cGMP-specific 3',5'-cyclic phosphodiesterase

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Regions

Sites

Amino acid modifications

Preferred order of sections

Molecule processing

Regions

Sites

Amino acid modifications

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

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O54735 (PDE5A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Sequence length	833 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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.

Keywords
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Metal-binding Nucleotide-binding cGMP cGMP-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nervous system development Inferred from expression pattern Ref.1. Source: RGD positive regulation of apoptotic process Inferred from mutant phenotype. Source: RGD positive regulation of chronic inflammatory response Inferred from mutant phenotype. Source: RGD positive regulation of vasoconstriction Inferred from mutant phenotype. Source: RGD regulation of the force of heart contraction Inferred from mutant phenotype. Source: RGD response to hypoxia Inferred from expression pattern. Source: RGD response to lipopolysaccharide Inferred from expression pattern. Source: RGD response to testosterone stimulus Inferred from expression pattern. Source: RGD short-term memory Inferred from mutant phenotype. Source: RGD signal transduction Inferred from electronic annotation. Source: InterPro vasodilation Inferred from expression pattern. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD
Molecular function	3',5'-cyclic-GMP phosphodiesterase activity Inferred from direct assay. Source: RGD cGMP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 833

833

cGMP-specific 3',5'-cyclic phosphodiesterase

PRO_0000198825

Domain

122 – 272

151

GAF 1

Domain

304 – 461

158

GAF 2

Region

546 – 811

266

Catalytic By similarity

Active site

571

Proton donor By similarity

Metal binding

575

Divalent metal cation 1 By similarity

Metal binding

611

Divalent metal cation 1 By similarity

Metal binding

612

Divalent metal cation 1 By similarity

Metal binding

612

Divalent metal cation 2 By similarity

Metal binding

722

Divalent metal cation 1 By similarity

Binding site

775

cGMP By similarity

Modified residue

Phosphoserine Potential

Sequence

Length

Mass (Da)

Tools

Isoform PDE5A2 [UniParc].

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

FASTA

833

94,556

        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).

–

[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: 9370351] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Lung.
+	Additional computationally mapped references.

Sequence databases
EMBL GenBank DDBJ	D89093 mRNA. Translation: BAA23672.1.
IPI	IPI00328073.
RefSeq	NP_598268.1. NM_133584.1.
UniGene	Rn.10861. Rn.133138.
3D structure databases
ProteinModelPortal	O54735.
SMR	O54735. Positions 122-269, 493-818.
ModBase	Search...
Protein-protein interaction databases
STRING	O54735.
PTM databases
PhosphoSite	O54735.
Proteomic databases
PRIDE	O54735.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	171115.
KEGG	rno:171115.
UCSC	NM_133584. rat.
Organism-specific databases
CTD	8654.
RGD	620995. Pde5a.
Phylogenomic databases
eggNOG	maNOG05677.
HOVERGEN	HBG101207.
InParanoid	O54735.
OrthoDB	EOG4WSW90.
Gene expression databases
ArrayExpress	O54735.
Genevestigator	O54735.
GermOnline	ENSRNOG00000014443. Rattus norvegicus.
Family and domain databases
InterPro	IPR003018. GAF. IPR003607. Metal-dep_PHydrolase_HD_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [Graphical view]
Gene3D	G3DSA:1.10.1300.10. PDEase_catalytic_dom. 1 hit.
KO	K13762.
Pfam	PF01590. GAF. 2 hits. PF00233. PDEase_I. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00065. GAF. 2 hits. SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	621836.

Entry name

PDE5A_RAT

Accession

Primary (citable) accession number: O54735

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

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.