SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14432

- PDE3A_HUMAN

UniProt

Q14432 - PDE3A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 donor By similarity
Metal bindingi756 – 7561Divalent metal cation 1 By similarity
Metal bindingi836 – 8361Divalent metal cation 1 By similarity
Metal bindingi837 – 8371Divalent metal cation 1 By similarity
Metal bindingi837 – 8371Divalent metal cation 2 By similarity
Metal bindingi950 – 9501Divalent metal cation 1 By 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. cGMP-mediated signaling Source: UniProtKB
  5. cellular response to cGMP Source: UniProtKB
  6. cellular response to transforming growth factor beta stimulus 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 – 8121Helical; Reviewed prediction
Add
BLAST
Transmembranei130 – 15021Helical; Reviewed prediction
Add
BLAST
Transmembranei160 – 18021Helical; Reviewed prediction
Add
BLAST
Transmembranei185 – 20521Helical; Reviewed prediction
Add
BLAST
Transmembranei210 – 23021Helical; Reviewed prediction
Add
BLAST
Transmembranei232 – 25221Helical; Reviewed prediction
Add
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 A
PRO_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

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi815 – 8173
Helixi823 – 83513
Turni836 – 8394
Helixi845 – 8506
Helixi854 – 8585
Turni859 – 8613
Helixi864 – 87613
Turni877 – 8793
Turni885 – 8884
Helixi891 – 90616
Helixi910 – 9123
Helixi913 – 9186
Helixi939 – 95012
Helixi953 – 9553
Helixi958 – 98124
Helixi997 – 100711
Helixi1009 – 10168

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LRCmodel-A812-1017[»]
ProteinModelPortaliQ14432.
SMRiQ14432. Positions 677-1087.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni728 – 1086359Catalytic By similarity
Add
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.
HOGENOMiHOG000060144.
HOVERGENiHBG053541.
InParanoidiQ14432.
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

MAVPGDAARV RDKPVHSGVS QAPTAGRDCH HRADPASPRD SGCRGCWGDL     50
VLQPLRSSRK LSSALCAGSL SFLLALLVRL VRGEVGCDLE QCKEAAAAEE 100
EEAAPGAEGG VFPGPRGGAP GGGARLSPWL QPSALLFSLL CAFFWMGLYL 150
LRAGVRLPLA VALLAACCGG EALVQIGLGV GEDHLLSLPA AGVVLSCLAA 200
ATWLVLRLRL GVLMIALTSA VRTVSLISLE RFKVAWRPYL AYLAGVLGIL 250
LARYVEQILP QSAEAAPREH LGSQLIAGTK EDIPVFKRRR RSSSVVSAEM 300
SGCSSKSHRR TSLPCIPREQ LMGHSEWDHK RGPRGSQSSG TSITVDIAVM 350
GEAHGLITDL LADPSLPPNV CTSLRAVSNL LSTQLTFQAI HKPRVNPVTS 400
LSENYTCSDS EESSEKDKLA IPKRLRRSLP PGLLRRVSST WTTTTSATGL 450
PTLEPAPVRR DRSTSIKLQE APSSSPDSWN NPVMMTLTKS RSFTSSYAIS 500
AANHVKAKKQ SRPGALAKIS PLSSPCSSPL QGTPASSLVS KISAVQFPES 550
ADTTAKQSLG SHRALTYTQS APDLSPQILT PPVICSSCGR PYSQGNPADE 600
PLERSGVATR TPSRTDDTAQ VTSDYETNNN SDSSDIVQNE DETECLREPL 650
RKASACSTYA PETMMFLDKP ILAPEPLVMD NLDSIMEQLN TWNFPIFDLV 700
ENIGRKCGRI LSQVSYRLFE DMGLFEAFKI PIREFMNYFH ALEIGYRDIP 750
YHNRIHATDV LHAVWYLTTQ PIPGLSTVIN DHGSTSDSDS DSGFTHGHMG 800
YVFSKTYNVT DDKYGCLSGN IPALELMALY VAAAMHDYDH PGRTNAFLVA 850
TSAPQAVLYN DRSVLENHHA AAAWNLFMSR PEYNFLINLD HVEFKHFRFL 900
VIEAILATDL KKHFDFVAKF NGKVNDDVGI DWTNENDRLL VCQMCIKLAD 950
INGPAKCKEL HLQWTDGIVN EFYEQGDEEA SLGLPISPFM DRSAPQLANL 1000
QESFISHIVG PLCNSYDSAG LMPGKWVEDS DESGDTDDPE EEEEEAPAPN 1050
EEETCENNES PKKKTFKRRK IYCQITQHLL QNHKMWKKVI EEEQRLAGIE 1100
NQSLDQTPQS HSSEQIQAIK EEEEEKGKPR GEEIPTQKPD Q 1141
Length:1,141
Mass (Da):124,979
Last modified:May 10, 2004 - v3
Checksum:iE69504130F39EFEA
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691S → C in AAB18673. 1 Publication
Sequence conflicti110 – 1101G → A in AAB18673. 1 Publication
Sequence conflicti354 – 37118HGLIT…PPNVC → TASLPTSWQTLLFHQTCA1 Publication
Add
BLAST
Sequence conflicti354 – 37118HGLIT…PPNVC → TASLPTSWQTLLFHQTCA1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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 CHEMBL2095153.
DrugBanki DB01223. Aminophylline.
DB01427. Amrinone.
DB00261. Anagrelide.
DB01166. Cilostazol.
DB04880. Enoximone.
DB00235. Milrinone.
DB00277. Theophylline.
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.
HOGENOMi HOG000060144.
HOVERGENi HBG053541.
InParanoidi Q14432.
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: September 3, 2014
This is version 136 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

Similar proteinsi