cGMP-dependent 3',5'-cyclic phosphodiesterase

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Q922S4 (PDE2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 90. History...

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

Documents (3) |

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-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

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	916 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. 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 component	Membrane
Domain	Repeat
Ligand	Metal-binding Nucleotide-binding cAMP cGMP cGMP-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cAMP catabolic process Inferred from mutant phenotype. Source: UniProtKB cAMP-mediated signaling Inferred from mutant phenotype. Source: UniProtKB cGMP catabolic process Inferred from mutant phenotype. Source: UniProtKB cGMP-mediated signaling Non-traceable author statement. 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. Source: UniProtKB cellular response to mechanical stimulus Inferred from direct assay. Source: UniProtKB establishment of endothelial barrier Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cAMP biosynthetic process Inferred from mutant phenotype. 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. Source: UniProtKB positive regulation of inflammatory response Inferred from mutant phenotype. Source: UniProtKB protein targeting to mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from direct assay. Source: UniProtKB cytosol Inferred from direct assay. Source: UniProtKB endoplasmic reticulum Inferred from direct assay. 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. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from direct assay. Source: UniProtKB presynaptic membrane Inferred from direct assay. Source: UniProtKB
Molecular function	GAF domain binding Inferred from direct assay Ref.4. Source: UniProtKB cAMP binding Inferred from mutant phenotype. Source: UniProtKB cGMP binding Inferred from direct assay Ref.4. Source: UniProtKB cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Inferred from direct assay. 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 916

916

cGMP-dependent 3',5'-cyclic phosphodiesterase

PRO_0000198797

Regions

Domain

216 – 353

138

GAF 1

Domain

385 – 524

140

GAF 2

Region

609 – 867

259

Catalytic By similarity

Region

632 – 636

Substrate binding By similarity

Sites

Active site

632

Proton donor By similarity

Metal binding

636

Divalent metal cation 1 By similarity

Metal binding

672

Divalent metal cation 1 By similarity

Metal binding

673

Divalent metal cation 1 By similarity

Metal binding

673

Divalent metal cation 2 By similarity

Metal binding

784

Divalent metal cation 1 By similarity

Binding site

407

cGMP

Binding site

422

cGMP

Binding site

475

cGMP

Binding site

673

Substrate By similarity

Binding site

784

Substrate By similarity

Amino acid modifications

Modified residue

885

Phosphoserine By similarity

Experimental info

Sequence conflict

4 – 5

VS → QP in BC057029. Ref.2

Secondary structure

916

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q922S4 [UniParc].

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

916

103,249

        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' referencesShow '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. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[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: 15489334] [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, 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: 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.

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.

IPI

IPI00623742.

UniGene

Mm.247564.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MC0	X-ray	2.86	A	190-549	[»]

ProteinModelPortal

Q922S4.

SMR

Q922S4. Positions 198-892.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q922S4. 2 interactions.

STRING

Q922S4.

PTM databases

PhosphoSite

Q922S4.

Proteomic databases

PRIDE

Q922S4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000032889; ENSMUSP00000032889; ENSMUSG00000030653.

UCSC

uc009ioq.2. mouse.

Organism-specific databases

MGI

MGI:2446107. Pde2a.

Phylogenomic databases

GeneTree

ENSGT00590000082915.

HOVERGEN

HBG053540.

Gene expression databases

ArrayExpress

Q922S4.

Bgee

Q922S4.

CleanEx

MM_PDE2A.

Genevestigator

Q922S4.

GermOnline

ENSMUSG00000030653. Mus musculus.

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.

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

SOURCE

Search...

Entry information

Entry name

PDE2A_MOUSE

Accession

Primary (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:	November 16, 2011
This is version 90 of the entry and version 3 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

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