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Q27884

- PPP6_DROME

UniProt

Q27884 - PPP6_DROME

Protein

Serine/threonine-protein phosphatase 6 catalytic subunit

Gene

PpV

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    May be involved in controlling cellularization or in regulating transcription of the genes involved in this process.1 Publication

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi51 – 511Manganese 1By similarity
    Metal bindingi53 – 531Manganese 1By similarity
    Metal bindingi79 – 791Manganese 1By similarity
    Metal bindingi79 – 791Manganese 2By similarity
    Metal bindingi111 – 1111Manganese 2By similarity
    Active sitei112 – 1121Proton donorBy similarity
    Metal bindingi161 – 1611Manganese 2By similarity
    Metal bindingi235 – 2351Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein serine/threonine phosphatase activity Source: FlyBase

    GO - Biological processi

    1. G1/S transition of mitotic cell cycle Source: FlyBase
    2. mitotic cell cycle Source: FlyBase
    3. protein dephosphorylation Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    SignaLinkiQ27884.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 6 catalytic subunit (EC:3.1.3.16)
    Short name:
    PP6C
    Alternative name(s):
    Phosphatase V
    Short name:
    PP-V
    Gene namesi
    Name:PpV
    Synonyms:PPPV6A
    ORF Names:CG12217
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0003139. PpV.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 303303Serine/threonine-protein phosphatase 6 catalytic subunitPRO_0000058880Add
    BLAST

    Proteomic databases

    PaxDbiQ27884.
    PRIDEiQ27884.

    Expressioni

    Developmental stagei

    Expressed at highest levels in 2-4 hours embryos.1 Publication

    Gene expression databases

    BgeeiQ27884.

    Interactioni

    Protein-protein interaction databases

    BioGridi58069. 2 interactions.
    DIPiDIP-20494N.
    IntActiQ27884. 3 interactions.
    MINTiMINT-803511.

    Structurei

    3D structure databases

    ProteinModelPortaliQ27884.
    SMRiQ27884. Positions 3-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00550000074961.
    InParanoidiQ27884.
    KOiK15498.
    OMAiVPETSYI.
    OrthoDBiEOG74N5H2.
    PhylomeDBiQ27884.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q27884-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDVDKWIED VKKCKYLPEN ELKKLCEMVC DILLEETNIL PVSTPVTVCG    50
    DIHGQFYDLE QLFRTGGQVP HTNYIFMGDF VDRGYYSLET FTRLLTLKAR 100
    YPSRITLLRG NHETRQITKV YGFFDECFSK YGNANGWKYC CKVFDLLTIA 150
    AIIDEEVLCV HGGLSPEIIT LDQIRTIDRN GEIPYKGAFC DLVWSDPEDM 200
    EYWGQSPRGA GWLFGHNVTK DFMAINNLNL ICRAHQLVNE GIKYMFDGKL 250
    VTVWSAPNYC YRCGNVAAIL SFETAEKRQT KIFLAVPDAE RVIPKQNTTP 300
    YFL 303
    Length:303
    Mass (Da):34,759
    Last modified:November 1, 1997 - v1
    Checksum:i5269F971416E55EC
    GO

    Sequence cautioni

    The sequence AAM51039.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75980 mRNA. Translation: CAA53588.1.
    AE014298 Genomic DNA. Translation: AAF46163.1.
    BT021230 mRNA. Translation: AAX33378.1.
    AY119179 mRNA. Translation: AAM51039.1. Different initiation.
    PIRiS39611.
    RefSeqiNP_001259272.1. NM_001272343.1.
    NP_001259273.1. NM_001272344.1.
    NP_001259274.1. NM_001272345.1.
    NP_511061.1. NM_078506.3.
    UniGeneiDm.2624.

    Genome annotation databases

    EnsemblMetazoaiFBtr0070921; FBpp0070883; FBgn0003139.
    FBtr0331430; FBpp0303847; FBgn0003139.
    FBtr0331431; FBpp0303848; FBgn0003139.
    FBtr0331432; FBpp0303849; FBgn0003139.
    GeneIDi31582.
    KEGGidme:Dmel_CG12217.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75980 mRNA. Translation: CAA53588.1 .
    AE014298 Genomic DNA. Translation: AAF46163.1 .
    BT021230 mRNA. Translation: AAX33378.1 .
    AY119179 mRNA. Translation: AAM51039.1 . Different initiation.
    PIRi S39611.
    RefSeqi NP_001259272.1. NM_001272343.1.
    NP_001259273.1. NM_001272344.1.
    NP_001259274.1. NM_001272345.1.
    NP_511061.1. NM_078506.3.
    UniGenei Dm.2624.

    3D structure databases

    ProteinModelPortali Q27884.
    SMRi Q27884. Positions 3-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58069. 2 interactions.
    DIPi DIP-20494N.
    IntActi Q27884. 3 interactions.
    MINTi MINT-803511.

    Proteomic databases

    PaxDbi Q27884.
    PRIDEi Q27884.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0070921 ; FBpp0070883 ; FBgn0003139 .
    FBtr0331430 ; FBpp0303847 ; FBgn0003139 .
    FBtr0331431 ; FBpp0303848 ; FBgn0003139 .
    FBtr0331432 ; FBpp0303849 ; FBgn0003139 .
    GeneIDi 31582.
    KEGGi dme:Dmel_CG12217.

    Organism-specific databases

    CTDi 31582.
    FlyBasei FBgn0003139. PpV.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00550000074961.
    InParanoidi Q27884.
    KOi K15498.
    OMAi VPETSYI.
    OrthoDBi EOG74N5H2.
    PhylomeDBi Q27884.

    Enzyme and pathway databases

    SignaLinki Q27884.

    Miscellaneous databases

    ChiTaRSi PpV. drosophila.
    GenomeRNAii 31582.
    NextBioi 774303.
    PROi Q27884.

    Gene expression databases

    Bgeei Q27884.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Drosophila protein phosphatase V functionally complements a SIT4 mutant in Saccharomyces cerevisiae and its amino-terminal region can confer this complementation to a heterologous phosphatase catalytic domain."
      Mann D.J., Dombradi V., Cohen P.T.W.
      EMBO J. 12:4833-4842(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
      Strain: Oregon-R.
      Tissue: Eye imaginal disk and Head.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-303.
      Strain: Berkeley.
      Tissue: Embryo.

    Entry informationi

    Entry nameiPPP6_DROME
    AccessioniPrimary (citable) accession number: Q27884
    Secondary accession number(s): Q5BIJ4, Q8MRZ7, Q9W3Z8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3