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

 PDE5A_HUMAN             Reviewed;         875 AA.
O76074; A0AV69; A8K2C4; O75026; O75887; Q86UI0; Q86V66; Q9Y6Z6;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
22-NOV-2017, entry version 172.
RecName: Full=cGMP-specific 3',5'-cyclic phosphodiesterase;
EC=3.1.4.35 {ECO:0000269|PubMed:9714779};
AltName: Full=cGMP-binding cGMP-specific phosphodiesterase;
Short=CGB-PDE;
Name=PDE5A; Synonyms=PDE5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE5A1 AND PDE5A2), FUNCTION,
CATALYTIC ACTIVITY, AND VARIANT VAL-93.
PubMed=9714779; DOI=10.1016/S0378-1119(98)00303-5;
Loughney K., Hill T.R., Florio V.A., Uher L., Rosman G.J., Wolda S.L.,
Jones B.A., Howard M.L., McAllister-Lucas L.M., Sonnenburg W.K.,
Francis S.H., Corbin J.D., Beavo J.A., Ferguson K.;
"Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-
binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase.";
Gene 216:139-147(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM PDE5A1), AND VARIANT
VAL-93.
TISSUE=Lung, and Placenta;
PubMed=9716380; DOI=10.1046/j.1432-1327.1998.2550391.x;
Yanaka N., Kotera J., Ohtsuka A., Akatsuka H., Imai Y., Michibata H.,
Fujishige K., Kawai E., Takebayashi S., Okumura K., Omori K.;
"Expression, structure and chromosomal localization of the human cGMP-
binding cGMP-specific phosphodiesterase PDE5A gene.";
Eur. J. Biochem. 255:391-399(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A1), AND VARIANT VAL-93.
TISSUE=Prostate, and Skeletal muscle;
PubMed=9642111; DOI=10.1006/bbrc.1998.8769;
Stacey P., Rulten S., Dapling A., Phillips S.C.;
"Molecular cloning and expression of human cGMP-binding cGMP-specific
phosphodiesterase.";
Biochem. Biophys. Res. Commun. 247:249-254(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A2), AND VARIANT VAL-93.
TISSUE=Lung;
Kotera J., Imai Y., Omori K.;
"Molecular cloning and characterization of human cGMP-specific
phosphodiesterase 5A2 cDNA.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A2).
TISSUE=Colon carcinoma;
Sopory S., Visweswariah S.S.;
"PDE5A splice variants in T84 cells.";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE5A1), AND VARIANT
VAL-93.
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE5A1).
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 157-411.
TISSUE=Trabecular meshwork;
PubMed=10393044;
Zhou L., Thompson W.J., Potter D.E.;
"Multiple cyclic nucleotide phosphodiesterases in human trabecular
meshwork cells.";
Invest. Ophthalmol. Vis. Sci. 40:1745-1752(1999).
[10]
PHOSPHORYLATION BY PRKG1.
PubMed=11723116; DOI=10.1074/jbc.M106562200;
Rybalkin S.D., Rybalkina I.G., Feil R., Hofmann F., Beavo J.A.;
"Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation
in smooth muscle cells.";
J. Biol. Chem. 277:3310-3317(2002).
[11]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 537-860 IN COMPLEX WITH ZINC;
MAGNESIUM AND THE INHIBITORS SILDENAFIL; TADALAFIL AND VARDENAFIL,
COFACTOR, AND ENZYME REGULATION.
PubMed=12955149; DOI=10.1038/nature01914;
Sung B.-J., Hwang K.Y., Jeon Y.H., Lee J.I., Heo Y.-S., Kim J.H.,
Moon J., Yoon J.M., Hyun Y.-L., Kim E., Eum S.J., Park S.-Y.,
Lee J.-O., Lee T.G., Ro S., Cho J.M.;
"Structure of the catalytic domain of human phosphodiesterase 5 with
bound drug molecules.";
Nature 425:98-102(2003).
[12]
FUNCTION.
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: 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 (PubMed:9714779, PubMed:15489334). Specifically regulates
nitric-oxide-generated cGMP (PubMed:15489334).
{ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9714779}.
-!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
guanosine 5'-phosphate. {ECO:0000269|PubMed:9714779}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:12955149};
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:0000269|PubMed:12955149};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12955149};
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:0000269|PubMed:12955149};
-!- ENZYME REGULATION: Sildenafil (Viagra) is a highly selective and
potent inhibitor of PDE5A and is effective in the treatment of
penile erectile dysfunction. Also inhibited by zaprinast.
{ECO:0000269|PubMed:12955149}.
-!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
3',5'-cyclic GMP: step 1/1.
-!- INTERACTION:
Q13976:PRKG1; NbExp=4; IntAct=EBI-9023531, EBI-3952014;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=PDE5A1;
IsoId=O76074-1; Sequence=Displayed;
Name=PDE5A2;
IsoId=O76074-2; Sequence=VSP_004591;
-!- TISSUE SPECIFICITY: Expressed in aortic smooth muscle cells,
heart, placenta, skeletal muscle and pancreas and, to a much
lesser extent, in brain, liver and lung.
-!- 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 (By similarity). Phosphorylation by PRKG1 leads
to its activation. {ECO:0000250, ECO:0000269|PubMed:11723116}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. {ECO:0000305}.
-!- CAUTION: Was initially thought to act as a major regulator of
cardiac hypertrophy in myocytes and muscle and investigations have
been made on selective PDE5A inhibitors that could protect against
cardiovascular disease. However, while PDE5A regulates nitric-
oxide-generated cGMP, nitric oxide signaling is often depressed by
heart disease, limiting its effect. Moreover, clinical trial using
PDE5A inhibitors were disappointing.
{ECO:0000269|PubMed:25799991}.
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EMBL; AF043731; AAC63967.1; -; mRNA.
EMBL; AF043732; AAC63968.1; -; mRNA.
EMBL; AB001635; BAA33372.2; -; Genomic_DNA.
EMBL; D89094; BAA28945.1; -; mRNA.
EMBL; AJ004865; CAA06170.1; -; mRNA.
EMBL; AB015656; BAA81667.1; -; mRNA.
EMBL; AY264918; AAP21809.1; -; mRNA.
EMBL; AK290189; BAF82878.1; -; mRNA.
EMBL; AC093752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC080089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC126233; AAI26234.1; -; mRNA.
EMBL; AY266363; AAP31235.1; -; mRNA.
CCDS; CCDS34055.1; -. [O76074-2]
CCDS; CCDS3713.1; -. [O76074-1]
PIR; JW0106; JW0106.
RefSeq; NP_001074.2; NM_001083.3. [O76074-1]
RefSeq; NP_236914.2; NM_033430.2. [O76074-2]
RefSeq; NP_246273.2; NM_033437.3.
UniGene; Hs.647971; -.
PDB; 1RKP; X-ray; 2.05 A; A=535-860.
PDB; 1T9R; X-ray; 2.10 A; A=531-875.
PDB; 1T9S; X-ray; 2.00 A; A/B=534-858.
PDB; 1TBF; X-ray; 1.30 A; A=534-858.
PDB; 1UDT; X-ray; 2.30 A; A=537-860.
PDB; 1UDU; X-ray; 2.83 A; A/B=537-860.
PDB; 1UHO; X-ray; 2.50 A; A=537-860.
PDB; 1XOZ; X-ray; 1.37 A; A=534-875.
PDB; 1XP0; X-ray; 1.79 A; A=534-875.
PDB; 2CHM; X-ray; 1.60 A; A=534-656, A=682-858.
PDB; 2H40; X-ray; 1.85 A; A=535-860.
PDB; 2H42; X-ray; 2.30 A; A/B/C=535-860.
PDB; 2H44; X-ray; 1.80 A; A=535-860.
PDB; 2XSS; X-ray; 2.50 A; A/B=346-509.
PDB; 3B2R; X-ray; 2.07 A; A/B=535-860.
PDB; 3BJC; X-ray; 2.00 A; A=1-875.
PDB; 3HC8; X-ray; 1.79 A; A=536-657, A=682-858.
PDB; 3HDZ; X-ray; 1.80 A; A=536-657, A=682-858.
PDB; 3JWQ; X-ray; 2.87 A; A/B/C/D=535-786, A/B/C/D=827-860.
PDB; 3JWR; X-ray; 2.99 A; A/B=535-786, A/B=827-860.
PDB; 3LFV; X-ray; 2.80 A; A/B=98-518.
PDB; 3MF0; X-ray; 3.10 A; A/B=89-518.
PDB; 3SHY; X-ray; 2.65 A; A=535-860.
PDB; 3SHZ; X-ray; 2.45 A; A=535-860.
PDB; 3SIE; X-ray; 1.93 A; A/B=535-860.
PDB; 3TGE; X-ray; 1.96 A; A=534-656, A=682-858.
PDB; 3TGG; X-ray; 1.91 A; A=534-660, A=662-858.
PDB; 4G2W; X-ray; 2.28 A; A=535-860.
PDB; 4G2Y; X-ray; 2.40 A; A=535-860.
PDB; 4I9Z; X-ray; 2.08 A; A=535-860.
PDB; 4IA0; X-ray; 2.17 A; A=535-860.
PDB; 4MD6; X-ray; 2.00 A; A=535-860.
PDB; 4OEW; X-ray; 2.44 A; A=535-860.
PDB; 4OEX; X-ray; 2.14 A; A=535-860.
PDB; 5JO3; X-ray; 1.49 A; B=534-858.
PDBsum; 1RKP; -.
PDBsum; 1T9R; -.
PDBsum; 1T9S; -.
PDBsum; 1TBF; -.
PDBsum; 1UDT; -.
PDBsum; 1UDU; -.
PDBsum; 1UHO; -.
PDBsum; 1XOZ; -.
PDBsum; 1XP0; -.
PDBsum; 2CHM; -.
PDBsum; 2H40; -.
PDBsum; 2H42; -.
PDBsum; 2H44; -.
PDBsum; 2XSS; -.
PDBsum; 3B2R; -.
PDBsum; 3BJC; -.
PDBsum; 3HC8; -.
PDBsum; 3HDZ; -.
PDBsum; 3JWQ; -.
PDBsum; 3JWR; -.
PDBsum; 3LFV; -.
PDBsum; 3MF0; -.
PDBsum; 3SHY; -.
PDBsum; 3SHZ; -.
PDBsum; 3SIE; -.
PDBsum; 3TGE; -.
PDBsum; 3TGG; -.
PDBsum; 4G2W; -.
PDBsum; 4G2Y; -.
PDBsum; 4I9Z; -.
PDBsum; 4IA0; -.
PDBsum; 4MD6; -.
PDBsum; 4OEW; -.
PDBsum; 4OEX; -.
PDBsum; 5JO3; -.
ProteinModelPortal; O76074; -.
SMR; O76074; -.
BioGrid; 114205; 8.
DIP; DIP-46287N; -.
IntAct; O76074; 4.
STRING; 9606.ENSP00000347046; -.
BindingDB; O76074; -.
ChEMBL; CHEMBL1827; -.
DrugBank; DB07954; 3-isobutyl-1-methyl-7H-xanthine.
DrugBank; DB06237; Avanafil.
DrugBank; DB00201; Caffeine.
DrugBank; DB04272; Citric Acid.
DrugBank; DB00975; Dipyridamole.
DrugBank; DB03597; Gamma-Glutamyl[S-(2-Iodobenzyl)Cysteinyl]Glycine.
DrugBank; DB01972; Guanosine-5'-Monophosphate.
DrugBank; DB05415; OSI-461.
DrugBank; DB00806; Pentoxifylline.
DrugBank; DB00203; Sildenafil.
DrugBank; DB00820; Tadalafil.
DrugBank; DB00277; Theophylline.
DrugBank; DB06267; Udenafil.
DrugBank; DB00862; Vardenafil.
GuidetoPHARMACOLOGY; 1304; -.
iPTMnet; O76074; -.
PhosphoSitePlus; O76074; -.
BioMuta; PDE5A; -.
EPD; O76074; -.
MaxQB; O76074; -.
PaxDb; O76074; -.
PeptideAtlas; O76074; -.
PRIDE; O76074; -.
DNASU; 8654; -.
Ensembl; ENST00000264805; ENSP00000264805; ENSG00000138735. [O76074-2]
Ensembl; ENST00000354960; ENSP00000347046; ENSG00000138735. [O76074-1]
GeneID; 8654; -.
KEGG; hsa:8654; -.
UCSC; uc003idf.4; human. [O76074-1]
CTD; 8654; -.
DisGeNET; 8654; -.
EuPathDB; HostDB:ENSG00000138735.15; -.
GeneCards; PDE5A; -.
HGNC; HGNC:8784; PDE5A.
HPA; HPA004729; -.
HPA; HPA012873; -.
MIM; 603310; gene.
neXtProt; NX_O76074; -.
OpenTargets; ENSG00000138735; -.
PharmGKB; PA33132; -.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000119066; -.
HOVERGEN; HBG101207; -.
KO; K13762; -.
OMA; VDEDCSD; -.
OrthoDB; EOG091G04JU; -.
PhylomeDB; O76074; -.
TreeFam; TF316499; -.
BRENDA; 3.1.4.35; 2681.
Reactome; R-HSA-418457; cGMP effects.
SIGNOR; O76074; -.
UniPathway; UPA00763; UER00748.
ChiTaRS; PDE5A; human.
EvolutionaryTrace; O76074; -.
GeneWiki; CGMP-specific_phosphodiesterase_type_5; -.
GenomeRNAi; 8654; -.
PRO; PR:O76074; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138735; -.
CleanEx; HS_PDE5A; -.
ExpressionAtlas; O76074; baseline and differential.
Genevisible; O76074; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; NAS:UniProtKB.
GO; GO:0030553; F:cGMP binding; TAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046069; P:cGMP catabolic process; IDA:UniProtKB.
GO; GO:0055118; P:negative regulation of cardiac muscle contraction; IEA:Ensembl.
GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0060282; P:positive regulation of oocyte development; IEA:Ensembl.
GO; GO:0030823; P:regulation of cGMP metabolic process; IEA:Ensembl.
GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
Gene3D; 3.30.450.40; -; 2.
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.
SUPFAM; SSF55781; SSF55781; 2.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Alternative splicing; cGMP;
cGMP-binding; Complete proteome; Hydrolase; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat.
CHAIN 1 875 cGMP-specific 3',5'-cyclic
phosphodiesterase.
/FTId=PRO_0000198823.
DOMAIN 164 314 GAF 1.
DOMAIN 346 503 GAF 2.
REGION 588 853 Catalytic. {ECO:0000250}.
COMPBIAS 10 24 Poly-Gln.
ACT_SITE 613 613 Proton donor.
{ECO:0000250|UniProtKB:O76083}.
METAL 617 617 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:12955149}.
METAL 653 653 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:12955149}.
METAL 654 654 Magnesium. {ECO:0000269|PubMed:12955149}.
METAL 654 654 Zinc. {ECO:0000269|PubMed:12955149}.
METAL 764 764 Zinc. {ECO:0000269|PubMed:12955149}.
BINDING 817 817 cGMP. {ECO:0000269|PubMed:12955149}.
MOD_RES 102 102 Phosphoserine. {ECO:0000255}.
VAR_SEQ 1 49 MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFT
FSYFVRKA -> MLPFGDK (in isoform PDE5A2).
{ECO:0000303|PubMed:9714779,
ECO:0000303|Ref.4, ECO:0000303|Ref.5}.
/FTId=VSP_004591.
VARIANT 93 93 A -> V (in dbSNP:rs3733526).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:9642111,
ECO:0000269|PubMed:9714779,
ECO:0000269|PubMed:9716380,
ECO:0000269|Ref.4}.
/FTId=VAR_027775.
VARIANT 181 181 S -> A (in dbSNP:rs17051276).
/FTId=VAR_027776.
CONFLICT 159 159 I -> V (in Ref. 9; AAP31235).
{ECO:0000305}.
CONFLICT 310 310 C -> G (in Ref. 9; AAP31235).
{ECO:0000305}.
CONFLICT 381 381 S -> F (in Ref. 9; AAP31235).
{ECO:0000305}.
CONFLICT 406 406 K -> R (in Ref. 9; AAP31235).
{ECO:0000305}.
CONFLICT 642 642 E -> G (in Ref. 4; BAA81667).
{ECO:0000305}.
HELIX 103 106 {ECO:0000244|PDB:3LFV}.
STRAND 115 117 {ECO:0000244|PDB:3LFV}.
TURN 118 120 {ECO:0000244|PDB:3LFV}.
STRAND 121 124 {ECO:0000244|PDB:3LFV}.
HELIX 148 160 {ECO:0000244|PDB:3LFV}.
HELIX 165 177 {ECO:0000244|PDB:3LFV}.
STRAND 182 192 {ECO:0000244|PDB:3LFV}.
STRAND 198 205 {ECO:0000244|PDB:3LFV}.
STRAND 208 210 {ECO:0000244|PDB:3MF0}.
STRAND 213 218 {ECO:0000244|PDB:3LFV}.
STRAND 221 224 {ECO:0000244|PDB:3LFV}.
HELIX 228 236 {ECO:0000244|PDB:3LFV}.
STRAND 240 243 {ECO:0000244|PDB:3LFV}.
HELIX 245 247 {ECO:0000244|PDB:3LFV}.
HELIX 254 259 {ECO:0000244|PDB:3LFV}.
STRAND 266 272 {ECO:0000244|PDB:3LFV}.
STRAND 278 287 {ECO:0000244|PDB:3LFV}.
HELIX 299 340 {ECO:0000244|PDB:3LFV}.
TURN 342 345 {ECO:0000244|PDB:3MF0}.
HELIX 346 362 {ECO:0000244|PDB:2XSS}.
STRAND 365 372 {ECO:0000244|PDB:2XSS}.
STRAND 374 376 {ECO:0000244|PDB:3LFV}.
STRAND 379 387 {ECO:0000244|PDB:2XSS}.
TURN 388 390 {ECO:0000244|PDB:3LFV}.
STRAND 391 393 {ECO:0000244|PDB:3LFV}.
HELIX 400 403 {ECO:0000244|PDB:2XSS}.
HELIX 407 409 {ECO:0000244|PDB:2XSS}.
HELIX 410 418 {ECO:0000244|PDB:2XSS}.
STRAND 422 425 {ECO:0000244|PDB:2XSS}.
TURN 427 429 {ECO:0000244|PDB:2XSS}.
STRAND 431 433 {ECO:0000244|PDB:3LFV}.
STRAND 451 457 {ECO:0000244|PDB:2XSS}.
STRAND 461 471 {ECO:0000244|PDB:2XSS}.
TURN 476 478 {ECO:0000244|PDB:3LFV}.
HELIX 486 506 {ECO:0000244|PDB:2XSS}.
HELIX 535 545 {ECO:0000244|PDB:1TBF}.
HELIX 551 554 {ECO:0000244|PDB:1TBF}.
TURN 555 557 {ECO:0000244|PDB:1TBF}.
HELIX 568 581 {ECO:0000244|PDB:1TBF}.
HELIX 584 587 {ECO:0000244|PDB:1TBF}.
HELIX 592 604 {ECO:0000244|PDB:1TBF}.
TURN 606 608 {ECO:0000244|PDB:1T9R}.
STRAND 610 614 {ECO:0000244|PDB:1TBF}.
HELIX 615 630 {ECO:0000244|PDB:1TBF}.
TURN 631 633 {ECO:0000244|PDB:1UHO}.
HELIX 635 637 {ECO:0000244|PDB:1TBF}.
HELIX 640 652 {ECO:0000244|PDB:1TBF}.
TURN 653 656 {ECO:0000244|PDB:1TBF}.
HELIX 662 667 {ECO:0000244|PDB:1TBF}.
HELIX 671 675 {ECO:0000244|PDB:1TBF}.
STRAND 677 679 {ECO:0000244|PDB:3JWQ}.
HELIX 680 694 {ECO:0000244|PDB:1TBF}.
TURN 700 703 {ECO:0000244|PDB:1TBF}.
HELIX 706 722 {ECO:0000244|PDB:1TBF}.
HELIX 725 740 {ECO:0000244|PDB:1TBF}.
STRAND 746 748 {ECO:0000244|PDB:1UDU}.
HELIX 749 764 {ECO:0000244|PDB:1TBF}.
HELIX 766 769 {ECO:0000244|PDB:1TBF}.
HELIX 772 796 {ECO:0000244|PDB:1TBF}.
HELIX 803 805 {ECO:0000244|PDB:1TBF}.
HELIX 807 812 {ECO:0000244|PDB:1TBF}.
HELIX 813 823 {ECO:0000244|PDB:1TBF}.
HELIX 825 835 {ECO:0000244|PDB:1TBF}.
HELIX 837 839 {ECO:0000244|PDB:1TBF}.
HELIX 840 857 {ECO:0000244|PDB:1TBF}.
SEQUENCE 875 AA; 99985 MW; 9E30C6C182F13388 CRC64;
MERAGPSFGQ QRQQQQPQQQ KQQQRDQDSV EAWLDDHWDF TFSYFVRKAT REMVNAWFAE
RVHTIPVCKE GIRGHTESCS CPLQQSPRAD NSAPGTPTRK ISASEFDRPL RPIVVKDSEG
TVSFLSDSEK KEQMPLTPPR FDHDEGDQCS RLLELVKDIS SHLDVTALCH KIFLHIHGLI
SADRYSLFLV CEDSSNDKFL ISRLFDVAEG STLEEVSNNC IRLEWNKGIV GHVAALGEPL
NIKDAYEDPR FNAEVDQITG YKTQSILCMP IKNHREEVVG VAQAINKKSG NGGTFTEKDE
KDFAAYLAFC GIVLHNAQLY ETSLLENKRN QVLLDLASLI FEEQQSLEVI LKKIAATIIS
FMQVQKCTIF IVDEDCSDSF SSVFHMECEE LEKSSDTLTR EHDANKINYM YAQYVKNTME
PLNIPDVSKD KRFPWTTENT GNVNQQCIRS LLCTPIKNGK KNKVIGVCQL VNKMEENTGK
VKPFNRNDEQ FLEAFVIFCG LGIQNTQMYE AVERAMAKQM VTLEVLSYHA SAAEEETREL
QSLAAAVVPS AQTLKITDFS FSDFELSDLE TALCTIRMFT DLNLVQNFQM KHEVLCRWIL
SVKKNYRKNV AYHNWRHAFN TAQCMFAALK AGKIQNKLTD LEILALLIAA LSHDLDHRGV
NNSYIQRSEH PLAQLYCHSI MEHHHFDQCL MILNSPGNQI LSGLSIEEYK TTLKIIKQAI
LATDLALYIK RRGEFFELIR KNQFNLEDPH QKELFLAMLM TACDLSAITK PWPIQQRIAE
LVATEFFDQG DRERKELNIE PTDLMNREKK NKIPSMQVGF IDAICLQLYE ALTHVSEDCF
PLLDGCRKNR QKWQALAEQQ EKMLINGESG QAKRN


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