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Q9Z339

- GSTO1_RAT

UniProt

Q9Z339 - GSTO1_RAT

Protein

Glutathione S-transferase omega-1

Gene

Gsto1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (24 Jan 2001)
      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: RGD
    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 biosynthetic process Source: RGD
    3. L-ascorbic acid metabolic process Source: UniProtKB
    4. xenobiotic catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    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
    Gene namesi
    Name:Gsto1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi70952. Gsto1.

    Subcellular locationi

    GO - Cellular componenti

    1. axon Source: RGD
    2. basement membrane Source: RGD
    3. cell body Source: RGD
    4. cytoplasm Source: RGD
    5. cytosol Source: RGD
    6. myelin sheath Source: RGD
    7. nuclear membrane Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 241240Glutathione S-transferase omega-1PRO_0000185887Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei57 – 571N6-acetyllysineBy similarity
    Modified residuei143 – 1431N6-acetyllysineBy similarity
    Modified residuei148 – 1481N6-acetyllysineBy similarity
    Modified residuei152 – 1521N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9Z339.
    PRIDEiQ9Z339.

    2D gel databases

    World-2DPAGE0004:Q9Z339.

    PTM databases

    PhosphoSiteiQ9Z339.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9Z339.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    MINTiMINT-4569802.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z339.
    SMRiQ9Z339. Positions 5-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 10180GST N-terminalAdd
    BLAST
    Domaini106 – 228123GST 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.
    HOGENOMiHOG000006560.
    HOVERGENiHBG051853.
    InParanoidiQ9Z339.
    PhylomeDBiQ9Z339.

    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.

    Q9Z339-1 [UniParc]FASTAAdd to Basket

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    MSGASARSLG KGSAPPGPVP EGQIRVYSMR FCPFAQRTLM VLKAKGIRHE    50
    IININLKNKP EWFFEKNPFG LVPVLENTQG HLITESVITC EYLDEAYPEK 100
    KLFPDDPYEK ACQKMTFELF SKVPSLVTSF IRAKRKEDHP GIKEELKKEF 150
    SKLEEAMANK RTAFFGGNSL SMIDYLIWPW FQRLEALELN ECIDHTPKLK 200
    LWMATMQEDP VASSHFIDAK TYRDYLSLYL QDSPEACDYG L 241
    Length:241
    Mass (Da):27,669
    Last modified:January 24, 2001 - v2
    Checksum:i31EAC5A7CAF22BC6
    GO

    Sequence cautioni

    The sequence BAA34217.1 differs from that shown. Reason: Frameshift at position 23.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008807 mRNA. Translation: BAA34217.1. Frameshift.
    UniGeneiRn.25166.

    Genome annotation databases

    UCSCiRGD:70952. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008807 mRNA. Translation: BAA34217.1 . Frameshift.
    UniGenei Rn.25166.

    3D structure databases

    ProteinModelPortali Q9Z339.
    SMRi Q9Z339. Positions 5-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4569802.

    PTM databases

    PhosphoSitei Q9Z339.

    2D gel databases

    World-2DPAGE 0004:Q9Z339.

    Proteomic databases

    PaxDbi Q9Z339.
    PRIDEi Q9Z339.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:70952. rat.

    Organism-specific databases

    RGDi 70952. Gsto1.

    Phylogenomic databases

    eggNOGi COG0625.
    HOGENOMi HOG000006560.
    HOVERGENi HBG051853.
    InParanoidi Q9Z339.
    PhylomeDBi Q9Z339.

    Miscellaneous databases

    PROi Q9Z339.

    Gene expression databases

    Genevestigatori Q9Z339.

    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. "Molecular cloning and functional expression of rat liver glutathione-dependent dehydroascorbate reductase."
      Ishikawa T., Casini A.F., Nishikimi M.
      J. Biol. Chem. 273:28708-28712(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. Lubec G., Diao W., Kang S.U., Lubec S.
      Submitted (SEP-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 38-43 AND 123-132, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Hippocampus.
    3. "Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver."
      Maellaro E., Del Bello B., Sugherini L., Santucci A., Comporti M., Casini A.F.
      Biochem. J. 301:471-476(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Tissue: Liver.

    Entry informationi

    Entry nameiGSTO1_RAT
    AccessioniPrimary (citable) accession number: Q9Z339
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 104 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3