cGMP-dependent 3',5'-cyclic phosphodiesterase

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Q01062 (PDE2A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. History...

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

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Third-party data

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

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	928 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Metal-binding Nucleotide-binding cAMP cGMP cGMP-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cAMP 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 12573460 PubMed 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_component	Golgi apparatus Inferred from sequence or structural similarity. 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_function	cAMP 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 12107056 PubMed 12573460 PubMed 12834273. Source: RGD 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 PubMed 12573460. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Aip	Q5FWY5	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 928

928

cGMP-dependent 3',5'-cyclic phosphodiesterase

PRO_0000198798

Regions

Domain

228 – 365

138

GAF 1

Domain

397 – 536

140

GAF 2

Region

621 – 879

259

Catalytic By similarity

Region

644 – 648

Substrate binding By similarity

Sites

Active site

644

Proton donor By similarity

Metal binding

648

Divalent metal cation 1 By similarity

Metal binding

684

Divalent metal cation 1 By similarity

Metal binding

685

Divalent metal cation 1 By similarity

Metal binding

685

Divalent metal cation 2 By similarity

Metal binding

796

Divalent metal cation 1 By similarity

Binding site

419

cGMP By similarity

Binding site

434

cGMP By similarity

Binding site

487

cGMP By similarity

Binding site

685

Substrate By similarity

Binding site

796

Substrate By similarity

Experimental info

Sequence conflict

646

W → R in AAA40922. Ref.2

Sequence conflict

758

L → M Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform PDE2A3 [UniParc].

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

FASTA

928

104,664

        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.
IPI	IPI00199076.
PIR	JC2486.
RefSeq	NP_001137319.1. NM_001143847.1. NP_112341.1. NM_031079.1.
UniGene	Rn.10044.
3D structure databases
ProteinModelPortal	Q01062.
SMR	Q01062. Positions 210-550, 566-903.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q01062. 1 interaction.
STRING	10116.ENSRNOP00000026586.
PTM databases
PhosphoSite	Q01062.
Proteomic databases
PRIDE	Q01062.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	81743.
KEGG	rno:81743.
UCSC	RGD:620965. rat.
Organism-specific databases
CTD	5138.
RGD	620965. Pde2a.
Phylogenomic databases
eggNOG	NOG270709.
HOGENOM	HOG000007068.
HOVERGEN	HBG053540.
KO	K01120.
OrthoDB	EOG4THVS9.
Enzyme and pathway databases
SABIO-RK	Q01062.
Gene expression databases
ArrayExpress	Q01062.
Genevestigator	Q01062.
GermOnline	ENSRNOG00000019560. Rattus norvegicus.
Family and domain databases
Gene3D	1.10.1300.10. 1 hit.
InterPro	IPR003018. GAF. IPR003607. HD/PDEase_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [Graphical view]
Pfam	PF01590. GAF. 2 hits. PF00233. PDEase_I. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00065. GAF. 3 hits. SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q01062.
ChEMBL	CHEMBL4650.
NextBio	615464.

Entry information

Entry name

PDE2A_RAT

Accession

Primary (citable) accession number: Q01062

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 103 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

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents