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Q27497

- GLC7A_CAEEL

UniProt

Q27497 - GLC7A_CAEEL

Protein

Serine/threonine-protein phosphatase PP1-alpha

Gene

gsp-1

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (01 Jan 1999)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein phosphatase which antagonizes the function of air-2 in the regulation of chromosome cohesion. Dephosphorylates histone H3 at 'Ser-10'. Also involved in the activation of chloride channel clh-3 during cell swelling and meiotic maturation.4 Publications

    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 bindingi64 – 641Manganese 1By similarity
    Metal bindingi66 – 661Manganese 1By similarity
    Metal bindingi92 – 921Manganese 1By similarity
    Metal bindingi92 – 921Manganese 2By similarity
    Metal bindingi124 – 1241Manganese 2By similarity
    Active sitei125 – 1251Proton donorBy similarity
    Metal bindingi173 – 1731Manganese 2By similarity
    Metal bindingi248 – 2481Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoprotein phosphatase activity Source: UniProtKB-KW
    3. protein binding Source: WormBase

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. meiotic nuclear division Source: UniProtKB-KW
    3. mitotic nuclear division Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Meiosis, Mitosis

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_227023. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1-alpha (EC:3.1.3.16)
    Alternative name(s):
    CeGLC-7-alpha
    Glc seven-like phosphatase 1
    Gene namesi
    Name:gsp-1
    ORF Names:F29F11.6
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome V

    Organism-specific databases

    WormBaseiF29F11.6a; CE20735; WBGene00001747; gsp-1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329Serine/threonine-protein phosphatase PP1-alphaPRO_0000268637Add
    BLAST

    Proteomic databases

    PaxDbiQ27497.
    PRIDEiQ27497.

    Interactioni

    Protein-protein interaction databases

    BioGridi44515. 2 interactions.
    DIPiDIP-55373N.
    IntActiQ27497. 3 interactions.
    STRINGi6239.F29F11.6.

    Structurei

    3D structure databases

    ProteinModelPortaliQ27497.
    SMRiQ27497. Positions 4-309.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000062911.
    HOGENOMiHOG000172697.
    InParanoidiQ27497.
    KOiK06269.
    OMAiPDLQGME.
    PhylomeDBiQ27497.

    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.

    Q27497-1 [UniParc]FASTAAdd to Basket

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    MSNDGDLNID NLITRLLEVR GCRPGKPVTM SEAEIRALCH KSREIFLSQP    50
    ILLELEAPLK ICGDIHGQYN DLLRLFEYGG FPPEANYLFL GDYVDRGKQS 100
    LETICLLLAY KVKYPENFFL LRGNHECASI NRIYGFYDEC KRRFSIKLWK 150
    TFTDCFNCLP IAALIDEKIF CCHGGLSPDL QNMEQIRRVM RPTDVPDTGL 200
    LCDLLWSDPD KDVTGWGEND RGVSFTFGPD VVAKFLNRHD LDLICRAHQV 250
    VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG GMMSVDETLM CSFQILKPSE 300
    KKAKYQYQGM NSGRPAVGGG RPGTTAGKK 329
    Length:329
    Mass (Da):37,205
    Last modified:January 1, 1999 - v2
    Checksum:i500145324CA16D1B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z73974 Genomic DNA. Translation: CAA98273.1.
    PIRiT21553.
    RefSeqiNP_001256249.1. NM_001269320.1.
    NP_001256250.1. NM_001269321.1.
    UniGeneiCel.17676.

    Genome annotation databases

    EnsemblMetazoaiF29F11.6a; F29F11.6a; WBGene00001747.
    F29F11.6b; F29F11.6b; WBGene00001747.
    GeneIDi179486.
    KEGGicel:CELE_F29F11.6.
    UCSCiF29F11.6. c. elegans.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z73974 Genomic DNA. Translation: CAA98273.1 .
    PIRi T21553.
    RefSeqi NP_001256249.1. NM_001269320.1.
    NP_001256250.1. NM_001269321.1.
    UniGenei Cel.17676.

    3D structure databases

    ProteinModelPortali Q27497.
    SMRi Q27497. Positions 4-309.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 44515. 2 interactions.
    DIPi DIP-55373N.
    IntActi Q27497. 3 interactions.
    STRINGi 6239.F29F11.6.

    Proteomic databases

    PaxDbi Q27497.
    PRIDEi Q27497.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai F29F11.6a ; F29F11.6a ; WBGene00001747 .
    F29F11.6b ; F29F11.6b ; WBGene00001747 .
    GeneIDi 179486.
    KEGGi cel:CELE_F29F11.6.
    UCSCi F29F11.6. c. elegans.

    Organism-specific databases

    CTDi 179486.
    WormBasei F29F11.6a ; CE20735 ; WBGene00001747 ; gsp-1.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00530000062911.
    HOGENOMi HOG000172697.
    InParanoidi Q27497.
    KOi K06269.
    OMAi PDLQGME.
    PhylomeDBi Q27497.

    Enzyme and pathway databases

    Reactomei REACT_227023. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    NextBioi 905606.
    PROi Q27497.

    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. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.
    2. "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes."
      Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K., Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M., Allis C.D.
      Cell 102:279-291(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    3. "The aurora kinase AIR-2 functions in the release of chromosome cohesion in Caenorhabditis elegans meiosis."
      Rogers E., Bishop J.D., Waddle J.A., Schumacher J.M., Lin R.
      J. Cell Biol. 157:219-229(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "Cell cycle- and swelling-induced activation of a Caenorhabditis elegans ClC channel is mediated by CeGLC-7alpha/beta phosphatases."
      Rutledge E., Denton J., Strange K.
      J. Cell Biol. 158:435-444(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Caenorhabditis elegans RBX1 is essential for meiosis, mitotic chromosomal condensation and segregation, and cytokinesis."
      Sasagawa Y., Urano T., Kohara Y., Takahashi H., Higashitani A.
      Genes Cells 8:857-872(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiGLC7A_CAEEL
    AccessioniPrimary (citable) accession number: Q27497
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: January 1, 1999
    Last modified: October 1, 2014
    This is version 103 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3