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Q922S4 (PDE2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-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) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

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.4

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. Ref.4

Miscellaneous

cGMP binds at an allosteric activator site.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE2 subfamily.

Contains 2 GAF domains.

Ontologies

Keywords
   Cellular componentMembrane
   DomainRepeat
   LigandcAMP
cGMP
cGMP-binding
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcAMP catabolic process

Inferred from mutant phenotype PubMed 21571906. Source: UniProtKB

cAMP-mediated signaling

Inferred from mutant phenotype PubMed 21724846. Source: UniProtKB

cGMP catabolic process

Inferred from mutant phenotype PubMed 19632989PubMed 19632989. Source: UniProtKB

cGMP-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to cGMP

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to granulocyte macrophage colony-stimulating factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 21571906. Source: UniProtKB

cellular response to macrophage colony-stimulating factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from direct assay PubMed 21571906. Source: UniProtKB

establishment of endothelial barrier

Inferred from sequence or structural similarity. Source: UniProtKB

metabolic process

Inferred from direct assay PubMed 15210692. Source: UniProtKB

negative regulation of cAMP biosynthetic process

Inferred from mutant phenotype PubMed 21724846. Source: UniProtKB

negative regulation of protein import into nucleus, translocation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of vascular permeability

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype PubMed 21571906. Source: UniProtKB

positive regulation of inflammatory response

Inferred from mutant phenotype PubMed 21571906. Source: UniProtKB

positive regulation of vascular permeability

Inferred from sequence or structural similarity. Source: UniProtKB

protein targeting to mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 19632989. Source: UniProtKB

axon

Inferred from direct assay PubMed 8586960. Source: MGI

cytoplasm

Inferred from direct assay PubMed 19506089PubMed 21571906. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 19632989PubMed 19632989PubMed 19632989. Source: UniProtKB

dendrite

Inferred from direct assay PubMed 8586960. Source: MGI

endoplasmic reticulum

Inferred from direct assay PubMed 19632989. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial matrix

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 19632989. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 19632989. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 19632989PubMed 19632989. Source: UniProtKB

presynaptic membrane

Inferred from direct assay PubMed 19506089. Source: UniProtKB

   Molecular_functionGAF domain binding

Inferred from direct assay Ref.4. Source: UniProtKB

cAMP binding

Inferred from mutant phenotype PubMed 15210692. Source: UniProtKB

cGMP binding

Inferred from direct assay Ref.4. Source: UniProtKB

cGMP-stimulated cyclic-nucleotide phosphodiesterase activity

Inferred from direct assay PubMed 15210692. Source: UniProtKB

cyclic-nucleotide phosphodiesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein homodimerization activity

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

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 site4071cGMP
Binding site4221cGMP
Binding site4751cGMP
Binding site6731Substrate By similarity
Binding site7841Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Sequence conflict4 – 52VS → QP in BC057029. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q922S4 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: A386C6773CC4F5B4

FASTA916103,249
        10         20         30         40         50         60 
MRRVSAASQD 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

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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: Mammary tumor.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 805-814, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[4]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 183-549 IN COMPLEX WITH CGMP, DOMAIN GAF 1, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC129079 Genomic DNA. No translation available.
AC129609 Genomic DNA. No translation available.
BC006845 mRNA. Translation: AAH06845.1.
BC029810 mRNA. Translation: AAH29810.1.
BC057029 mRNA. No translation available.
UniGeneMm.247564.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MC0X-ray2.86A190-549[»]
ProteinModelPortalQ922S4.
SMRQ922S4. Positions 198-892.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ922S4. 2 interactions.
STRING10090.ENSMUSP00000095842.

PTM databases

PhosphoSiteQ922S4.

Proteomic databases

PaxDbQ922S4.
PRIDEQ922S4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCuc009ioq.3. mouse.

Organism-specific databases

MGIMGI:2446107. Pde2a.

Phylogenomic databases

eggNOGNOG270709.
HOGENOMHOG000007068.
HOVERGENHBG053540.

Gene expression databases

CleanExMM_PDE2A.
GenevestigatorQ922S4.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003018. GAF.
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]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ922S4.
PROQ922S4.
SOURCESearch...

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 27, 2011
Last modified: April 16, 2014
This is version 107 of the entry and version 3 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

MGD cross-references

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