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cGMP-inhibited 3',5'-cyclic phosphodiesterase A (EC 3.1.4.17) (Cyclic GMP-inhibited phosphodiesterase A) (CGI-PDE A)

 PDE3A_HUMAN             Reviewed;        1141 AA.
Q14432; O60865; Q13348; Q17RD1;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 3.
30-AUG-2017, entry version 163.
RecName: Full=cGMP-inhibited 3',5'-cyclic phosphodiesterase A;
EC=3.1.4.17;
AltName: Full=Cyclic GMP-inhibited phosphodiesterase A;
Short=CGI-PDE A;
Name=PDE3A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Myocardium;
PubMed=1315035; DOI=10.1073/pnas.89.9.3721;
Meacci E., Taira M., Moos M. Jr., Smith C.J., Movsesian M.A.,
Degerman E., Belfrage P., Manganiello V.;
"Molecular cloning and expression of human myocardial cGMP-inhibited
cAMP phosphodiesterase.";
Proc. Natl. Acad. Sci. U.S.A. 89:3721-3725(1992).
[2]
SEQUENCE REVISION TO 12; 63-64 AND 354-371.
Liu H., Manganiello V.;
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-12.
TISSUE=Blood;
PubMed=8695850;
Cheung P.P., Xu H., McLaughlin M.M., Ghazaleh F.A., Livi G.P.,
Colman R.W.;
"Human platelet cGI-PDE: expression in yeast and localization of the
catalytic domain by deletion mutagenesis.";
Blood 88:1321-1329(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Penis;
PubMed=10421499; DOI=10.1016/S0009-2797(99)00074-5;
Kuthe A., Eckel H., Stief C.G., Uckert S., Forssmann W.-G., Jonas U.,
Maegert H.-J.;
"Molecular biological characterization of phosphodiesterase 3A from
human corpus cavernosum.";
Chem. Biol. Interact. 119:593-598(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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).
[6]
PARTIAL PROTEIN SEQUENCE.
PubMed=8155697; DOI=10.1016/0167-4838(94)90233-X;
Degerman E., Moos M. Jr., Rascon A., Vasta V., Meacci E., Smith C.J.,
Lindgren S., Andersson K.-E., Belfrage P., Manganiello V.;
"Single-step affinity purification, partial structure and properties
of human platelet cGMP inhibited cAMP phosphodiesterase.";
Biochim. Biophys. Acta 1205:189-198(1994).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-492 AND
SER-520, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
INVOLVEMENT IN HTNB, VARIANTS HTNB ALA-445; ASN-445; SER-445; THR-447;
VAL-447 AND VAL-449, AND CHARACTERIZATION OF VARIANTS HTNB ALA-445;
ASN-445; SER-445; THR-447; VAL-447 AND VAL-449.
PubMed=25961942; DOI=10.1038/ng.3302;
Maass P.G., Aydin A., Luft F.C., Schaechterle C., Weise A.,
Stricker S., Lindschau C., Vaegler M., Qadri F., Toka H.R., Schulz H.,
Krawitz P.M., Parkhomchuk D., Hecht J., Hollfinger I.,
Wefeld-Neuenfeld Y., Bartels-Klein E., Muehl A., Kann M., Schuster H.,
Chitayat D., Bialer M.G., Wienker T.F., Ott J., Rittscher K.,
Liehr T., Jordan J., Plessis G., Tank J., Mai K., Naraghi R.,
Hodge R., Hopp M., Hattenbach L.O., Busjahn A., Rauch A., Vandeput F.,
Gong M., Rueschendorf F., Huebner N., Haller H., Mundlos S.,
Bilginturan N., Movsesian M.A., Klussmann E., Toka O., Baehring S.;
"PDE3A mutations cause autosomal dominant hypertension with
brachydactyly.";
Nat. Genet. 47:647-653(2015).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1120, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-
specificity for the second messengers cAMP and cGMP, which are key
regulators of many important physiological processes.
{ECO:0000250|UniProtKB:Q9Z0X4}.
-!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
nucleoside 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=Binds 2 divalent metal cations per subunit. Site 1 may
preferentially bind zinc ions, while site 2 has a preference for
magnesium and/or manganese ions. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by cGMP.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- DISEASE: Hypertension and brachydactyly syndrome (HTNB)
[MIM:112410]: A syndrome characterized by brachydactyly type E,
severe salt-independent but age-dependent hypertension, an
increased fibroblast growth rate, neurovascular contact at the
rostral-ventrolateral medulla, and altered baroreflex blood
pressure regulation. It results in death from stroke before age 50
years when untreated. Brachydactyly type E is characterized by
shortening of the fingers mainly in the metacarpals and
metatarsals. {ECO:0000269|PubMed:25961942}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE3 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=PDE3 entry;
URL="https://en.wikipedia.org/wiki/PDE3";
-----------------------------------------------------------------------
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EMBL; M91667; AAA35912.2; -; mRNA.
EMBL; U36798; AAB18673.1; -; mRNA.
EMBL; AJ005036; CAA06304.1; -; mRNA.
EMBL; BC117369; AAI17370.1; -; mRNA.
EMBL; BC117371; AAI17372.1; -; mRNA.
CCDS; CCDS31754.1; -.
PIR; A44093; A44093.
RefSeq; NP_000912.3; NM_000921.4.
UniGene; Hs.386791; -.
UniGene; Hs.737522; -.
PDB; 1LRC; Model; -; A=812-1017.
PDBsum; 1LRC; -.
ProteinModelPortal; Q14432; -.
SMR; Q14432; -.
BioGrid; 111165; 27.
DIP; DIP-42197N; -.
IntAct; Q14432; 15.
MINT; MINT-3295914; -.
STRING; 9606.ENSP00000351957; -.
BindingDB; Q14432; -.
ChEMBL; CHEMBL241; -.
DrugBank; DB01223; Aminophylline.
DrugBank; DB01427; Amrinone.
DrugBank; DB00261; Anagrelide.
DrugBank; DB00201; Caffeine.
DrugBank; DB01166; Cilostazol.
DrugBank; DB04880; Enoximone.
DrugBank; DB05266; Ibudilast.
DrugBank; DB00922; Levosimendan.
DrugBank; DB00235; Milrinone.
DrugBank; DB01303; Oxtriphylline.
DrugBank; DB00277; Theophylline.
DrugBank; DB08811; Tofisopam.
GuidetoPHARMACOLOGY; 1298; -.
iPTMnet; Q14432; -.
PhosphoSitePlus; Q14432; -.
BioMuta; PDE3A; -.
DMDM; 47117888; -.
EPD; Q14432; -.
MaxQB; Q14432; -.
PaxDb; Q14432; -.
PeptideAtlas; Q14432; -.
PRIDE; Q14432; -.
Ensembl; ENST00000359062; ENSP00000351957; ENSG00000172572.
GeneID; 5139; -.
KEGG; hsa:5139; -.
UCSC; uc001reh.3; human.
CTD; 5139; -.
DisGeNET; 5139; -.
GeneCards; PDE3A; -.
HGNC; HGNC:8778; PDE3A.
HPA; HPA014492; -.
MalaCards; PDE3A; -.
MIM; 112410; phenotype.
MIM; 123805; gene.
neXtProt; NX_Q14432; -.
OpenTargets; ENSG00000172572; -.
PharmGKB; PA33126; -.
eggNOG; ENOG410IEGG; Eukaryota.
eggNOG; ENOG410XT2V; LUCA.
GeneTree; ENSGT00760000119066; -.
HOGENOM; HOG000060144; -.
HOVERGEN; HBG053541; -.
KO; K19021; -.
OMA; PNEEETC; -.
OrthoDB; EOG091G0BTI; -.
PhylomeDB; Q14432; -.
TreeFam; TF329631; -.
BRENDA; 3.1.4.17; 2681.
Reactome; R-HSA-418457; cGMP effects.
Reactome; R-HSA-418555; G alpha (s) signalling events.
SABIO-RK; Q14432; -.
SIGNOR; Q14432; -.
ChiTaRS; PDE3A; human.
GenomeRNAi; 5139; -.
PRO; PR:Q14432; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000172572; -.
CleanEx; HS_PDE3A; -.
Genevisible; Q14432; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0030552; F:cAMP binding; IEA:Ensembl.
GO; GO:0004119; F:cGMP-inhibited cyclic-nucleotide phosphodiesterase activity; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IDA:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB.
GO; GO:0071321; P:cellular response to cGMP; IDA:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
GO; GO:0019934; P:cGMP-mediated signaling; IMP:UniProtKB.
GO; GO:0016101; P:diterpenoid metabolic process; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0043116; P:negative regulation of vascular permeability; IMP:UniProtKB.
GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
GO; GO:0060282; P:positive regulation of oocyte development; IEA:Ensembl.
GO; GO:0043117; P:positive regulation of vascular permeability; IMP:UniProtKB.
GO; GO:0040020; P:regulation of meiotic nuclear division; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR023174; PDEase_CS.
Pfam; PF00233; PDEase_I; 1.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
3D-structure; cAMP; cGMP; Complete proteome;
Direct protein sequencing; Disease mutation; Hydrolase;
Isopeptide bond; Membrane; Metal-binding; Phosphoprotein;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1 1141 cGMP-inhibited 3',5'-cyclic
phosphodiesterase A.
/FTId=PRO_0000198799.
TRANSMEM 61 81 Helical. {ECO:0000255}.
TRANSMEM 130 150 Helical. {ECO:0000255}.
TRANSMEM 160 180 Helical. {ECO:0000255}.
TRANSMEM 185 205 Helical. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
TRANSMEM 232 252 Helical. {ECO:0000255}.
REGION 728 1086 Catalytic. {ECO:0000250}.
COMPBIAS 95 98 Poly-Ala.
COMPBIAS 99 102 Poly-Glu.
COMPBIAS 288 291 Poly-Arg.
COMPBIAS 440 445 Poly-Thr.
COMPBIAS 870 873 Poly-Ala.
COMPBIAS 1040 1045 Poly-Glu.
COMPBIAS 1121 1125 Poly-Glu.
ACT_SITE 752 752 Proton donor. {ECO:0000250}.
METAL 756 756 Divalent metal cation 1. {ECO:0000250}.
METAL 836 836 Divalent metal cation 1. {ECO:0000250}.
METAL 837 837 Divalent metal cation 1. {ECO:0000250}.
METAL 837 837 Divalent metal cation 2. {ECO:0000250}.
METAL 950 950 Divalent metal cation 1. {ECO:0000250}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 520 520 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:23186163}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0X4}.
MOD_RES 1033 1033 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0X4}.
MOD_RES 1036 1036 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z0X4}.
CROSSLNK 1120 1120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 12 12 D -> N (in dbSNP:rs12305038).
{ECO:0000269|PubMed:8695850}.
/FTId=VAR_059543.
VARIANT 445 445 T -> A (in HTNB; gain of function
mutation with increased cAMP-hydrolytic
activity; dbSNP:rs794726865).
{ECO:0000269|PubMed:25961942}.
/FTId=VAR_073869.
VARIANT 445 445 T -> N (in HTNB; gain of function
mutation with increased cAMP-hydrolytic
activity; dbSNP:rs794726864).
{ECO:0000269|PubMed:25961942}.
/FTId=VAR_073870.
VARIANT 445 445 T -> S (in HTNB; gain of function
mutation with increased cAMP-hydrolytic
activity). {ECO:0000269|PubMed:25961942}.
/FTId=VAR_073871.
VARIANT 447 447 A -> T (in HTNB; gain of function
mutation with increased cAMP-hydrolytic
activity; dbSNP:rs794726866).
{ECO:0000269|PubMed:25961942}.
/FTId=VAR_073872.
VARIANT 447 447 A -> V (in HTNB; gain of function
mutationwith increased cAMP-hydrolytic
activity; dbSNP:rs794726867).
{ECO:0000269|PubMed:25961942}.
/FTId=VAR_073873.
VARIANT 449 449 G -> V (in HTNB; gain of function
mutation with increased cAMP-hydrolytic
activity; dbSNP:rs794726868).
{ECO:0000269|PubMed:25961942}.
/FTId=VAR_073874.
CONFLICT 69 69 S -> C (in Ref. 3; AAB18673).
{ECO:0000305}.
CONFLICT 110 110 G -> A (in Ref. 3; AAB18673).
{ECO:0000305}.
CONFLICT 354 371 HGLITDLLADPSLPPNVC -> TASLPTSWQTLLFHQTCA
(in Ref. 3 and 4; CAA06304).
{ECO:0000305}.
SEQUENCE 1141 AA; 124979 MW; E69504130F39EFEA CRC64;
MAVPGDAARV RDKPVHSGVS QAPTAGRDCH HRADPASPRD SGCRGCWGDL VLQPLRSSRK
LSSALCAGSL SFLLALLVRL VRGEVGCDLE QCKEAAAAEE EEAAPGAEGG VFPGPRGGAP
GGGARLSPWL QPSALLFSLL CAFFWMGLYL LRAGVRLPLA VALLAACCGG EALVQIGLGV
GEDHLLSLPA AGVVLSCLAA ATWLVLRLRL GVLMIALTSA VRTVSLISLE RFKVAWRPYL
AYLAGVLGIL LARYVEQILP QSAEAAPREH LGSQLIAGTK EDIPVFKRRR RSSSVVSAEM
SGCSSKSHRR TSLPCIPREQ LMGHSEWDHK RGPRGSQSSG TSITVDIAVM GEAHGLITDL
LADPSLPPNV CTSLRAVSNL LSTQLTFQAI HKPRVNPVTS LSENYTCSDS EESSEKDKLA
IPKRLRRSLP PGLLRRVSST WTTTTSATGL PTLEPAPVRR DRSTSIKLQE APSSSPDSWN
NPVMMTLTKS RSFTSSYAIS AANHVKAKKQ SRPGALAKIS PLSSPCSSPL QGTPASSLVS
KISAVQFPES ADTTAKQSLG SHRALTYTQS APDLSPQILT PPVICSSCGR PYSQGNPADE
PLERSGVATR TPSRTDDTAQ VTSDYETNNN SDSSDIVQNE DETECLREPL RKASACSTYA
PETMMFLDKP ILAPEPLVMD NLDSIMEQLN TWNFPIFDLV ENIGRKCGRI LSQVSYRLFE
DMGLFEAFKI PIREFMNYFH ALEIGYRDIP YHNRIHATDV LHAVWYLTTQ PIPGLSTVIN
DHGSTSDSDS DSGFTHGHMG YVFSKTYNVT DDKYGCLSGN IPALELMALY VAAAMHDYDH
PGRTNAFLVA TSAPQAVLYN DRSVLENHHA AAAWNLFMSR PEYNFLINLD HVEFKHFRFL
VIEAILATDL KKHFDFVAKF NGKVNDDVGI DWTNENDRLL VCQMCIKLAD INGPAKCKEL
HLQWTDGIVN EFYEQGDEEA SLGLPISPFM DRSAPQLANL QESFISHIVG PLCNSYDSAG
LMPGKWVEDS DESGDTDDPE EEEEEAPAPN EEETCENNES PKKKTFKRRK IYCQITQHLL
QNHKMWKKVI EEEQRLAGIE NQSLDQTPQS HSSEQIQAIK EEEEEKGKPR GEEIPTQKPD
Q


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