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P13745

- GSTA1_MOUSE

UniProt

P13745 - GSTA1_MOUSE

Protein

Glutathione S-transferase A1

Gene

Gsta1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91Glutathione
    Binding sitei45 – 451Glutathione
    Binding sitei55 – 551Glutathione; via amide nitrogen and carbonyl oxygen

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB

    GO - Biological processi

    1. glutathione metabolic process Source: UniProtKB
    2. response to stilbenoid Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_215316. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase A1 (EC:2.5.1.18)
    Alternative name(s):
    GST class-alpha member 1
    Glutathione S-transferase Ya
    Glutathione S-transferase Ya1
    Cleaved into the following chain:
    Gene namesi
    Name:Gsta1
    Synonyms:Gsta, Gstya
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1095417. Gsta1.

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 223223Glutathione S-transferase A1PRO_0000185788Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 223222Glutathione S-transferase A1, N-terminally processedPRO_0000423204Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP13745.
    PaxDbiP13745.
    PRIDEiP13745.

    PTM databases

    PhosphoSiteiP13745.

    Expressioni

    Inductioni

    Induced in the liver by beta-naphthoflavone (BNF) and 23-t-butyl-4-hydroxyanisole (BHA).1 Publication

    Gene expression databases

    BgeeiP13745.
    CleanExiMM_GSTA1.
    GenevestigatoriP13745.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP13745. 3 interactions.
    MINTiMINT-4096961.

    Structurei

    Secondary structure

    1
    223
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 127
    Turni14 – 163
    Helixi17 – 259
    Beta strandi31 – 355
    Helixi38 – 469
    Beta strandi57 – 604
    Beta strandi63 – 675
    Helixi68 – 7811
    Helixi86 – 10823
    Helixi109 – 1113
    Turni114 – 1163
    Helixi117 – 13014
    Helixi132 – 14312
    Beta strandi146 – 1494
    Helixi155 – 17117
    Helixi172 – 1754
    Helixi179 – 18911
    Helixi192 – 1987
    Helixi210 – 2178

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F3AX-ray1.90A/B2-223[»]
    1F3BX-ray2.00A/B2-223[»]
    ProteinModelPortaliP13745.
    SMRiP13745. Positions 2-222.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13745.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8381GST N-terminalAdd
    BLAST
    Domaini85 – 208124GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni67 – 682Glutathione binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG266414.
    GeneTreeiENSGT00670000097856.
    HOGENOMiHOG000115734.
    HOVERGENiHBG053749.
    InParanoidiA2RTN4.
    KOiK00799.
    OMAiILHYSND.
    OrthoDBiEOG79CZ0K.
    PhylomeDBiP13745.
    TreeFamiTF105321.

    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.
    IPR003080. GST_alpha.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01266. GSTRNSFRASEA.
    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.

    P13745-1 [UniParc]FASTAAdd to Basket

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    MAGKPVLHYF NARGRMECIR WLLAAAGVEF EEKFIQSPED LEKLKKDGNL    50
    MFDQVPMVEI DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYSEGIL 100
    DLTEMIGQLV LCPPDQREAK TALAKDRTKN RYLPAFEKVL KSHGQDYLVG 150
    NRLTRVDIHL LEVLLYVEEF DASLLTPFPL LKAFKSRISS LPNVKKFLQP 200
    GSQRKPPMDA KQIQEARKAF KIQ 223
    Length:223
    Mass (Da):25,608
    Last modified:January 23, 2007 - v2
    Checksum:iA348A07133FBEC1D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19256
    , M19251, M19252, M19253, M19254, M19255 Genomic DNA. Translation: AAA37750.1. Sequence problems.
    BC132572 mRNA. Translation: AAI32573.1.
    BC132576 mRNA. Translation: AAI32577.1.
    CCDSiCCDS23358.1.
    PIRiA27848.
    RefSeqiNP_032207.3. NM_008181.3.
    UniGeneiMm.467426.

    Genome annotation databases

    EnsembliENSMUST00000098537; ENSMUSP00000096139; ENSMUSG00000074183.
    GeneIDi14857.
    KEGGimmu:14857.
    UCSCiuc009qtz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19256
    , M19251 , M19252 , M19253 , M19254 , M19255 Genomic DNA. Translation: AAA37750.1 . Sequence problems.
    BC132572 mRNA. Translation: AAI32573.1 .
    BC132576 mRNA. Translation: AAI32577.1 .
    CCDSi CCDS23358.1.
    PIRi A27848.
    RefSeqi NP_032207.3. NM_008181.3.
    UniGenei Mm.467426.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F3A X-ray 1.90 A/B 2-223 [» ]
    1F3B X-ray 2.00 A/B 2-223 [» ]
    ProteinModelPortali P13745.
    SMRi P13745. Positions 2-222.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P13745. 3 interactions.
    MINTi MINT-4096961.

    Chemistry

    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei P13745.

    Proteomic databases

    MaxQBi P13745.
    PaxDbi P13745.
    PRIDEi P13745.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000098537 ; ENSMUSP00000096139 ; ENSMUSG00000074183 .
    GeneIDi 14857.
    KEGGi mmu:14857.
    UCSCi uc009qtz.1. mouse.

    Organism-specific databases

    CTDi 2938.
    MGIi MGI:1095417. Gsta1.

    Phylogenomic databases

    eggNOGi NOG266414.
    GeneTreei ENSGT00670000097856.
    HOGENOMi HOG000115734.
    HOVERGENi HBG053749.
    InParanoidi A2RTN4.
    KOi K00799.
    OMAi ILHYSND.
    OrthoDBi EOG79CZ0K.
    PhylomeDBi P13745.
    TreeFami TF105321.

    Enzyme and pathway databases

    Reactomei REACT_215316. Glutathione conjugation.

    Miscellaneous databases

    EvolutionaryTracei P13745.
    NextBioi 287087.
    PROi P13745.
    SOURCEi Search...

    Gene expression databases

    Bgeei P13745.
    CleanExi MM_GSTA1.
    Genevestigatori P13745.

    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.
    IPR003080. GST_alpha.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01266. GSTRNSFRASEA.
    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. "Mouse glutathione S-transferase Ya subunit: gene structure and sequence."
      Daniel V., Sharon R., Tichauer Y., Sarid S.
      DNA 6:317-324(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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].
      Tissue: Brain.
    3. "Regulation of mouse glutathione S-transferases by chemoprotectors. Molecular evidence for the existence of three distinct alpha-class glutathione S-transferase subunits, Ya1, Ya2, and Ya3, in mouse liver."
      McLellan L.I., Kerr L.A., Cronshaw A.D., Hayes J.D.
      Biochem. J. 276:461-469(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-36; 51-59; 63-165 AND 208-223, INDUCTION.
      Tissue: Liver.
    4. "Residue R216 and catalytic efficiency of a murine class alpha glutathione S-transferase toward benzo[a]pyrene 7(R),8(S)-diol 9(S), 10(R)-epoxide."
      Gu Y., Singh S.V., Ji X.
      Biochemistry 39:12552-12557(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND SUBSTRATE, SUBUNIT.

    Entry informationi

    Entry nameiGSTA1_MOUSE
    AccessioniPrimary (citable) accession number: P13745
    Secondary accession number(s): A2RTN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3