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Q01062 (PDE2A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length928 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 By similarity.

Subcellular location

Membrane; Peripheral membrane protein Potential.

Tissue specificity

Brain.

Domain

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

Miscellaneous

cGMP binds at an allosteric activator site By similarity.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE2 subfamily.

Contains 2 GAF domains.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandcAMP
cGMP
cGMP-binding
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcAMP catabolic process

Inferred from direct assay PubMed 21724846. Source: UniProtKB

cAMP-mediated signaling

Inferred from mutant phenotype PubMed 21724846. Source: UniProtKB

cGMP catabolic process

Inferred from direct assay PubMed 12573460PubMed 12834273. Source: RGD

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 macrophage colony-stimulating factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of endothelial barrier

Inferred from direct assay PubMed 20139324. 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 inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of vascular permeability

Inferred from sequence or structural similarity. Source: UniProtKB

protein targeting to mitochondrion

Inferred from mutant phenotype PubMed 21724846. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 19506089. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 12573460. Source: RGD

mitochondrial matrix

Inferred from direct assay PubMed 21724846. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

presynaptic membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncAMP binding

Inferred from direct assay PubMed 12573460. Source: RGD

cGMP binding

Inferred from direct assay PubMed 12573460. Source: RGD

cGMP-stimulated cyclic-nucleotide phosphodiesterase activity

Inferred from direct assay PubMed 12107056PubMed 12573460PubMed 12834273. Source: RGD

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 binding

Inferred from physical interaction PubMed 17329248. Source: IntAct

protein homodimerization activity

Inferred from direct assay PubMed 12573460. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AipQ5FWY52EBI-1786062,EBI-1786045

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Select]

Note: Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms.
Isoform PDE2A3 (identifier: Q01062-1)

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 PDE2A1 (identifier: Q01062-2)

The sequence of this isoform is not available.
Isoform PDE2A2 (identifier: Q01062-3)

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 928928cGMP-dependent 3',5'-cyclic phosphodiesterase
PRO_0000198798

Regions

Domain228 – 365138GAF 1
Domain397 – 536140GAF 2
Region621 – 879259Catalytic By similarity
Region644 – 6485Substrate binding By similarity

Sites

Active site6441Proton donor By similarity
Metal binding6481Divalent metal cation 1 By similarity
Metal binding6841Divalent metal cation 1 By similarity
Metal binding6851Divalent metal cation 1 By similarity
Metal binding6851Divalent metal cation 2 By similarity
Metal binding7961Divalent metal cation 1 By similarity
Binding site4191cGMP By similarity
Binding site4341cGMP By similarity
Binding site4871cGMP By similarity
Binding site6851Substrate By similarity
Binding site7961Substrate By similarity

Experimental info

Sequence conflict6461W → R in AAA40922. Ref.2
Sequence conflict7581L → M Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform PDE2A3 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: EF0B8C1E266EAB18

FASTA928104,664
        10         20         30         40         50         60 
MVLVLHHILI AVVQFLRRGQ QVFLKPDEPP PQPCADSLQD ALLSLGAVID IAGLRQAAKD 

        70         80         90        100        110        120 
ALSAVLPKVE TVYTYLVDGE SRLVCEDPPH ELPQEGKIRE AVISRKRLSC DGLGPSDLLG 

       130        140        150        160        170        180 
KPLARLVAPL APDTQVLVIP LLDKETGTVA AVILVHCGQL SDSEEQSLQV VEKHALVALQ 

       190        200        210        220        230        240 
RVQALQQRRP EAVQNTSADP SEDQKDEKGY TAHDRKILQL CGELYDLDAT SLQLKVLRYL 

       250        260        270        280        290        300 
QQETQATHCC LLLVSEDNLQ LSCKVIGEKV LGEEVSFPLT MGRLGQVVED KQCIQLKDLT 

       310        320        330        340        350        360 
SDDVQQLQNM LGCELRAMLC VPVISRATDQ VVALACAFNK LGGDFFTDED ERAIQHCFHY 

       370        380        390        400        410        420 
TGTVLTSTLA FQKEQKLKCE CQALLQVAKN LFTHLDDVSV LLQEIITEAR NLSNAEICSV 

       430        440        450        460        470        480 
FLLDQNELVA KVFDGGVVDD ESYEIRIPAD QGIAGHVATT GQILNIPDAY AHPLFYRGVD 

       490        500        510        520        530        540 
DSTGFRTRNI LCFPIKNENQ EVIGVAELVN KINGPWFSKF DEDLATAFSI YCGISIAHSL 

       550        560        570        580        590        600 
LYKKVNEAQY RSHLANEMMM YHMKVSDDEY TKLLHDGIQP VAAIDSNFAN FTYTPRSLPE 

       610        620        630        640        650        660 
DDTSMAILSM LQDMNFINNY KIDCPTLARF CLMVKKGYRD PPYHNWMHAF SVSHFCYLLY 

       670        680        690        700        710        720 
KNLELSNYLE DIEIFALFIS CMCHDLDHRG TNNSFQVASK SVLAALYSSE GSVMERHHFA 

       730        740        750        760        770        780 
QAIAILNTHG CNIFDHFSRK DYQRMLDLMR DIILATDLAH HLRIFKDLQK MAEVGYDRNN 

       790        800        810        820        830        840 
KQHHRLLLCL LMTSCDLSDQ TKGWKTTRKI AELIYKEFFS QGDLEKAMGN RPMEMMDREK 

       850        860        870        880        890        900 
AYIPELQISF MEHIAMPIYK LLQDLFPKAA ELYERVASNR EHWTKVSHKF TIRGLPSNNS 

       910        920 
LDFLDEEYEV PDLDVTRAPV NGCCSLEG 

« Hide

Isoform PDE2A1 (Sequence not available).
Isoform PDE2A2 (Sequence not available).

References

[1]"A novel cyclic GMP stimulated phosphodiesterase from rat brain."
Yang Q., Paskind M., Bolger G., Thompson W.J., Repaske D.R., Cutler L.S., Epstein P.M.
Biochem. Biophys. Res. Commun. 205:1850-1858(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase."
Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.
J. Biol. Chem. 267:18683-18688(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 643-759.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U21101 mRNA. Translation: AAA63683.1.
M94540 mRNA. Translation: AAA40922.1.
PIRJC2486.
RefSeqNP_001137319.1. NM_001143847.1.
NP_112341.1. NM_031079.1. [Q01062-1]
UniGeneRn.10044.

3D structure databases

ProteinModelPortalQ01062.
SMRQ01062. Positions 210-550, 566-903.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ01062. 1 interaction.
STRING10116.ENSRNOP00000026586.

Chemistry

BindingDBQ01062.
ChEMBLCHEMBL4650.

PTM databases

PhosphoSiteQ01062.

Proteomic databases

PRIDEQ01062.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81743.
KEGGrno:81743.
UCSCRGD:620965. rat. [Q01062-1]

Organism-specific databases

CTD5138.
RGD620965. Pde2a.

Phylogenomic databases

eggNOGNOG270709.
HOGENOMHOG000007068.
HOVERGENHBG053540.
KOK01120.
PhylomeDBQ01062.

Enzyme and pathway databases

SABIO-RKQ01062.

Gene expression databases

GenevestigatorQ01062.

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. 3 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMSSF55781. SSF55781. 3 hits.
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615464.
PROQ01062.

Entry information

Entry namePDE2A_RAT
AccessionPrimary (citable) accession number: Q01062
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 113 of the entry and version 2 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