cGMP-specific 3',5'-cyclic phosphodiesterase

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Q8CG03 (PDE5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. History...

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

Documents (4) |

Third-party data

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

Names and origin

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	865 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Domain	Repeat
Ligand	Metal-binding Nucleotide-binding cGMP cGMP-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cGMP catabolic process Inferred from direct assay. Source: MGI negative regulation of T cell proliferation Inferred from mutant phenotype. Source: MGI negative regulation of cardiac muscle contraction Inferred from mutant phenotype. Source: BHF-UCL positive regulation of G-protein coupled receptor protein signaling pathway Inferred by curator. Source: BHF-UCL positive regulation of MAP kinase activity Inferred from mutant phenotype. Source: BHF-UCL positive regulation of cardiac muscle hypertrophy Inferred from mutant phenotype. Source: BHF-UCL positive regulation of oocyte development Inferred from mutant phenotype. Source: MGI relaxation of cardiac muscle Inferred from mutant phenotype. Source: BHF-UCL signal transduction Inferred from electronic annotation. Source: InterPro
Molecular function	3',5'-cyclic-GMP phosphodiesterase activity Inferred from electronic annotation. Source: EC cGMP binding Inferred from direct assay. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 865

865

cGMP-specific 3',5'-cyclic phosphodiesterase

PRO_0000198824

Regions

Domain

154 – 304

151

GAF 1

Domain

336 – 493

158

GAF 2

Region

578 – 843

266

Catalytic By similarity

Sites

Active site

603

Proton donor By similarity

Metal binding

607

Divalent metal cation 1 By similarity

Metal binding

643

Divalent metal cation 1 By similarity

Metal binding

644

Divalent metal cation 1 By similarity

Metal binding

644

Divalent metal cation 2 By similarity

Metal binding

754

Divalent metal cation 1 By similarity

Binding site

807

cGMP By similarity

Amino acid modifications

Modified residue

Phosphoserine Potential

Experimental info

Sequence conflict

176

S → T in AAN17330. Ref.1

Secondary structure

865

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q8CG03 [UniParc].

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

FASTA

865

98,407

        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' referencesShow '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: 15489334] [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.

IPI

IPI00229355.

RefSeq

NP_700471.2. NM_153422.2.

UniGene

Mm.134911.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K31	NMR	-	A	154-320	[»]

ProteinModelPortal

Q8CG03.

SMR

Q8CG03. Positions 89-509, 525-850.

ModBase

Search...

Protein-protein interaction databases

STRING

Q8CG03.

PTM databases

PhosphoSite

Q8CG03.

Proteomic databases

PRIDE

Q8CG03.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000066728; ENSMUSP00000069011; ENSMUSG00000053965.

GeneID

242202.

KEGG

mmu:242202.

Organism-specific databases

CTD

8654.

MGI

MGI:2651499. Pde5a.

Phylogenomic databases

eggNOG

roNOG13527.

GeneTree

ENSGT00550000074280.

HOGENOM

HBG444971.

HOVERGEN

HBG101207.

InParanoid

Q8CG03.

OrthoDB

EOG4WSW90.

Gene expression databases

ArrayExpress

Q8CG03.

Bgee

Q8CG03.

CleanEx

MM_PDE5A.

Genevestigator

Q8CG03.

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.

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

385258.

SOURCE

Search...

Entry information

Entry name

PDE5A_MOUSE

Accession

Primary (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:	January 25, 2012
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

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

Entry information

Relevant documents