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Q922S4

- PDE2A_MOUSE

UniProt

Q922S4 - PDE2A_MOUSE

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Protein

cGMP-dependent 3',5'-cyclic phosphodiesterase

Gene

Pde2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei407 – 4071cGMP1 Publication
Binding sitei422 – 4221cGMP1 Publication
Binding sitei475 – 4751cGMP1 Publication
Active sitei632 – 6321Proton donorBy similarity
Metal bindingi636 – 6361Divalent metal cation 1By similarity
Metal bindingi672 – 6721Divalent metal cation 1By similarity
Metal bindingi673 – 6731Divalent metal cation 1By similarity
Metal bindingi673 – 6731Divalent metal cation 2By similarity
Binding sitei673 – 6731SubstrateBy similarity
Metal bindingi784 – 7841Divalent metal cation 1By similarity
Binding sitei784 – 7841SubstrateBy similarity

GO - Molecular functioni

  1. cAMP binding Source: UniProtKB
  2. cGMP binding Source: UniProtKB
  3. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  4. cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  5. drug binding Source: UniProtKB
  6. GAF domain binding Source: UniProtKB
  7. metal ion binding Source: UniProtKB-KW
  8. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. cAMP catabolic process Source: UniProtKB
  2. cAMP-mediated signaling Source: UniProtKB
  3. cellular response to cGMP Source: UniProtKB
  4. cellular response to drug Source: UniProtKB
  5. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: UniProtKB
  6. cellular response to lipopolysaccharide Source: UniProtKB
  7. cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
  8. cellular response to mechanical stimulus Source: UniProtKB
  9. cGMP catabolic process Source: UniProtKB
  10. cGMP-mediated signaling Source: UniProtKB
  11. establishment of endothelial barrier Source: UniProtKB
  12. metabolic process Source: UniProtKB
  13. negative regulation of cAMP biosynthetic process Source: UniProtKB
  14. negative regulation of protein import into nucleus, translocation Source: UniProtKB
  15. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  16. negative regulation of vascular permeability Source: UniProtKB
  17. positive regulation of gene expression Source: UniProtKB
  18. positive regulation of inflammatory response Source: UniProtKB
  19. positive regulation of vascular permeability Source: UniProtKB
  20. protein targeting to mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:Pde2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:2446107. Pde2a.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: MGI
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. dendrite Source: MGI
  5. endoplasmic reticulum Source: UniProtKB
  6. Golgi apparatus Source: UniProtKB
  7. membrane Source: UniProtKB-KW
  8. mitochondrial matrix Source: UniProtKB
  9. nucleus Source: UniProtKB
  10. perinuclear region of cytoplasm Source: UniProtKB
  11. plasma membrane Source: UniProtKB
  12. presynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 916916cGMP-dependent 3',5'-cyclic phosphodiesterasePRO_0000198797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ922S4.
PaxDbiQ922S4.
PRIDEiQ922S4.

PTM databases

PhosphoSiteiQ922S4.

Expressioni

Gene expression databases

CleanExiMM_PDE2A.
GenevestigatoriQ922S4.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiQ922S4. 2 interactions.
STRINGi10090.ENSMUSP00000095842.

Structurei

Secondary structure

1
916
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi199 – 21012
Helixi217 – 23115
Beta strandi234 – 2429
Beta strandi244 – 2463
Beta strandi248 – 2547
Beta strandi257 – 27115
Helixi272 – 2787
Helixi284 – 2863
Helixi289 – 29911
Beta strandi306 – 3127
Turni314 – 3163
Beta strandi318 – 33013
Helixi337 – 38145
Turni382 – 3843
Turni386 – 3883
Helixi389 – 40113
Beta strandi403 – 4119
Beta strandi413 – 4219
Helixi440 – 4489
Beta strandi452 – 4554
Helixi468 – 4714
Beta strandi478 – 4847
Beta strandi490 – 49910
Beta strandi502 – 5043
Helixi507 – 53529

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MC0X-ray2.86A190-549[»]
ProteinModelPortaliQ922S4.
SMRiQ922S4. Positions 198-892.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ922S4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini216 – 353138GAF 1Add
BLAST
Domaini385 – 524140GAF 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni609 – 867259CatalyticBy similarityAdd
BLAST
Regioni632 – 6365Substrate bindingBy similarity

Domaini

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

Sequence similaritiesi

Contains 2 GAF domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270709.
HOGENOMiHOG000007068.
HOVERGENiHBG053540.
InParanoidiQ922S4.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 3 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q922S4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRRVSAASQD PLAQKPEPPG SRDDRLEDAL LSLGAVIDIA GLRQAARDAL
60 70 80 90 100
SAVLPKVETV YTYLLDGESR LVCEDPPHEL PQEGKIREAV ISQKRLSCNG
110 120 130 140 150
LGPSDLLGKP LARLVAPLAP DMQVLVIPLL DKETGSVAAV ILVHCGQLSD
160 170 180 190 200
SEEQSLQVVE KHALVALRRV QALQQRRPEA VQNTSVDASE DQKDEKGYTD
210 220 230 240 250
HDRKILQLCG ELFDLDATSL QLKVLQYLQQ ETQATHCCLL LVSEDNLQLS
260 270 280 290 300
CKVIGDKVLG EEVSFPLTMG RLGQVVEDKQ CIQLKDLTSD DVQQLQNMLG
310 320 330 340 350
CELQAMLCVP VISRATDQVV ALACAFNKLG GDFFTDEDEH VIQHCFHYTG
360 370 380 390 400
TVLTSTLAFQ KEQKLKCECQ ALLQVAKNLF THLDDVSVLL QEIITEARNL
410 420 430 440 450
SNAEICSVFL LDQNELVAKV FDGGVVDDES YEIRIPADQG IAGHVATTGQ
460 470 480 490 500
ILNIPDAYAH PLFYRGVDDS TGFRTRNILC FPIKNENQEV IGVAELVNKI
510 520 530 540 550
NGPWFSKFDE DLATAFSIYC GISIAHSLLY KKVNEAQYRS HLANEMMMYH
560 570 580 590 600
MKVSDDEYTK LLHDGIQPVA AIDSNFANFT YTPRSLPEDD TSMAILSMLQ
610 620 630 640 650
DMNFINNYKI DCPTLARFCL MVKKGYRDPP YHNWMHAFSV SHFCYLLYKN
660 670 680 690 700
LELSNYLEDI EIFALFISCM CHDLDHRGTN NSFQVASKSV LAALYSSEGS
710 720 730 740 750
VMERHHFAQA IAILNTHGCN IFDHFSRKDY QRMLDLMRDI ILATDLAHHL
760 770 780 790 800
RIFKDLQKMA EVGYDRNNRQ HHRLLLCLLM TSCDLSDQTK GWKTTRKIAE
810 820 830 840 850
LIYKEFFSQG DLEKAMGNRP MEMMDREKAY IPELQISFME HIAMPIYKLL
860 870 880 890 900
QDLFPKAAEL YERVASNREH WTKVSHKFTI RGLPSNNSLD FLDEEYEVPD
910
LDGTRAPVNG CCSLEG
Length:916
Mass (Da):103,249
Last modified:July 27, 2011 - v3
Checksum:iA386C6773CC4F5B4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 52VS → QP in BC057029. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
UniGeneiMm.247564.

Genome annotation databases

UCSCiuc009ioq.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
UniGenei Mm.247564.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MC0 X-ray 2.86 A 190-549 [» ]
ProteinModelPortali Q922S4.
SMRi Q922S4. Positions 198-892.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q922S4. 2 interactions.
STRINGi 10090.ENSMUSP00000095842.

PTM databases

PhosphoSitei Q922S4.

Proteomic databases

MaxQBi Q922S4.
PaxDbi Q922S4.
PRIDEi Q922S4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi uc009ioq.3. mouse.

Organism-specific databases

MGIi MGI:2446107. Pde2a.

Phylogenomic databases

eggNOGi NOG270709.
HOGENOMi HOG000007068.
HOVERGENi HBG053540.
InParanoidi Q922S4.

Miscellaneous databases

EvolutionaryTracei Q922S4.
PROi Q922S4.
SOURCEi Search...

Gene expression databases

CleanExi MM_PDE2A.
Genevestigatori Q922S4.

Family and domain databases

Gene3Di 1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProi IPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view ]
SUPFAMi SSF55781. SSF55781. 3 hits.
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiPDE2A_MOUSE
AccessioniPrimary (citable) accession number: Q922S4
Secondary accession number(s): Q8K2U1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

cGMP binds at an allosteric activator site.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3