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Q14432

- PDE3A_HUMAN

UniProt

Q14432 - PDE3A_HUMAN

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Protein

cGMP-inhibited 3',5'-cyclic phosphodiesterase A

Gene

PDE3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes.By similarity

Catalytic activityi

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.

Cofactori

a divalent metal cationBy similarityNote: 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.By similarity

Enzyme regulationi

Inhibited by cGMP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei752 – 7521Proton donorBy similarity
Metal bindingi756 – 7561Divalent metal cation 1By similarity
Metal bindingi836 – 8361Divalent metal cation 1By similarity
Metal bindingi837 – 8371Divalent metal cation 1By similarity
Metal bindingi837 – 8371Divalent metal cation 2By similarity
Metal bindingi950 – 9501Divalent metal cation 1By similarity

GO - Molecular functioni

  1. 3',5'-cyclic-AMP phosphodiesterase activity Source: Ensembl
  2. cAMP binding Source: Ensembl
  3. cGMP-inhibited cyclic-nucleotide phosphodiesterase activity Source: ProtInc
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cAMP catabolic process Source: UniProtKB
  3. cAMP-mediated signaling Source: UniProtKB
  4. cellular response to cGMP Source: UniProtKB
  5. cellular response to transforming growth factor beta stimulus Source: UniProtKB
  6. cGMP-mediated signaling Source: UniProtKB
  7. diterpenoid metabolic process Source: Ensembl
  8. lipid metabolic process Source: ProtInc
  9. negative regulation of apoptotic process Source: Ensembl
  10. negative regulation of vascular permeability Source: UniProtKB
  11. oocyte maturation Source: Ensembl
  12. positive regulation of oocyte development Source: Ensembl
  13. positive regulation of vascular permeability Source: UniProtKB
  14. regulation of meiosis Source: Ensembl
  15. response to cAMP Source: Ensembl
  16. response to drug Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, cGMP, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_19327. G alpha (s) signalling events.
REACT_23767. cGMP effects.
SABIO-RKQ14432.

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-inhibited 3',5'-cyclic phosphodiesterase A (EC:3.1.4.17)
Alternative name(s):
Cyclic GMP-inhibited phosphodiesterase A
Short name:
CGI-PDE A
Gene namesi
Name:PDE3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:8778. PDE3A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei61 – 8121HelicalSequence AnalysisAdd
BLAST
Transmembranei130 – 15021HelicalSequence AnalysisAdd
BLAST
Transmembranei160 – 18021HelicalSequence AnalysisAdd
BLAST
Transmembranei185 – 20521HelicalSequence AnalysisAdd
BLAST
Transmembranei210 – 23021HelicalSequence AnalysisAdd
BLAST
Transmembranei232 – 25221HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33126.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11411141cGMP-inhibited 3',5'-cyclic phosphodiesterase APRO_0000198799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei312 – 3121Phosphoserine1 Publication
Modified residuei520 – 5201Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14432.
PaxDbiQ14432.
PRIDEiQ14432.

PTM databases

PhosphoSiteiQ14432.

Expressioni

Gene expression databases

BgeeiQ14432.
CleanExiHS_PDE3A.
GenevestigatoriQ14432.

Organism-specific databases

HPAiHPA014492.

Interactioni

Protein-protein interaction databases

BioGridi111165. 13 interactions.
DIPiDIP-42197N.
IntActiQ14432. 2 interactions.
MINTiMINT-3295914.
STRINGi9606.ENSP00000351957.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LRCmodel-A812-1017[»]
ProteinModelPortaliQ14432.
SMRiQ14432. Positions 677-1087.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni728 – 1086359CatalyticBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi95 – 984Poly-Ala
Compositional biasi99 – 1024Poly-Glu
Compositional biasi288 – 2914Poly-Arg
Compositional biasi440 – 4456Poly-Thr
Compositional biasi870 – 8734Poly-Ala
Compositional biasi1040 – 10456Poly-Glu
Compositional biasi1121 – 11255Poly-Glu

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG145074.
GeneTreeiENSGT00760000119066.
HOGENOMiHOG000060144.
HOVERGENiHBG053541.
KOiK13296.
OMAiPETMMFL.
OrthoDBiEOG7KDF95.
PhylomeDBiQ14432.
TreeFamiTF329631.

Family and domain databases

Gene3Di1.10.1300.10. 2 hits.
InterProiIPR003607. HD/PDEase_dom.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14432-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVPGDAARV RDKPVHSGVS QAPTAGRDCH HRADPASPRD SGCRGCWGDL
60 70 80 90 100
VLQPLRSSRK LSSALCAGSL SFLLALLVRL VRGEVGCDLE QCKEAAAAEE
110 120 130 140 150
EEAAPGAEGG VFPGPRGGAP GGGARLSPWL QPSALLFSLL CAFFWMGLYL
160 170 180 190 200
LRAGVRLPLA VALLAACCGG EALVQIGLGV GEDHLLSLPA AGVVLSCLAA
210 220 230 240 250
ATWLVLRLRL GVLMIALTSA VRTVSLISLE RFKVAWRPYL AYLAGVLGIL
260 270 280 290 300
LARYVEQILP QSAEAAPREH LGSQLIAGTK EDIPVFKRRR RSSSVVSAEM
310 320 330 340 350
SGCSSKSHRR TSLPCIPREQ LMGHSEWDHK RGPRGSQSSG TSITVDIAVM
360 370 380 390 400
GEAHGLITDL LADPSLPPNV CTSLRAVSNL LSTQLTFQAI HKPRVNPVTS
410 420 430 440 450
LSENYTCSDS EESSEKDKLA IPKRLRRSLP PGLLRRVSST WTTTTSATGL
460 470 480 490 500
PTLEPAPVRR DRSTSIKLQE APSSSPDSWN NPVMMTLTKS RSFTSSYAIS
510 520 530 540 550
AANHVKAKKQ SRPGALAKIS PLSSPCSSPL QGTPASSLVS KISAVQFPES
560 570 580 590 600
ADTTAKQSLG SHRALTYTQS APDLSPQILT PPVICSSCGR PYSQGNPADE
610 620 630 640 650
PLERSGVATR TPSRTDDTAQ VTSDYETNNN SDSSDIVQNE DETECLREPL
660 670 680 690 700
RKASACSTYA PETMMFLDKP ILAPEPLVMD NLDSIMEQLN TWNFPIFDLV
710 720 730 740 750
ENIGRKCGRI LSQVSYRLFE DMGLFEAFKI PIREFMNYFH ALEIGYRDIP
760 770 780 790 800
YHNRIHATDV LHAVWYLTTQ PIPGLSTVIN DHGSTSDSDS DSGFTHGHMG
810 820 830 840 850
YVFSKTYNVT DDKYGCLSGN IPALELMALY VAAAMHDYDH PGRTNAFLVA
860 870 880 890 900
TSAPQAVLYN DRSVLENHHA AAAWNLFMSR PEYNFLINLD HVEFKHFRFL
910 920 930 940 950
VIEAILATDL KKHFDFVAKF NGKVNDDVGI DWTNENDRLL VCQMCIKLAD
960 970 980 990 1000
INGPAKCKEL HLQWTDGIVN EFYEQGDEEA SLGLPISPFM DRSAPQLANL
1010 1020 1030 1040 1050
QESFISHIVG PLCNSYDSAG LMPGKWVEDS DESGDTDDPE EEEEEAPAPN
1060 1070 1080 1090 1100
EEETCENNES PKKKTFKRRK IYCQITQHLL QNHKMWKKVI EEEQRLAGIE
1110 1120 1130 1140
NQSLDQTPQS HSSEQIQAIK EEEEEKGKPR GEEIPTQKPD Q
Length:1,141
Mass (Da):124,979
Last modified:May 10, 2004 - v3
Checksum:iE69504130F39EFEA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691S → C in AAB18673. (PubMed:8695850)Curated
Sequence conflicti110 – 1101G → A in AAB18673. (PubMed:8695850)Curated
Sequence conflicti354 – 37118HGLIT…PPNVC → TASLPTSWQTLLFHQTCA(PubMed:8695850)CuratedAdd
BLAST
Sequence conflicti354 – 37118HGLIT…PPNVC → TASLPTSWQTLLFHQTCA(PubMed:10421499)CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121D → N.1 Publication
Corresponds to variant rs12305038 [ dbSNP | Ensembl ].
VAR_059543

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91667 mRNA. Translation: AAA35912.2.
U36798 mRNA. Translation: AAB18673.1.
AJ005036 mRNA. Translation: CAA06304.1.
BC117369 mRNA. Translation: AAI17370.1.
BC117371 mRNA. Translation: AAI17372.1.
CCDSiCCDS31754.1.
PIRiA44093.
RefSeqiNP_000912.3. NM_000921.4.
UniGeneiHs.386791.
Hs.737522.

Genome annotation databases

EnsembliENST00000359062; ENSP00000351957; ENSG00000172572.
GeneIDi5139.
KEGGihsa:5139.
UCSCiuc001reh.2. human.

Polymorphism databases

DMDMi47117888.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

PDE3 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91667 mRNA. Translation: AAA35912.2 .
U36798 mRNA. Translation: AAB18673.1 .
AJ005036 mRNA. Translation: CAA06304.1 .
BC117369 mRNA. Translation: AAI17370.1 .
BC117371 mRNA. Translation: AAI17372.1 .
CCDSi CCDS31754.1.
PIRi A44093.
RefSeqi NP_000912.3. NM_000921.4.
UniGenei Hs.386791.
Hs.737522.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LRC model - A 812-1017 [» ]
ProteinModelPortali Q14432.
SMRi Q14432. Positions 677-1087.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111165. 13 interactions.
DIPi DIP-42197N.
IntActi Q14432. 2 interactions.
MINTi MINT-3295914.
STRINGi 9606.ENSP00000351957.

Chemistry

BindingDBi Q14432.
ChEMBLi CHEMBL241.
DrugBanki DB01223. Aminophylline.
DB01427. Amrinone.
DB00261. Anagrelide.
DB00201. Caffeine.
DB01166. Cilostazol.
DB04880. Enoximone.
DB05266. Ibudilast.
DB00922. Levosimendan.
DB00235. Milrinone.
DB01303. Oxtriphylline.
DB00277. Theophylline.
DB08811. Tofisopam.
GuidetoPHARMACOLOGYi 1298.

PTM databases

PhosphoSitei Q14432.

Polymorphism databases

DMDMi 47117888.

Proteomic databases

MaxQBi Q14432.
PaxDbi Q14432.
PRIDEi Q14432.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359062 ; ENSP00000351957 ; ENSG00000172572 .
GeneIDi 5139.
KEGGi hsa:5139.
UCSCi uc001reh.2. human.

Organism-specific databases

CTDi 5139.
GeneCardsi GC12P020422.
HGNCi HGNC:8778. PDE3A.
HPAi HPA014492.
MIMi 123805. gene.
neXtProti NX_Q14432.
PharmGKBi PA33126.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG145074.
GeneTreei ENSGT00760000119066.
HOGENOMi HOG000060144.
HOVERGENi HBG053541.
KOi K13296.
OMAi PETMMFL.
OrthoDBi EOG7KDF95.
PhylomeDBi Q14432.
TreeFami TF329631.

Enzyme and pathway databases

Reactomei REACT_19327. G alpha (s) signalling events.
REACT_23767. cGMP effects.
SABIO-RK Q14432.

Miscellaneous databases

ChiTaRSi PDE3A. human.
GenomeRNAii 5139.
NextBioi 19816.
PROi Q14432.
SOURCEi Search...

Gene expression databases

Bgeei Q14432.
CleanExi HS_PDE3A.
Genevestigatori Q14432.

Family and domain databases

Gene3Di 1.10.1300.10. 2 hits.
InterProi IPR003607. HD/PDEase_dom.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF00233. PDEase_I. 1 hit.
[Graphical view ]
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase."
    Meacci E., Taira M., Moos M. Jr., Smith C.J., Movsesian M.A., Degerman E., Belfrage P., Manganiello V.
    Proc. Natl. Acad. Sci. U.S.A. 89:3721-3725(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Myocardium.
  2. Liu H., Manganiello V.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 12; 63-64 AND 354-371.
  3. "Human platelet cGI-PDE: expression in yeast and localization of the catalytic domain by deletion mutagenesis."
    Cheung P.P., Xu H., McLaughlin M.M., Ghazaleh F.A., Livi G.P., Colman R.W.
    Blood 88:1321-1329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-12.
    Tissue: Blood.
  4. "Molecular biological characterization of phosphodiesterase 3A from human corpus cavernosum."
    Kuthe A., Eckel H., Stief C.G., Uckert S., Forssmann W.-G., Jonas U., Maegert H.-J.
    Chem. Biol. Interact. 119:593-598(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Penis.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  6. "Single-step affinity purification, partial structure and properties of human platelet cGMP inhibited cAMP phosphodiesterase."
    Degerman E., Moos M. Jr., Rascon A., Vasta V., Meacci E., Smith C.J., Lindgren S., Andersson K.-E., Belfrage P., Manganiello V.
    Biochim. Biophys. Acta 1205:189-198(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDE3A_HUMAN
AccessioniPrimary (citable) accession number: Q14432
Secondary accession number(s): O60865, Q13348, Q17RD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 10, 2004
Last modified: November 26, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3