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Reviewed, UniProtKB/Swiss-Prot Q922S4 (PDE2A_MOUSE)

Last modified February 9, 2010. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    cGMP-dependent 3',5'-cyclic phosphodiesterase
    EC=3.1.4.17
Alternative name(s):
    Cyclic GMP-stimulated phosphodiesterase
      Short name=CGS-PDE
      Short name=cGSPDE
Gene names
Name: Pde2a
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length916 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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 activity

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 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.

Subunit structure

Homodimer. Ref.3

Subcellular location

Membrane; Peripheral membrane protein Potential.

Domain

GAF 1 functions as a dimerization domain, whereas GAF 2 binds cGMP, which causes activation of the catalytic activity of the enzyme.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE2 subfamily.

Contains 2 GAF domains.

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Ontologies

Keywords
   Cellular componentMembrane
   DomainRepeat
   LigandMetal-binding
Nucleotide-binding
cAMP
cGMP
cGMP-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processsignal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentextrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3',5'-cyclic-nucleotide phosphodiesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 916916cGMP-dependent 3',5'-cyclic phosphodiesterase
PRO_0000198797

Regions

Domain216 – 353138GAF 1
Domain385 – 524140GAF 2
Region609 – 867259Catalytic By similarity
Region632 – 6365Substrate binding By similarity

Sites

Active site6321Proton donor By similarity
Metal binding6361Divalent metal cation 1 By similarity
Metal binding6721Divalent metal cation 1 By similarity
Metal binding6731Divalent metal cation 1 By similarity
Metal binding6731Divalent metal cation 2 By similarity
Metal binding7841Divalent metal cation 1 By similarity
Binding site4071Allosteric activator cGMP
Binding site4221Allosteric activator cGMP
Binding site4751Allosteric activator cGMP
Binding site6731Substrate By similarity
Binding site7841Substrate By similarity

Amino acid modifications

Modified residue8851Phosphoserine By similarity

Secondary structure

1 ................................................ 916
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q922S4-1 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: 51C03B086633BF20

FASTA916103,288
        10         20         30         40         50         60 
MRRQPAASQD PLAQKPEPPG SRDDRLEDAL LSLGAVIDIA GLRQAARDAL SAVLPKVETV 

        70         80         90        100        110        120 
YTYLLDGESR LVCEDPPHEL PQEGKIREAV ISQKRLSCNG LGPSDLLGKP LARLVAPLAP 

       130        140        150        160        170        180 
DMQVLVIPLL DKETGSVAAV ILVHCGQLSD SEEQSLQVVE KHALVALRRV QALQQRRPEA 

       190        200        210        220        230        240 
VQNTSVDASE DQKDEKGYTD HDRKILQLCG ELFDLDATSL QLKVLQYLQQ ETQATHCCLL 

       250        260        270        280        290        300 
LVSEDNLQLS CKVIGDKVLG EEVSFPLTMG RLGQVVEDKQ CIQLKDLTSD DVQQLQNMLG 

       310        320        330        340        350        360 
CELQAMLCVP VISRATDQVV ALACAFNKLG GDFFTDEDEH VIQHCFHYTG TVLTSTLAFQ 

       370        380        390        400        410        420 
KEQKLKCECQ ALLQVAKNLF THLDDVSVLL QEIITEARNL SNAEICSVFL LDQNELVAKV 

       430        440        450        460        470        480 
FDGGVVDDES YEIRIPADQG IAGHVATTGQ ILNIPDAYAH PLFYRGVDDS TGFRTRNILC 

       490        500        510        520        530        540 
FPIKNENQEV IGVAELVNKI NGPWFSKFDE DLATAFSIYC GISIAHSLLY KKVNEAQYRS 

       550        560        570        580        590        600 
HLANEMMMYH MKVSDDEYTK LLHDGIQPVA AIDSNFANFT YTPRSLPEDD TSMAILSMLQ 

       610        620        630        640        650        660 
DMNFINNYKI DCPTLARFCL MVKKGYRDPP YHNWMHAFSV SHFCYLLYKN LELSNYLEDI 

       670        680        690        700        710        720 
EIFALFISCM CHDLDHRGTN NSFQVASKSV LAALYSSEGS VMERHHFAQA IAILNTHGCN 

       730        740        750        760        770        780 
IFDHFSRKDY QRMLDLMRDI ILATDLAHHL RIFKDLQKMA EVGYDRNNRQ HHRLLLCLLM 

       790        800        810        820        830        840 
TSCDLSDQTK GWKTTRKIAE LIYKEFFSQG DLEKAMGNRP MEMMDREKAY IPELQISFME 

       850        860        870        880        890        900 
HIAMPIYKLL QDLFPKAAEL YERVASNREH WTKVSHKFTI RGLPSNNSLD FLDEEYEVPD 

       910 
LDGTRAPVNG CCSLEG

« Hide

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References

« Hide 'large scale' references
[1]"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: Mammary tumor.
[2]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 805-814, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[3]"The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding."
Martinez S.E., Wu A.Y., Glavas N.A., Tang X.-B., Turley S., Hol W.G.J., Beavo J.A.
Proc. Natl. Acad. Sci. U.S.A. 99:13260-13265(2002) [PubMed: 12271124] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 183-549 IN COMPLEX WITH CGMP, DOMAIN GAF 1, SUBUNIT.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC006845 mRNA. Translation: AAH06845.1.
BC029810 mRNA. Translation: AAH29810.1.
BC057029 mRNA. No translation available.
IPIIPI00623742.
UniGeneMm.247564

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MC0X-ray2.86A190-549[»]
SMRQ922S4. Positions 554-891.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ922S4.

PTM databases

PhosphoSiteQ922S4.

Proteomic databases

PRIDEQ922S4.

Genome annotation databases

EnsemblENSMUST00000032889; ENSMUSP00000032889; ENSMUSG00000030653; Mus musculus. [Genome view]
UCSCuc009ioq.1. mouse.

Organism-specific databases

MGIMGI:2446107. Pde2a.

Phylogenomic databases

HOVERGENQ922S4.

Enzyme and pathway databases

BRENDA3.1.4.17. 244.

Gene expression databases

ArrayExpressQ922S4.
BgeeQ922S4.
CleanExMM_PDE2A.
GenevestigatorQ922S4.
GermOnlineENSMUSG00000030653. Mus musculus.

Family and domain databases

InterProIPR003018. GAF.
IPR003607. Metal-dep_PHydrolase_HD_dom.
IPR002073. PDEase.
[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]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry namePDE2A_MOUSE
AccessionPrimary (citable) accession number: Q922S4
Secondary accession number(s): Q8K2U1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents