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O54735 (PDE5A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length833 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

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
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandcGMP
cGMP-binding
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcGMP catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

nervous system development

Inferred from expression pattern Ref.1. Source: RGD

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 19474186. Source: RGD

positive regulation of chronic inflammatory response

Inferred from mutant phenotype PubMed 19129291. Source: RGD

positive regulation of vasoconstriction

Inferred from mutant phenotype PubMed 19542492. Source: RGD

regulation of the force of heart contraction

Inferred from mutant phenotype PubMed 17606845. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 12466227. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 17141339. Source: RGD

response to testosterone

Inferred from expression pattern PubMed 17138653. Source: RGD

short-term memory

Inferred from mutant phenotype PubMed 19129291. Source: RGD

signal transduction

Inferred from electronic annotation. Source: InterPro

vasodilation

Inferred from expression pattern PubMed 16545481. Source: RGD

   Cellular_componentcytosol

Inferred from direct assay PubMed 17141339. Source: RGD

   Molecular_function3',5'-cyclic-GMP phosphodiesterase activity

Inferred from direct assay PubMed 15100365PubMed 15623434. Source: RGD

cGMP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]
Isoform PDE5A2 (identifier: O54735-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform PDE5A1 (identifier: O54735-2)

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 833833cGMP-specific 3',5'-cyclic phosphodiesterase
PRO_0000198825

Regions

Domain122 – 272151GAF 1
Domain304 – 461158GAF 2
Region546 – 811266Catalytic By similarity

Sites

Active site5711Proton donor By similarity
Metal binding5751Divalent metal cation 1 By similarity
Metal binding6111Divalent metal cation 1 By similarity
Metal binding6121Divalent metal cation 1 By similarity
Metal binding6121Divalent metal cation 2 By similarity
Metal binding7221Divalent metal cation 1 By similarity
Binding site7751cGMP By similarity

Amino acid modifications

Modified residue601Phosphoserine Potential

Sequences

Sequence LengthMass (Da)Tools
Isoform PDE5A2 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 712DC159C80CB09D

FASTA83394,556
        10         20         30         40         50         60 
MLPFGDKTRD MVNAWFSERV HNIPVCKEGI RAHTESCSCS LPQSPHADNT TPGAPARKIS 

        70         80         90        100        110        120 
ASEFDRPLRP IVVKDSEGTV SFLSDSGKKE QMPLTSPRFD SDEGDQCSRL LELVKDISSH 

       130        140        150        160        170        180 
LDVTALCHKI FLHIHGLISA DRYSLFLVCE DSSKDKFLVS RLFDVAEGST LEEASNNCIR 

       190        200        210        220        230        240 
LEWNKGIVGH VAAFGEPLNI KDAYEDPRFN AEVDQITGYK TQSILCMPIK NHREEVVGVA 

       250        260        270        280        290        300 
QAINKKSGNG GTFTEKDEKD FAAYLAFCGI VLHNAQLYET SLLENKRNQV LLDLASLIFE 

       310        320        330        340        350        360 
EQQSLEVILK KIAATIISFM QVQKCTIFIV DEDCPDSFSR VFQMEWEEVG KSSEPLTREH 

       370        380        390        400        410        420 
DANKINYMYA QYVKNTMEPL NIPDVTKDNR FPWTNENMGH INTHCIRSLL CTPIKNGKKN 

       430        440        450        460        470        480 
KVIGVCQLVN KMEEKTGKIK AFNQNDEQFL EAFVIFCGLG IQNTQMYEAV ERAMAKQMVT 

       490        500        510        520        530        540 
LEVLSYHASA AEEETRELQA LAAAVVPSAQ TLKITDFSFS DFELSDLETA LCTIRMFTDL 

       550        560        570        580        590        600 
NLVQNFQMKH EVLCRWILSV KKNYRKNVAY HNWRHAFNTA QCMFAALKAG KIQNKLTDLE 

       610        620        630        640        650        660 
TLALLIAALS HDLDHRGVNN SYIQRSEHPL AQLYCHSTME HHHFDQCLMV LNSPGNQILS 

       670        680        690        700        710        720 
GLSIEEYKTT LKIIKQAILA TDLALYIKRR GEFFELIRKN EFSFEDPLQK ELFLAMLMTA 

       730        740        750        760        770        780 
CDLSAITKPW PIQQRIAELV AAEFFDQGDR ERKELNMEPA DLMNREKKNK IPSMQVGFID 

       790        800        810        820        830 
AICLQLYEAL THVSEDCLPL LDGCRKNRQK WQALADQQEK TLLNGESGQA KRD 

« Hide

Isoform PDE5A1 (Sequence not available).

References

[1]"Expression of rat cGMP-binding cGMP-specific phosphodiesterase mRNA in Purkinje cell layers during postnatal neuronal development."
Kotera J., Yanaka N., Fujishige K., Imai Y., Akatsuka H., Ishizuka T., Kawashima K., Omori K.
Eur. J. Biochem. 249:434-442(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89093 mRNA. Translation: BAA23672.1.
RefSeqNP_598268.1. NM_133584.1. [O54735-1]
UniGeneRn.10861.
Rn.133138.

3D structure databases

ProteinModelPortalO54735.
SMRO54735. Positions 122-269, 493-818.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBO54735.
ChEMBLCHEMBL4567.

PTM databases

PhosphoSiteO54735.

Proteomic databases

PaxDbO54735.
PRIDEO54735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID171115.
KEGGrno:171115.
UCSCRGD:620995. rat. [O54735-1]

Organism-specific databases

CTD8654.
RGD620995. Pde5a.

Phylogenomic databases

eggNOGNOG270709.
HOGENOMHOG000007068.
HOVERGENHBG101207.
InParanoidO54735.
KOK13762.
PhylomeDBO54735.

Enzyme and pathway databases

UniPathwayUPA00763; UER00748.

Gene expression databases

GenevestigatorO54735.

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

NextBio621836.
PROO54735.

Entry information

Entry namePDE5A_RAT
AccessionPrimary (citable) accession number: O54735
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: June 11, 2014
This is version 105 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways