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cGMP-specific 3',5'-cyclic phosphodiesterase (EC 3.1.4.35) (cGMP-binding cGMP-specific phosphodiesterase) (CGB-PDE)

 PDE5A_RAT               Reviewed;         833 AA.
O54735;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
23-MAY-2018, entry version 128.
RecName: Full=cGMP-specific 3',5'-cyclic phosphodiesterase;
EC=3.1.4.35 {ECO:0000250|UniProtKB:O76074};
AltName: Full=cGMP-binding cGMP-specific phosphodiesterase;
Short=CGB-PDE;
Name=Pde5a; Synonyms=Pde5;
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].
STRAIN=Sprague-Dawley; TISSUE=Lung;
PubMed=9370351; DOI=10.1111/j.1432-1033.1997.t01-1-00434.x;
Kotera J., Yanaka N., Fujishige K., Imai Y., Akatsuka H., Ishizuka T.,
Kawashima K., Omori K.;
"Expression of rat cGMP-binding cGMP-specific phosphodiesterase mRNA
in Purkinje cell layers during postnatal neuronal development.";
Eur. J. Biochem. 249:434-442(1997).
-!- FUNCTION: Plays a role in signal transduction by regulating the
intracellular concentration of cyclic nucleotides. This
phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-
GMP. Specifically regulates nitric-oxide-generated cGMP.
{ECO:0000250|UniProtKB:O76074}.
-!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
guanosine 5'-phosphate. {ECO:0000250|UniProtKB:O76074}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:O76074};
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:O76074};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:O76074};
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:O76074};
-!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
3',5'-cyclic GMP: step 1/1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=PDE5A2;
IsoId=O54735-1; Sequence=Displayed;
Name=PDE5A1;
IsoId=O54735-2; Sequence=Not described;
-!- DOMAIN: Composed of a C-terminal catalytic domain containing two
putative divalent metal sites and an N-terminal regulatory domain
which contains two homologous allosteric cGMP-binding regions, A
and B.
-!- PTM: Phosphorylation is regulated by binding of cGMP to the two
allosteric sites. Phosphorylation by PRKG1 leads to its
activation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. {ECO:0000305}.
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EMBL; D89093; BAA23672.1; -; mRNA.
RefSeq; NP_598268.1; NM_133584.1. [O54735-1]
UniGene; Rn.10861; -.
UniGene; Rn.133138; -.
ProteinModelPortal; O54735; -.
SMR; O54735; -.
STRING; 10116.ENSRNOP00000019637; -.
BindingDB; O54735; -.
ChEMBL; CHEMBL4567; -.
iPTMnet; O54735; -.
PhosphoSitePlus; O54735; -.
PaxDb; O54735; -.
PRIDE; O54735; -.
GeneID; 171115; -.
KEGG; rno:171115; -.
UCSC; RGD:620995; rat. [O54735-1]
CTD; 8654; -.
RGD; 620995; Pde5a.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
HOGENOM; HOG000007068; -.
HOVERGEN; HBG101207; -.
InParanoid; O54735; -.
KO; K13762; -.
PhylomeDB; O54735; -.
BRENDA; 3.1.4.35; 5301.
UniPathway; UPA00763; UER00748.
PRO; PR:O54735; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IDA:RGD.
GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046069; P:cGMP catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0007399; P:nervous system development; IEP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0002678; P:positive regulation of chronic inflammatory response; IMP:RGD.
GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
GO; GO:0002026; P:regulation of the force of heart contraction; IMP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0033574; P:response to testosterone; IEP:RGD.
GO; GO:0007614; P:short-term memory; IMP:RGD.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0042311; P:vasodilation; IEP:RGD.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
Gene3D; 3.30.450.40; -; 3.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF-like_dom_sf.
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; 2.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00065; GAF; 2.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I_1; 1.
PROSITE; PS51845; PDEASE_I_2; 1.
2: Evidence at transcript level;
Allosteric enzyme; Alternative splicing; cGMP; cGMP-binding;
Complete proteome; Hydrolase; Magnesium; Metal-binding;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Zinc.
CHAIN 1 833 cGMP-specific 3',5'-cyclic
phosphodiesterase.
/FTId=PRO_0000198825.
DOMAIN 122 272 GAF 1.
DOMAIN 304 461 GAF 2.
DOMAIN 494 818 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
ACT_SITE 571 571 Proton donor.
{ECO:0000250|UniProtKB:O76083}.
METAL 575 575 Zinc; via tele nitrogen.
{ECO:0000250|UniProtKB:O76074}.
METAL 611 611 Zinc; via tele nitrogen.
{ECO:0000250|UniProtKB:O76074}.
METAL 612 612 Magnesium.
{ECO:0000250|UniProtKB:O76074}.
METAL 612 612 Zinc. {ECO:0000250|UniProtKB:O76074}.
METAL 722 722 Zinc. {ECO:0000250|UniProtKB:O76074}.
BINDING 775 775 cGMP. {ECO:0000250|UniProtKB:O76074}.
MOD_RES 60 60 Phosphoserine. {ECO:0000255}.
SEQUENCE 833 AA; 94556 MW; 712DC159C80CB09D CRC64;
MLPFGDKTRD MVNAWFSERV HNIPVCKEGI RAHTESCSCS LPQSPHADNT TPGAPARKIS
ASEFDRPLRP IVVKDSEGTV SFLSDSGKKE QMPLTSPRFD SDEGDQCSRL LELVKDISSH
LDVTALCHKI FLHIHGLISA DRYSLFLVCE DSSKDKFLVS RLFDVAEGST LEEASNNCIR
LEWNKGIVGH VAAFGEPLNI KDAYEDPRFN AEVDQITGYK TQSILCMPIK NHREEVVGVA
QAINKKSGNG GTFTEKDEKD FAAYLAFCGI VLHNAQLYET SLLENKRNQV LLDLASLIFE
EQQSLEVILK KIAATIISFM QVQKCTIFIV DEDCPDSFSR VFQMEWEEVG KSSEPLTREH
DANKINYMYA QYVKNTMEPL NIPDVTKDNR FPWTNENMGH INTHCIRSLL CTPIKNGKKN
KVIGVCQLVN KMEEKTGKIK AFNQNDEQFL EAFVIFCGLG IQNTQMYEAV ERAMAKQMVT
LEVLSYHASA AEEETRELQA LAAAVVPSAQ TLKITDFSFS DFELSDLETA LCTIRMFTDL
NLVQNFQMKH EVLCRWILSV KKNYRKNVAY HNWRHAFNTA QCMFAALKAG KIQNKLTDLE
TLALLIAALS HDLDHRGVNN SYIQRSEHPL AQLYCHSTME HHHFDQCLMV LNSPGNQILS
GLSIEEYKTT LKIIKQAILA TDLALYIKRR GEFFELIRKN EFSFEDPLQK ELFLAMLMTA
CDLSAITKPW PIQQRIAELV AAEFFDQGDR ERKELNMEPA DLMNREKKNK IPSMQVGFID
AICLQLYEAL THVSEDCLPL LDGCRKNRQK WQALADQQEK TLLNGESGQA KRD


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