016.1; XM_008772794.2.
RefSeq; XP_008771017.1; XM_008772795.2.
UniGene; Rn.20981; -.
ProteinModelPortal; Q8QZV1; -.
SMR; Q8QZV1; -.
STRING; 10116.ENSRNOP00000001559; -.
BindingDB; Q8QZV1; -.
ChEMBL; CHEMBL3638358; -.
iPTMnet; Q8QZV1; -.
PhosphoSitePlus; Q8QZV1; -.
PaxDb; Q8QZV1; -.
PRIDE; Q8QZV1; -.
Ensembl; ENSRNOT00000001559; ENSRNOP00000001559; ENSRNOG00000001174.
GeneID; 191569; -.
KEGG; rno:191569; -.
UCSC; RGD:621035; rat.
CTD; 5152; -.
RGD; 621035; Pde9a.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000119066; -.
HOGENOM; HOG000008058; -.
HOVERGEN; HBG053545; -.
InParanoid; F1LRG6; -.
KO; K13761; -.
OMA; TQMMYSM; -.
OrthoDB; EOG091G082I; -.
PhylomeDB; Q8QZV1; -.
TreeFam; TF314638; -.
BRENDA; 3.1.4.35; 5301.
Reactome; R-RNO-418457; cGMP effects.
UniPathway; UPA00763; UER00748.
PRO; PR:Q8QZV1; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000001174; -.
Genevisible; Q8QZV1; RN.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0043204; C:perikaryon; IDA:RGD.
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:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046069; P:cGMP catabolic process; ISS:UniProtKB.
GO; GO:0046068; P:cGMP metabolic process; ISS:UniProtKB.
GO; GO:0019934; P:cGMP-mediated signaling; IEP:RGD.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS: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;
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_0000433157.
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:0000244|PubMed:16641100}.
SEQUENCE 534 AA; 61756 MW; 4AB9382BA2D2CB54 CRC64;
MGAGSSSYRP KAIYLDIDGR IQKVVFSKYC NSSDIMDLFC IATGLPRNTT ISLLTTDDAM
VSIDPTMPAN SERTPYKVRP VAVKQVSERE ELVQGVLAQV AEQFSRAFKI NELKAEVANH
LAMLEKRVEL EGLKVVEIEK CKSDIKKMRE ELAARNNRTN CPCKYSFLDN KKLTPRRDVP
TYPKYLLSPE TIEALRKPTF DVWLWEPNEM LSCLEHMYHD LGLVRDFSIN PITLRRWLLC
VHDNYRSNPF HNFRHCFCVT QMMYSMVWLC GLQEKFSQMD ILVLMTAAIC HDLDHPGYNN
TYQINARTEL AVRYNDISPL ENHHCAIAFQ ILARPECNIF ASVPPEGFRQ IRQGMITLIL
ATDMARHAEI MDSFKEKMEN FDYSNEEHLT LLKMILIKCC DISNEVRPME VAEPWVDCLL
EEYFMQSDRE KSEGLPVAPF MDRDKVTKAT AQIGFIKFVL IPMFETVTKL FPIVEETMLR
PLWESREHYE ELKQLDDAMK ELQKKTENLT SGATENAPEK TRDAKDNEDR SPPN


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