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O09131

- GSTO1_MOUSE

UniProt

O09131 - GSTO1_MOUSE

Protein

Glutathione S-transferase omega-1

Gene

Gsto1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid By similarity.By similarity

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.
    2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.
    Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei32 – 321NucleophileBy similarity
    Binding sitei59 – 591GlutathioneBy similarity
    Binding sitei72 – 721Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. glutathione dehydrogenase (ascorbate) activity Source: UniProtKB
    2. glutathione transferase activity Source: UniProtKB
    3. methylarsonate reductase activity Source: UniProtKB-EC
    4. oxidoreductase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to arsenic-containing substance Source: UniProtKB
    2. L-ascorbic acid metabolic process Source: UniProtKB
    3. negative regulation of ryanodine-sensitive calcium-release channel activity Source: Ensembl
    4. positive regulation of ryanodine-sensitive calcium-release channel activity Source: Ensembl
    5. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: Ensembl
    6. xenobiotic catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_215316. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase omega-1 (EC:2.5.1.18)
    Short name:
    GSTO-1
    Alternative name(s):
    Glutathione S-transferase omega 1-1
    Short name:
    GSTO 1-1
    Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
    Monomethylarsonic acid reductase (EC:1.20.4.2)
    Short name:
    MMA(V) reductase
    S-(Phenacyl)glutathione reductase
    Short name:
    SPG-R
    p28
    Gene namesi
    Name:Gsto1
    Synonyms:Gstx, Gtsttl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1342273. Gsto1.

    Subcellular locationi

    Cytoplasmcytosol By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 240239Glutathione S-transferase omega-1PRO_0000185885Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei57 – 571N6-acetyllysineBy similarity
    Modified residuei152 – 1521N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO09131.
    PaxDbiO09131.
    PRIDEiO09131.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00114285.

    PTM databases

    PhosphoSiteiO09131.

    Expressioni

    Gene expression databases

    BgeeiO09131.
    CleanExiMM_GSTO1.
    GenevestigatoriO09131.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiO09131. 2 interactions.
    MINTiMINT-1868625.
    STRINGi10090.ENSMUSP00000026050.

    Structurei

    3D structure databases

    ProteinModelPortaliO09131.
    SMRiO09131. Positions 3-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 10180GST N-terminalAdd
    BLAST
    Domaini106 – 227122GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni85 – 862Glutathione bindingBy similarity

    Sequence similaritiesi

    Belongs to the GST superfamily. Omega family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0625.
    GeneTreeiENSGT00390000005479.
    HOGENOMiHOG000006560.
    HOVERGENiHBG051853.
    InParanoidiO09131.
    KOiK00799.
    OMAiAYANEMP.
    OrthoDBiEOG71CFNG.
    PhylomeDBiO09131.
    TreeFamiTF105325.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR005442. GST_omega.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view]
    PRINTSiPR01625. GSTRNSFRASEO.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O09131-1 [UniParc]FASTAAdd to Basket

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    MSGESSRSLG KGSAPPGPVP EGQIRVYSMR FCPFAQRTLM VLKAKGIRHE    50
    VININLKNKP EWFFEKNPLG LVPVLENSQG HLVTESVITC EYLDEAYPEK 100
    KLFPDDPYKK ARQKMTLESF SKVPPLIASF VRSKRKEDSP NLREALENEF 150
    KKLEEGMDNY KSFLGGDSPS MVDYLTWPWF QRLEALELKE CLAHTPKLKL 200
    WMAAMQQDPV ASSHKIDAKT YREYLNLYLQ DSPEACDYGL 240
    Length:240
    Mass (Da):27,498
    Last modified:January 1, 1998 - v2
    Checksum:i17FEB52DB4BBE506
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80819 mRNA. Translation: AAB70110.1.
    AK027922 mRNA. Translation: BAC25667.1.
    AK146834 mRNA. Translation: BAE27469.1.
    AK168383 mRNA. Translation: BAE40311.1.
    BC085165 mRNA. Translation: AAH85165.1.
    CCDSiCCDS29893.1.
    RefSeqiNP_034492.1. NM_010362.2.
    UniGeneiMm.378931.

    Genome annotation databases

    EnsembliENSMUST00000026050; ENSMUSP00000026050; ENSMUSG00000025068.
    GeneIDi14873.
    KEGGimmu:14873.
    UCSCiuc008hvq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80819 mRNA. Translation: AAB70110.1 .
    AK027922 mRNA. Translation: BAC25667.1 .
    AK146834 mRNA. Translation: BAE27469.1 .
    AK168383 mRNA. Translation: BAE40311.1 .
    BC085165 mRNA. Translation: AAH85165.1 .
    CCDSi CCDS29893.1.
    RefSeqi NP_034492.1. NM_010362.2.
    UniGenei Mm.378931.

    3D structure databases

    ProteinModelPortali O09131.
    SMRi O09131. Positions 3-240.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O09131. 2 interactions.
    MINTi MINT-1868625.
    STRINGi 10090.ENSMUSP00000026050.

    PTM databases

    PhosphoSitei O09131.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00114285.

    Proteomic databases

    MaxQBi O09131.
    PaxDbi O09131.
    PRIDEi O09131.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026050 ; ENSMUSP00000026050 ; ENSMUSG00000025068 .
    GeneIDi 14873.
    KEGGi mmu:14873.
    UCSCi uc008hvq.1. mouse.

    Organism-specific databases

    CTDi 9446.
    MGIi MGI:1342273. Gsto1.

    Phylogenomic databases

    eggNOGi COG0625.
    GeneTreei ENSGT00390000005479.
    HOGENOMi HOG000006560.
    HOVERGENi HBG051853.
    InParanoidi O09131.
    KOi K00799.
    OMAi AYANEMP.
    OrthoDBi EOG71CFNG.
    PhylomeDBi O09131.
    TreeFami TF105325.

    Enzyme and pathway databases

    Reactomei REACT_215316. Glutathione conjugation.

    Miscellaneous databases

    NextBioi 287145.
    PROi O09131.
    SOURCEi Search...

    Gene expression databases

    Bgeei O09131.
    CleanExi MM_GSTO1.
    Genevestigatori O09131.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR005442. GST_omega.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view ]
    PRINTSi PR01625. GSTRNSFRASEO.
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cloning and characterization of a new stress response protein. A mammalian member of a family of theta class glutathione s-transferase-like proteins."
      Kodym R., Calkins P., Story M.D.
      J. Biol. Chem. 274:5131-5137(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Amnion.
    3. "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].
      Strain: C57BL/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiGSTO1_MOUSE
    AccessioniPrimary (citable) accession number: O09131
    Secondary accession number(s): Q3TH87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3