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Q8CG03 (PDE5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cGMP-specific 3',5'-cyclic phosphodiesterase

EC=3.1.4.35
Alternative name(s):
cGMP-binding cGMP-specific phosphodiesterase
Short name=CGB-PDE
Gene names
Name:Pde5a
Synonyms:Pde5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length865 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Catalytic activity

Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.

Cofactor

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.

Pathway

Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.

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.

Post-translational modification

Phosphorylation is regulated by binding of cGMP to the two allosteric sites By similarity. Phosphorylation by PRKG1 leads to its activation By similarity.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Contains 2 GAF domains.

Ontologies

Keywords
   DomainRepeat
   LigandcGMP
cGMP-binding
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcGMP catabolic process

Inferred from direct assay PubMed 12554648. Source: MGI

cGMP metabolic process

Inferred from mutant phenotype PubMed 19474061PubMed 20511540. Source: MGI

negative regulation of T cell proliferation

Inferred from mutant phenotype PubMed 17101732. Source: MGI

negative regulation of cardiac muscle contraction

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

positive regulation of G-protein coupled receptor protein signaling pathway

Inferred by curator PubMed 19127022. Source: BHF-UCL

positive regulation of MAP kinase activity

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

positive regulation of cardiac muscle hypertrophy

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

positive regulation of oocyte development

Inferred from mutant phenotype PubMed 19474061. Source: MGI

relaxation of cardiac muscle

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

signal transduction

Inferred from electronic annotation. Source: InterPro

   Molecular_function3',5'-cyclic-GMP phosphodiesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3',5'-cyclic-nucleotide phosphodiesterase activity

Inferred from mutant phenotype PubMed 19474061. Source: MGI

cGMP binding

Inferred from direct assay PubMed 12554648PubMed 18534985. Source: MGI

cyclic-nucleotide phosphodiesterase activity

Inferred from direct assay PubMed 12554648. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 865865cGMP-specific 3',5'-cyclic phosphodiesterase
PRO_0000198824

Regions

Domain154 – 304151GAF 1
Domain336 – 493158GAF 2
Region578 – 843266Catalytic By similarity

Sites

Active site6031Proton donor By similarity
Metal binding6071Divalent metal cation 1 By similarity
Metal binding6431Divalent metal cation 1 By similarity
Metal binding6441Divalent metal cation 1 By similarity
Metal binding6441Divalent metal cation 2 By similarity
Metal binding7541Divalent metal cation 1 By similarity
Binding site8071cGMP By similarity

Amino acid modifications

Modified residue921Phosphoserine Potential

Experimental info

Sequence conflict1761S → T in AAN17330. Ref.1

Secondary structure

............................ 865
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8CG03 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: BADD21CC6B62045E

FASTA86598,407
        10         20         30         40         50         60 
MERAGPNSVR SQQQRDPDWV EAWLDDHRDF TFSYFIRKAT RDMVNAWFSE RVHNIPVCKE 

        70         80         90        100        110        120 
GIRAHTESCS CSLQQSPHAD NTTPGAPARK ISASEFDRPL RPIVVKDSEG TVSFLSDSGK 

       130        140        150        160        170        180 
KEQMPLTPPR FDSDEGDQCS RLLELVKDIS SHLDVTALCH KIFLHIHGLI SADRYSLFLV 

       190        200        210        220        230        240 
CEDSSKDKFL ISRLFDVAEG STLEEASNNC IRLEWNKGIV GHVAAFGEPL NIKDAYEDPR 

       250        260        270        280        290        300 
FNAEVDQITG YKTQSILCMP IKNHREEVVG VAQAINKKSG NGGTFTEKDE KDFAAYLAFC 

       310        320        330        340        350        360 
GIVLHNAQLY ETSLLENKRN QVLLDLASLI FEEQQSLEVI LKKIAATIIS FMQVQKCTIF 

       370        380        390        400        410        420 
IVDEDCPDSF SRVFHMECEE VGKPSDPLTR EQDANKINYM YAQYVKNTME PLNIPDVTKD 

       430        440        450        460        470        480 
KRFPWTNENM GHVNTPCIGS LLCTPIKNGK KNKVIGVCQL VNKMEENTGK IKAFNQNDEQ 

       490        500        510        520        530        540 
FLEAFVIFCG LGIQNTQMYE AVERAMAKQM VTLEVLSYHA SAAEEETREL QALSAAVVPS 

       550        560        570        580        590        600 
AQTLKITDFS FSDFELSDLE TALCTIRMFT DLNLVQNFQM KHEVLCRWIL SVKKNYRKNV 

       610        620        630        640        650        660 
AYHNWRHAFN TAQCMFAALK AGKIQNKLTD LETLALLIAA LSHDLDHRGV NNSYIQRSEH 

       670        680        690        700        710        720 
PLAQLYCHSI MEHHHFDQCL MILNSPGNQI LSGLSIDEYK TTLKIIKQAI LATDLALYIK 

       730        740        750        760        770        780 
RRGEFFELIR KNQFSFEDPL QKELFLAMLM TACDLSAITK PWPIQQRIAE LVAAEFFDQG 

       790        800        810        820        830        840 
DRERKELNME PADLMNREKK NKIPSMQVGF IDAICLQLYE ALTHVSEDCL PLLDGCRKNR 

       850        860 
QKWQALAEQQ EKMLLNGESS QGKRD 

« Hide

References

« Hide 'large scale' references
[1]Burns F., Sonnenburg W.K., Rybalkin S.D., Beavo J.A.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF541937 mRNA. Translation: AAN17330.1.
CH466532 Genomic DNA. Translation: EDL12317.1.
BC119137 mRNA. Translation: AAI19138.1.
BC120486 mRNA. Translation: AAI20487.1.
CCDSCCDS17812.1.
RefSeqNP_700471.2. NM_153422.2.
UniGeneMm.134911.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K31NMR-A154-320[»]
ProteinModelPortalQ8CG03.
SMRQ8CG03. Positions 89-850.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8CG03. 1 interaction.
MINTMINT-4106875.

PTM databases

PhosphoSiteQ8CG03.

Proteomic databases

MaxQBQ8CG03.
PaxDbQ8CG03.
PRIDEQ8CG03.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066728; ENSMUSP00000069011; ENSMUSG00000053965.
GeneID242202.
KEGGmmu:242202.
UCSCuc008ret.2. mouse.

Organism-specific databases

CTD8654.
MGIMGI:2651499. Pde5a.

Phylogenomic databases

eggNOGNOG270709.
GeneTreeENSGT00750000117528.
HOGENOMHOG000007068.
HOVERGENHBG101207.
InParanoidQ0VBW0.
KOK13762.
OMAREHDANK.
OrthoDBEOG7RRF69.
TreeFamTF316499.

Enzyme and pathway databases

UniPathwayUPA00763; UER00748.

Gene expression databases

BgeeQ8CG03.
CleanExMM_PDE5A.
GenevestigatorQ8CG03.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMSSF55781. SSF55781. 2 hits.
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDE5A. mouse.
EvolutionaryTraceQ8CG03.
NextBio385258.
PROQ8CG03.
SOURCESearch...

Entry information

Entry namePDE5A_MOUSE
AccessionPrimary (citable) accession number: Q8CG03
Secondary accession number(s): Q0VBW0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot