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Q9N1F5

- GSTO1_PIG

UniProt

Q9N1F5 - GSTO1_PIG

Protein

Glutathione S-transferase omega-1

Gene

GSTO1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (31 Jan 2002)
      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. 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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 14

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    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 – 241240Glutathione S-transferase omega-1PRO_0000185886Add
    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

    PaxDbiQ9N1F5.

    Expressioni

    Tissue specificityi

    Most abundant in the liver and skeletal muscle; also expressed in heart, diaphragm, colon, thymus, kidney, lung, ovaries, spleen, intestine and pancreas.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000011310.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9N1F5.
    SMRiQ9N1F5. Positions 5-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 10180GST N-terminalAdd
    BLAST
    Domaini106 – 225120GST 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.
    KOiK00799.
    OMAiHKAYLDS.
    OrthoDBiEOG71CFNG.
    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.

    Q9N1F5-1 [UniParc]FASTAAdd to Basket

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    MSGGSARSLG KGSAPPGPVP EGLIRVYSMR FCPFAQRTLL VLNAKGIRHQ    50
    VININLKNKP EWFFQKNPSG LVPVLENSQG QLIYESAITC EYLDEAYPGK 100
    KLLPDDPYEK ACQKMVFELS SKVPPLLIRF IRRENEADCS GLKEELRKEF 150
    SKLEEVLTKK KTTYFGGSSL SMIDYLIWPW FERLEALELN ECIDHTPKLK 200
    LWMAAMMKDP AVSALHIEPR DLRAFNDLYL QNSPEACDYG L 241
    Length:241
    Mass (Da):27,419
    Last modified:January 31, 2002 - v2
    Checksum:iAA50EE81C70433A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti139 – 1391C → Y AA sequence (PubMed:11485575)Curated
    Sequence conflicti158 – 1581T → Q AA sequence (PubMed:11485575)Curated

    Mass spectrometryi

    Molecular mass is 27328±3 Da from positions 2 - 241. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF188838 mRNA. Translation: AAF71994.2.
    RefSeqiNP_999215.1. NM_214050.1.
    UniGeneiSsc.58505.

    Genome annotation databases

    EnsembliENSSSCT00000011607; ENSSSCP00000011305; ENSSSCG00000022351.
    GeneIDi397117.
    KEGGissc:397117.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF188838 mRNA. Translation: AAF71994.2 .
    RefSeqi NP_999215.1. NM_214050.1.
    UniGenei Ssc.58505.

    3D structure databases

    ProteinModelPortali Q9N1F5.
    SMRi Q9N1F5. Positions 5-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000011310.

    Proteomic databases

    PaxDbi Q9N1F5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000011607 ; ENSSSCP00000011305 ; ENSSSCG00000022351 .
    GeneIDi 397117.
    KEGGi ssc:397117.

    Organism-specific databases

    CTDi 9446.

    Phylogenomic databases

    eggNOGi COG0625.
    GeneTreei ENSGT00390000005479.
    HOGENOMi HOG000006560.
    HOVERGENi HBG051853.
    KOi K00799.
    OMAi HKAYLDS.
    OrthoDBi EOG71CFNG.
    TreeFami TF105325.

    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. "Purification and characterization of a glutathione S-transferase Omega in pig: evidence for two distinct organ-specific transcripts."
      Rouimi P., Anglade P., Benzekri A., Costet P., Debrauwer L., Pineau T., Tulliez J.
      Biochem. J. 358:257-262(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-31; 58-83; 101-110; 115-147; 149-160; 162-190; 201-228 AND 235-241, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY.
      Tissue: Liver.

    Entry informationi

    Entry nameiGSTO1_PIG
    AccessioniPrimary (citable) accession number: Q9N1F5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: January 31, 2002
    Last modified: October 1, 2014
    This is version 93 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