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Q922S4

- PDE2A_MOUSE

UniProt

Q922S4 - PDE2A_MOUSE

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
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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

    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-SubCell
    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

    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.

    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

    MRRVSAASQD PLAQKPEPPG SRDDRLEDAL LSLGAVIDIA GLRQAARDAL    50
    SAVLPKVETV YTYLLDGESR LVCEDPPHEL PQEGKIREAV ISQKRLSCNG 100
    LGPSDLLGKP LARLVAPLAP DMQVLVIPLL DKETGSVAAV ILVHCGQLSD 150
    SEEQSLQVVE KHALVALRRV QALQQRRPEA VQNTSVDASE DQKDEKGYTD 200
    HDRKILQLCG ELFDLDATSL QLKVLQYLQQ ETQATHCCLL LVSEDNLQLS 250
    CKVIGDKVLG EEVSFPLTMG RLGQVVEDKQ CIQLKDLTSD DVQQLQNMLG 300
    CELQAMLCVP VISRATDQVV ALACAFNKLG GDFFTDEDEH VIQHCFHYTG 350
    TVLTSTLAFQ KEQKLKCECQ ALLQVAKNLF THLDDVSVLL QEIITEARNL 400
    SNAEICSVFL LDQNELVAKV FDGGVVDDES YEIRIPADQG IAGHVATTGQ 450
    ILNIPDAYAH PLFYRGVDDS TGFRTRNILC FPIKNENQEV IGVAELVNKI 500
    NGPWFSKFDE DLATAFSIYC GISIAHSLLY KKVNEAQYRS HLANEMMMYH 550
    MKVSDDEYTK LLHDGIQPVA AIDSNFANFT YTPRSLPEDD TSMAILSMLQ 600
    DMNFINNYKI DCPTLARFCL MVKKGYRDPP YHNWMHAFSV SHFCYLLYKN 650
    LELSNYLEDI EIFALFISCM CHDLDHRGTN NSFQVASKSV LAALYSSEGS 700
    VMERHHFAQA IAILNTHGCN IFDHFSRKDY QRMLDLMRDI ILATDLAHHL 750
    RIFKDLQKMA EVGYDRNNRQ HHRLLLCLLM TSCDLSDQTK GWKTTRKIAE 800
    LIYKEFFSQG DLEKAMGNRP MEMMDREKAY IPELQISFME HIAMPIYKLL 850
    QDLFPKAAEL YERVASNREH WTKVSHKFTI RGLPSNNSLD FLDEEYEVPD 900
    LDGTRAPVNG CCSLEG 916
    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.

    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

    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 1, 2014
    This is version 110 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