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P14099

- PDE2A_BOVIN

UniProt

P14099 - PDE2A_BOVIN

Protein

cGMP-dependent 3',5'-cyclic phosphodiesterase

Gene

PDE2A

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (01 Dec 1992)
      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 sitei411 – 4111cGMPBy similarity
    Binding sitei426 – 4261cGMPBy similarity
    Binding sitei479 – 4791cGMPBy similarity
    Active sitei636 – 6361Proton donorBy similarity
    Metal bindingi640 – 6401Divalent metal cation 1By similarity
    Metal bindingi676 – 6761Divalent metal cation 1By similarity
    Metal bindingi677 – 6771Divalent metal cation 1By similarity
    Metal bindingi677 – 6771Divalent metal cation 2By similarity
    Binding sitei677 – 6771SubstrateBy similarity
    Metal bindingi788 – 7881Divalent metal cation 1By similarity
    Binding sitei788 – 7881SubstrateBy similarity

    GO - Molecular functioni

    1. cGMP binding Source: UniProtKB
    2. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    3. cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    4. drug binding Source: UniProtKB
    5. metal ion binding Source: UniProtKB-KW

    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 macrophage colony-stimulating factor stimulus Source: UniProtKB
    7. cellular response to mechanical stimulus Source: UniProtKB
    8. cGMP catabolic process Source: UniProtKB
    9. cGMP-mediated signaling Source: UniProtKB
    10. establishment of endothelial barrier Source: UniProtKB
    11. GMP catabolic process Source: AgBase
    12. metabolic process Source: GOC
    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 inflammatory response Source: UniProtKB
    18. positive regulation of vascular permeability Source: UniProtKB
    19. protein targeting to mitochondrion Source: UniProtKB
    20. regulation of cAMP metabolic process Source: AgBase

    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB
    4. Golgi apparatus Source: UniProtKB
    5. mitochondrial matrix Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB
    8. plasma membrane Source: UniProtKB
    9. presynaptic membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 921921cGMP-dependent 3',5'-cyclic phosphodiesterasePRO_0000198795Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP14099.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000042623.

    Structurei

    3D structure databases

    ProteinModelPortaliP14099.
    SMRiP14099. Positions 202-542, 558-895.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini220 – 357138GAF 1Add
    BLAST
    Domaini389 – 528140GAF 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni613 – 871259CatalyticAdd
    BLAST
    Regioni636 – 6405Substrate 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.By similarity

    Sequence similaritiesi

    Contains 2 GAF domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG270709.
    HOGENOMiHOG000007068.
    HOVERGENiHBG053540.
    KOiK18283.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform PDE2A1 (identifier: P14099-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MRRQPAASRD LFAQEPVPPG SGDGALQDAL LSLGSVIDVA GLQQAVKEAL    50
    SAVLPKVETV YTYLLDGESR LVCEEPPHEL PQEGKVREAV ISRKRLGCNG 100
    LGPSDLPGKP LARLVAPLAP DTQVLVIPLV DKEAGAVAAV ILVHCGQLSD 150
    NEEWSLQAVE KHTLVALKRV QALQQRESSV APEATQNPPE EAAGDQKGGV 200
    AYTNQDRKIL QLCGELYDLD ASSLQLKVLQ YLQQETQASR CCLLLVSEDN 250
    LQLSCKVIGD KVLEEEISFP LTTGRLGQVV EDKKSIQLKD LTSEDMQQLQ 300
    SMLGCEVQAM LCVPVISRAT DQVVALACAF NKLGGDLFTD QDEHVIQHCF 350
    HYTSTVLTST LAFQKEQKLK CECQALLQVA KNLFTHLDDV SVLLQEIITE 400
    ARNLSNAEIC SVFLLDQNEL VAKVFDGGVV EDESYEIRIP ADQGIAGHVA 450
    TTGQILNIPD AYAHPLFYRG VDDSTGFRTR NILCFPIKNE NQEVIGVAEL 500
    VNKINGPWFS KFDEDLATAF SIYCGISIAH SLLYKKVNEA QYRSHLANEM 550
    MMYHMKVSDD EYTKLLHDGI QPVAAIDSNF ASFTYTPRSL PEDDTSMAIL 600
    SMLQDMNFIN NYKIDCPTLA RFCLMVKKGY RDPPYHNWMH AFSVSHFCYL 650
    LYKNLELTNY LEDMEIFALF ISCMCHDLDH RGTNNSFQVA SKSVLAALYS 700
    SEGSVMERHH FAQAIAILNT HGCNIFDHFS RKDYQRMLDL MRDIILATDL 750
    AHHLRIFKDL QKMAEVGYDR TNKQHHSLLL CLLMTSCDLS DQTKGWKTTR 800
    KIAELIYKEF FSQGDLEKAM GNRPMEMMDR EKAYIPELQI SFMEHIAMPI 850
    YKLLQDLFPK AAELYERVAS NREHWTKVSH KFTIRGLPSN NSLDFLDEEY 900
    EVPDLDGARA PINGCCSLDA E 921
    Length:921
    Mass (Da):103,228
    Last modified:December 1, 1992 - v2
    Checksum:iE29F4C9875E83640
    GO
    Isoform PDE2A2 (identifier: P14099-3)

    Sequence is not available
    Length:
    Mass (Da):
    Isoform PDE2A3 (identifier: P14099-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: MRRQPAASRDLFAQEPVPPGSGDGA → MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADS

    Show »
    Length:942
    Mass (Da):105,575
    Checksum:iC2EC7D62C1C3F993
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti204 – 2041N → D in AAA87353. 1 PublicationCurated
    Sequence conflicti633 – 6331P → L AA sequence (PubMed:3025833)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2525MRRQP…SGDGA → MGQACGHSILCRSQQYPAAR PAEPRGQQVFLKPDEPPPPP QPCADS in isoform PDE2A3. 1 PublicationVSP_004555Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73512 mRNA. Translation: AAA74559.1.
    L49503 mRNA. Translation: AAA87353.1.
    PIRiA40981.
    RefSeqiNP_001137318.1. NM_001143846.1.
    NP_001243202.1. NM_001256273.1. [P14099-1]
    UniGeneiBt.4716.

    Genome annotation databases

    GeneIDi281971.
    KEGGibta:281971.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73512 mRNA. Translation: AAA74559.1 .
    L49503 mRNA. Translation: AAA87353.1 .
    PIRi A40981.
    RefSeqi NP_001137318.1. NM_001143846.1.
    NP_001243202.1. NM_001256273.1. [P14099-1 ]
    UniGenei Bt.4716.

    3D structure databases

    ProteinModelPortali P14099.
    SMRi P14099. Positions 202-542, 558-895.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000042623.

    Chemistry

    BindingDBi P14099.
    ChEMBLi CHEMBL3477.

    Proteomic databases

    PRIDEi P14099.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 281971.
    KEGGi bta:281971.

    Organism-specific databases

    CTDi 5138.

    Phylogenomic databases

    eggNOGi NOG270709.
    HOGENOMi HOG000007068.
    HOVERGENi HBG053540.
    KOi K18283.

    Miscellaneous databases

    NextBioi 20805842.

    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. "Molecular cloning of a cyclic GMP-stimulated cyclic nucleotide phosphodiesterase cDNA. Identification and distribution of isozyme variants."
      Sonnenburg W.K., Mullaney P.J., Beavo J.A.
      J. Biol. Chem. 266:17655-17661(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A1).
    2. Juilfs D.M., Sonnenburg W.K., Seraji S., Beavo J.A.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A3).
      Tissue: Brain.
    3. "Amino acid sequence of the cyclic GMP stimulated cyclic nucleotide phosphodiesterase from bovine heart."
      le Trong H., Beier N., Sonnenburg W.K., Stroop S.D., Walsh K.A., Beavo J.A., Charbonneau H.
      Biochemistry 29:10280-10288(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 592-921.
      Tissue: Heart.
    4. "Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species."
      Charbonneau H., Beier N., Walsh K.A., Beavo J.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:9308-9312(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 613-694 AND 808-868.
      Tissue: Heart.

    Entry informationi

    Entry nameiPDE2A_BOVIN
    AccessioniPrimary (citable) accession number: P14099
    Secondary accession number(s): Q28064
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    cGMP binds at an allosteric activator site.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3