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Database: UniProt
Entry: O76074
LinkDB: O76074
Original site: O76074 
ID   PDE5A_HUMAN             Reviewed;         875 AA.
AC   O76074; A0AV69; A8K2C4; O75026; O75887; Q86UI0; Q86V66; Q9Y6Z6;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   09-JUL-2014, entry version 143.
DE   RecName: Full=cGMP-specific 3',5'-cyclic phosphodiesterase;
DE            EC=3.1.4.35;
DE   AltName: Full=cGMP-binding cGMP-specific phosphodiesterase;
DE            Short=CGB-PDE;
GN   Name=PDE5A; Synonyms=PDE5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE5A1 AND PDE5A2), AND VARIANT
RP   VAL-93.
RX   PubMed=9714779; DOI=10.1016/S0378-1119(98)00303-5;
RA   Loughney K., Hill T.R., Florio V.A., Uher L., Rosman G.J., Wolda S.L.,
RA   Jones B.A., Howard M.L., McAllister-Lucas L.M., Sonnenburg W.K.,
RA   Francis S.H., Corbin J.D., Beavo J.A., Ferguson K.;
RT   "Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-
RT   binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase.";
RL   Gene 216:139-147(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM PDE5A1), AND VARIANT
RP   VAL-93.
RC   TISSUE=Lung, and Placenta;
RX   PubMed=9716380; DOI=10.1046/j.1432-1327.1998.2550391.x;
RA   Yanaka N., Kotera J., Ohtsuka A., Akatsuka H., Imai Y., Michibata H.,
RA   Fujishige K., Kawai E., Takebayashi S., Okumura K., Omori K.;
RT   "Expression, structure and chromosomal localization of the human cGMP-
RT   binding cGMP-specific phosphodiesterase PDE5A gene.";
RL   Eur. J. Biochem. 255:391-399(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A1), AND VARIANT VAL-93.
RC   TISSUE=Prostate, and Skeletal muscle;
RX   PubMed=9642111; DOI=10.1006/bbrc.1998.8769;
RA   Stacey P., Rulten S., Dapling A., Phillips S.C.;
RT   "Molecular cloning and expression of human cGMP-binding cGMP-specific
RT   phosphodiesterase.";
RL   Biochem. Biophys. Res. Commun. 247:249-254(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A2), AND VARIANT VAL-93.
RC   TISSUE=Lung;
RA   Kotera J., Imai Y., Omori K.;
RT   "Molecular cloning and characterization of human cGMP-specific
RT   phosphodiesterase 5A2 cDNA.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE5A2).
RC   TISSUE=Colon carcinoma;
RA   Sopory S., Visweswariah S.S.;
RT   "PDE5A splice variants in T84 cells.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE5A1), AND VARIANT
RP   VAL-93.
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE5A1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 157-411.
RC   TISSUE=Trabecular meshwork;
RX   PubMed=10393044;
RA   Zhou L., Thompson W.J., Potter D.E.;
RT   "Multiple cyclic nucleotide phosphodiesterases in human trabecular
RT   meshwork cells.";
RL   Invest. Ophthalmol. Vis. Sci. 40:1745-1752(1999).
RN   [10]
RP   PHOSPHORYLATION BY PRKG1.
RX   PubMed=11723116; DOI=10.1074/jbc.M106562200;
RA   Rybalkin S.D., Rybalkina I.G., Feil R., Hofmann F., Beavo J.A.;
RT   "Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation
RT   in smooth muscle cells.";
RL   J. Biol. Chem. 277:3310-3317(2002).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 537-860 IN COMPLEX WITH THE
RP   INHIBITORS SILDENAFIL; TADALAFIL AND VARDENAFIL, AND METAL-BINDING.
RX   PubMed=12955149; DOI=10.1038/nature01914;
RA   Sung B.-J., Hwang K.Y., Jeon Y.H., Lee J.I., Heo Y.-S., Kim J.H.,
RA   Moon J., Yoon J.M., Hyun Y.-L., Kim E., Eum S.J., Park S.-Y.,
RA   Lee J.-O., Lee T.G., Ro S., Cho J.M.;
RT   "Structure of the catalytic domain of human phosphodiesterase 5 with
RT   bound drug molecules.";
RL   Nature 425:98-102(2003).
CC   -!- FUNCTION: Plays a role in signal transduction by regulating the
CC       intracellular concentration of cyclic nucleotides. This
CC       phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-
CC       GMP.
CC   -!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
CC       guanosine 5'-phosphate.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions.
CC   -!- ENZYME REGULATION: Sildenafil (Viagra) is a highly selective and
CC       potent inhibitor of PDE5A and is effective in the treatment of
CC       penile erectile dysfunction. Also inhibited by zaprinast.
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
CC       3',5'-cyclic GMP: step 1/1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=PDE5A1;
CC         IsoId=O76074-1; Sequence=Displayed;
CC       Name=PDE5A2;
CC         IsoId=O76074-2; Sequence=VSP_004591;
CC   -!- TISSUE SPECIFICITY: Expressed in aortic smooth muscle cells,
CC       heart, placenta, skeletal muscle and pancreas and, to a much
CC       lesser extent, in brain, liver and lung.
CC   -!- DOMAIN: Composed of a C-terminal catalytic domain containing two
CC       putative divalent metal sites and an N-terminal regulatory domain
CC       which contains two homologous allosteric cGMP-binding regions, A
CC       and B.
CC   -!- PTM: Phosphorylation is regulated by binding of cGMP to the two
CC       allosteric sites (By similarity). Phosphorylation by PRKG1 leads
CC       to its activation.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family.
CC   -!- SIMILARITY: Contains 2 GAF domains.
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DR   EMBL; AF043731; AAC63967.1; -; mRNA.
DR   EMBL; AF043732; AAC63968.1; -; mRNA.
DR   EMBL; AB001635; BAA33372.2; -; Genomic_DNA.
DR   EMBL; D89094; BAA28945.1; -; mRNA.
DR   EMBL; AJ004865; CAA06170.1; -; mRNA.
DR   EMBL; AB015656; BAA81667.1; -; mRNA.
DR   EMBL; AY264918; AAP21809.1; -; mRNA.
DR   EMBL; AK290189; BAF82878.1; -; mRNA.
DR   EMBL; AC093752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC080089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC126233; AAI26234.1; -; mRNA.
DR   EMBL; AY266363; AAP31235.1; -; mRNA.
DR   CCDS; CCDS34055.1; -. [O76074-2]
DR   CCDS; CCDS3713.1; -. [O76074-1]
DR   PIR; JW0106; JW0106.
DR   RefSeq; NP_001074.2; NM_001083.3. [O76074-1]
DR   RefSeq; NP_236914.2; NM_033430.2. [O76074-2]
DR   RefSeq; NP_246273.2; NM_033437.3.
DR   UniGene; Hs.647971; -.
DR   PDB; 1RKP; X-ray; 2.05 A; A=535-860.
DR   PDB; 1T9R; X-ray; 2.10 A; A=531-875.
DR   PDB; 1T9S; X-ray; 2.00 A; A/B=534-858.
DR   PDB; 1TBF; X-ray; 1.30 A; A=534-858.
DR   PDB; 1UDT; X-ray; 2.30 A; A=537-860.
DR   PDB; 1UDU; X-ray; 2.83 A; A/B=537-860.
DR   PDB; 1UHO; X-ray; 2.50 A; A=537-860.
DR   PDB; 1XOZ; X-ray; 1.37 A; A=534-875.
DR   PDB; 1XP0; X-ray; 1.79 A; A=534-875.
DR   PDB; 2CHM; X-ray; 1.60 A; A=534-656, A=682-858.
DR   PDB; 2H40; X-ray; 1.85 A; A=535-860.
DR   PDB; 2H42; X-ray; 2.30 A; A/B/C=535-860.
DR   PDB; 2H44; X-ray; 1.80 A; A=535-860.
DR   PDB; 2XSS; X-ray; 2.50 A; A/B=346-509.
DR   PDB; 3B2R; X-ray; 2.07 A; A/B=535-860.
DR   PDB; 3BJC; X-ray; 2.00 A; A=1-875.
DR   PDB; 3HC8; X-ray; 1.79 A; A=536-858.
DR   PDB; 3HDZ; X-ray; 1.80 A; A=536-657, A=682-858.
DR   PDB; 3JWQ; X-ray; 2.87 A; A/B/C/D=535-786, A/B/C/D=827-860.
DR   PDB; 3JWR; X-ray; 2.99 A; A/B=535-786, A/B=706-860.
DR   PDB; 3LFV; X-ray; 2.80 A; A/B=98-518.
DR   PDB; 3MF0; X-ray; 3.10 A; A/B=89-518.
DR   PDB; 3SHY; X-ray; 2.65 A; A=535-860.
DR   PDB; 3SHZ; X-ray; 2.45 A; A=535-860.
DR   PDB; 3SIE; X-ray; 1.93 A; A/B=535-860.
DR   PDB; 3TGE; X-ray; 1.96 A; A=534-656, A=682-858.
DR   PDB; 3TGG; X-ray; 1.91 A; A=534-858.
DR   PDB; 3TSE; X-ray; 2.14 A; A=535-860.
DR   PDB; 3TSF; X-ray; 2.44 A; A=535-860.
DR   PDB; 4G2W; X-ray; 2.28 A; A=535-860.
DR   PDB; 4G2Y; X-ray; 2.40 A; A=535-860.
DR   PDB; 4I9Z; X-ray; 2.08 A; A=535-860.
DR   PDB; 4IA0; X-ray; 2.17 A; A=535-860.
DR   PDBsum; 1RKP; -.
DR   PDBsum; 1T9R; -.
DR   PDBsum; 1T9S; -.
DR   PDBsum; 1TBF; -.
DR   PDBsum; 1UDT; -.
DR   PDBsum; 1UDU; -.
DR   PDBsum; 1UHO; -.
DR   PDBsum; 1XOZ; -.
DR   PDBsum; 1XP0; -.
DR   PDBsum; 2CHM; -.
DR   PDBsum; 2H40; -.
DR   PDBsum; 2H42; -.
DR   PDBsum; 2H44; -.
DR   PDBsum; 2XSS; -.
DR   PDBsum; 3B2R; -.
DR   PDBsum; 3BJC; -.
DR   PDBsum; 3HC8; -.
DR   PDBsum; 3HDZ; -.
DR   PDBsum; 3JWQ; -.
DR   PDBsum; 3JWR; -.
DR   PDBsum; 3LFV; -.
DR   PDBsum; 3MF0; -.
DR   PDBsum; 3SHY; -.
DR   PDBsum; 3SHZ; -.
DR   PDBsum; 3SIE; -.
DR   PDBsum; 3TGE; -.
DR   PDBsum; 3TGG; -.
DR   PDBsum; 3TSE; -.
DR   PDBsum; 3TSF; -.
DR   PDBsum; 4G2W; -.
DR   PDBsum; 4G2Y; -.
DR   PDBsum; 4I9Z; -.
DR   PDBsum; 4IA0; -.
DR   ProteinModelPortal; O76074; -.
DR   SMR; O76074; 98-860.
DR   BioGrid; 114205; 1.
DR   DIP; DIP-46287N; -.
DR   STRING; 9606.ENSP00000347046; -.
DR   BindingDB; O76074; -.
DR   ChEMBL; CHEMBL2111340; -.
DR   DrugBank; DB00975; Dipyridamole.
DR   DrugBank; DB00806; Pentoxifylline.
DR   DrugBank; DB00203; Sildenafil.
DR   DrugBank; DB00820; Tadalafil.
DR   DrugBank; DB00277; Theophylline.
DR   DrugBank; DB00862; Vardenafil.
DR   GuidetoPHARMACOLOGY; 1304; -.
DR   PhosphoSite; O76074; -.
DR   MaxQB; O76074; -.
DR   PaxDb; O76074; -.
DR   PRIDE; O76074; -.
DR   DNASU; 8654; -.
DR   Ensembl; ENST00000264805; ENSP00000264805; ENSG00000138735. [O76074-2]
DR   Ensembl; ENST00000354960; ENSP00000347046; ENSG00000138735. [O76074-1]
DR   GeneID; 8654; -.
DR   KEGG; hsa:8654; -.
DR   UCSC; uc003idf.3; human. [O76074-2]
DR   UCSC; uc003idg.3; human. [O76074-1]
DR   CTD; 8654; -.
DR   GeneCards; GC04M120415; -.
DR   HGNC; HGNC:8784; PDE5A.
DR   HPA; HPA004729; -.
DR   HPA; HPA012873; -.
DR   MIM; 603310; gene.
DR   neXtProt; NX_O76074; -.
DR   PharmGKB; PA33132; -.
DR   eggNOG; NOG270709; -.
DR   HOVERGEN; HBG101207; -.
DR   InParanoid; O76074; -.
DR   KO; K13762; -.
DR   OMA; REHDANK; -.
DR   OrthoDB; EOG7RRF69; -.
DR   PhylomeDB; O76074; -.
DR   TreeFam; TF316499; -.
DR   BRENDA; 3.1.4.35; 2681.
DR   Reactome; REACT_604; Hemostasis.
DR   UniPathway; UPA00763; UER00748.
DR   ChiTaRS; PDE5A; human.
DR   EvolutionaryTrace; O76074; -.
DR   GeneWiki; CGMP-specific_phosphodiesterase_type_5; -.
DR   GenomeRNAi; 8654; -.
DR   NextBio; 32453; -.
DR   PRO; PR:O76074; -.
DR   ArrayExpress; O76074; -.
DR   Bgee; O76074; -.
DR   CleanEx; HS_PDE5A; -.
DR   Genevestigator; O76074; -.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; NAS:UniProtKB.
DR   GO; GO:0030553; F:cGMP binding; TAS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0046069; P:cGMP catabolic process; IDA:UniProtKB.
DR   GO; GO:0055118; P:negative regulation of cardiac muscle contraction; IEA:Ensembl.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
DR   GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IEA:Ensembl.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR   GO; GO:0060282; P:positive regulation of oocyte development; IEA:Ensembl.
DR   GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.1300.10; -; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF_dom_like.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF55781; SSF55781; 2.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Alternative splicing; cGMP;
KW   cGMP-binding; Complete proteome; Hydrolase; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat.
FT   CHAIN         1    875       cGMP-specific 3',5'-cyclic
FT                                phosphodiesterase.
FT                                /FTId=PRO_0000198823.
FT   DOMAIN      164    314       GAF 1.
FT   DOMAIN      346    503       GAF 2.
FT   REGION      588    853       Catalytic (By similarity).
FT   COMPBIAS     10     24       Poly-Gln.
FT   ACT_SITE    613    613       Proton donor (By similarity).
FT   METAL       617    617       Divalent metal cation 1.
FT   METAL       653    653       Divalent metal cation 1.
FT   METAL       654    654       Divalent metal cation 1.
FT   METAL       654    654       Divalent metal cation 2.
FT   METAL       764    764       Divalent metal cation 1.
FT   BINDING     817    817       cGMP.
FT   MOD_RES     102    102       Phosphoserine (Potential).
FT   VAR_SEQ       1     49       MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFT
FT                                FSYFVRKA -> MLPFGDK (in isoform PDE5A2).
FT                                /FTId=VSP_004591.
FT   VARIANT      93     93       A -> V (in dbSNP:rs3733526).
FT                                /FTId=VAR_027775.
FT   VARIANT     181    181       S -> A (in dbSNP:rs17051276).
FT                                /FTId=VAR_027776.
FT   CONFLICT    159    159       I -> V (in Ref. 9; AAP31235).
FT   CONFLICT    310    310       C -> G (in Ref. 9; AAP31235).
FT   CONFLICT    381    381       S -> F (in Ref. 9; AAP31235).
FT   CONFLICT    406    406       K -> R (in Ref. 9; AAP31235).
FT   CONFLICT    642    642       E -> G (in Ref. 4; BAA81667).
FT   HELIX       103    106
FT   STRAND      115    117
FT   TURN        118    120
FT   STRAND      121    124
FT   HELIX       148    160
FT   HELIX       165    177
FT   STRAND      182    192
FT   STRAND      198    205
FT   STRAND      208    210
FT   STRAND      213    218
FT   STRAND      221    224
FT   HELIX       228    236
FT   STRAND      240    243
FT   HELIX       245    247
FT   HELIX       254    259
FT   STRAND      266    272
FT   STRAND      278    287
FT   HELIX       299    340
FT   TURN        342    345
FT   HELIX       346    362
FT   STRAND      365    372
FT   STRAND      374    376
FT   STRAND      379    387
FT   TURN        388    390
FT   STRAND      391    393
FT   HELIX       400    403
FT   HELIX       407    409
FT   HELIX       410    418
FT   STRAND      422    425
FT   TURN        427    429
FT   STRAND      431    433
FT   STRAND      451    457
FT   STRAND      461    471
FT   TURN        476    478
FT   HELIX       486    506
FT   HELIX       535    545
FT   HELIX       551    554
FT   TURN        555    557
FT   HELIX       568    581
FT   HELIX       584    587
FT   HELIX       592    604
FT   TURN        606    608
FT   STRAND      610    614
FT   HELIX       615    630
FT   TURN        631    633
FT   HELIX       635    637
FT   HELIX       640    652
FT   TURN        653    656
FT   HELIX       662    667
FT   HELIX       671    675
FT   STRAND      677    679
FT   HELIX       680    694
FT   TURN        700    703
FT   HELIX       706    722
FT   HELIX       725    740
FT   STRAND      746    748
FT   HELIX       749    764
FT   HELIX       766    769
FT   HELIX       772    796
FT   HELIX       803    805
FT   HELIX       807    812
FT   HELIX       813    823
FT   HELIX       825    835
FT   HELIX       837    839
FT   HELIX       840    857
SQ   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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