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P06776

- PDE2_YEAST

UniProt

P06776 - PDE2_YEAST

Protein

3',5'-cyclic-nucleotide phosphodiesterase 2

Gene

PDE2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Controls the level of cAMP in yeast cells, together with the low-affinity cAMP phosphodiesterase (PDE1).

    Catalytic activityi

    Adenosine 3',5'-cyclic phosphate + H2O = adenosine 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
    Active sitei265 – 2651Proton donorBy similarity
    Metal bindingi269 – 2691Divalent metal cation 1By similarity
    Metal bindingi302 – 3021Divalent metal cation 1By similarity
    Metal bindingi303 – 3031Divalent metal cation 1By similarity
    Metal bindingi303 – 3031Divalent metal cation 2By similarity
    Metal bindingi400 – 4001Divalent metal cation 1By similarity

    GO - Molecular functioni

    1. 3',5'-cyclic-AMP phosphodiesterase activity Source: SGD
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cAMP-mediated signaling Source: SGD
    2. metabolic process Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:YOR360C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3',5'-cyclic-nucleotide phosphodiesterase 2 (EC:3.1.4.17)
    Short name:
    PDEase 2
    Alternative name(s):
    High-affinity cAMP phosphodiesterase
    Gene namesi
    Name:PDE2
    Synonyms:SRA5
    Ordered Locus Names:YOR360C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR360c.
    SGDiS000005887. PDE2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5265263',5'-cyclic-nucleotide phosphodiesterase 2PRO_0000198851Add
    BLAST

    Proteomic databases

    MaxQBiP06776.
    PaxDbiP06776.
    PeptideAtlasiP06776.

    Expressioni

    Gene expression databases

    GenevestigatoriP06776.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi34745. 236 interactions.
    DIPiDIP-4055N.
    IntActiP06776. 3 interactions.
    MINTiMINT-498200.
    STRINGi4932.YOR360C.

    Structurei

    3D structure databases

    ProteinModelPortaliP06776.
    SMRiP06776. Positions 176-521.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG282089.
    HOGENOMiHOG000066009.
    KOiK01120.
    OMAiKFHNFRH.
    OrthoDBiEOG71RXW4.

    Family and domain databases

    Gene3Di1.10.1300.10. 1 hit.
    InterProiIPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    [Graphical view]
    PfamiPF00233. PDEase_I. 1 hit.
    [Graphical view]
    PRINTSiPR00387. PDIESTERASE1.
    SMARTiSM00471. HDc. 1 hit.
    [Graphical view]
    PROSITEiPS00126. PDEASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06776-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTLFLIGIH EIEKSQTIVQ NEHYFDRVIE LQDLDSLMVA LYKDRVSPFP    50
    NVHNFETGVS IVLYDPSKFQ LSVRQLDVLF KRFFPSFNIS AIDHTREENL 100
    QRLECVEREN SICRNRITRI NHWMYHHHDD TPDGINKNSY GTVNGNSVPT 150
    QACEANIYTL LLHLNDSKAQ HLRKASVPRL IRNIEFMSFL SDPIEKISQE 200
    GSHYWNILST WDFCALSLST QELIWCGFTL IKKLSKDAKV LIADNKLLLL 250
    LFTLESSYHQ VNKFHNFRHA IDVMQATWRL CTYLLKDNPV QTLLLCMAAI 300
    GHDVGHPGTN NQLLCNCESE VAQNFKNVSI LENFHRELFQ QLLSEHWPQL 350
    LSISKKKFDF ISEAILATDM ALHSQYEDRL MHENPMKQIT LISLIIKAAD 400
    ISNVTRTLSI SARWAYLITL EFNDCALLET FHKAHRPEQD CFGDSYKNVD 450
    SPKEDLESIQ NILVNVTDPD DIIKDHPHIP NGQIFFINTF AEVFFNALSQ 500
    KFSGLKFLSD NVKINKEYWM KHKKPQ 526
    Length:526
    Mass (Da):61,000
    Last modified:November 1, 1997 - v2
    Checksum:i2058659DA87F286B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821R → G in AAA34846. (PubMed:3025832)Curated
    Sequence conflicti349 – 3502QL → LK in AAA34846. (PubMed:3025832)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14563 Genomic DNA. Translation: AAA34846.1.
    Z75268 Genomic DNA. Translation: CAA99689.1.
    BK006948 Genomic DNA. Translation: DAA11121.1.
    PIRiS67272.
    RefSeqiNP_015005.1. NM_001183780.1.

    Genome annotation databases

    EnsemblFungiiYOR360C; YOR360C; YOR360C.
    GeneIDi854542.
    KEGGisce:YOR360C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14563 Genomic DNA. Translation: AAA34846.1 .
    Z75268 Genomic DNA. Translation: CAA99689.1 .
    BK006948 Genomic DNA. Translation: DAA11121.1 .
    PIRi S67272.
    RefSeqi NP_015005.1. NM_001183780.1.

    3D structure databases

    ProteinModelPortali P06776.
    SMRi P06776. Positions 176-521.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34745. 236 interactions.
    DIPi DIP-4055N.
    IntActi P06776. 3 interactions.
    MINTi MINT-498200.
    STRINGi 4932.YOR360C.

    Proteomic databases

    MaxQBi P06776.
    PaxDbi P06776.
    PeptideAtlasi P06776.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR360C ; YOR360C ; YOR360C .
    GeneIDi 854542.
    KEGGi sce:YOR360C.

    Organism-specific databases

    CYGDi YOR360c.
    SGDi S000005887. PDE2.

    Phylogenomic databases

    eggNOGi NOG282089.
    HOGENOMi HOG000066009.
    KOi K01120.
    OMAi KFHNFRH.
    OrthoDBi EOG71RXW4.

    Enzyme and pathway databases

    BioCyci YEAST:YOR360C-MONOMER.

    Miscellaneous databases

    NextBioi 976949.

    Gene expression databases

    Genevestigatori P06776.

    Family and domain databases

    Gene3Di 1.10.1300.10. 1 hit.
    InterProi IPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    [Graphical view ]
    Pfami PF00233. PDEase_I. 1 hit.
    [Graphical view ]
    PRINTSi PR00387. PDIESTERASE1.
    SMARTi SM00471. HDc. 1 hit.
    [Graphical view ]
    PROSITEi PS00126. PDEASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the high-affinity cAMP phosphodiesterase of Saccharomyces cerevisiae."
      Sass P., Field J., Nikawa J., Toda T., Wigler M.
      Proc. Natl. Acad. Sci. U.S.A. 83:9303-9307(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPDE2_YEAST
    AccessioniPrimary (citable) accession number: P06776
    Secondary accession number(s): D6W355, Q08836
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 6510 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3