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P00502

- GSTA1_RAT

UniProt

P00502 - GSTA1_RAT

Protein

Glutathione S-transferase alpha-1

Gene

Gsta1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91Glutathione1 Publication
    Binding sitei45 – 451Glutathione1 Publication
    Binding sitei55 – 551Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

    GO - Molecular functioni

    1. drug binding Source: RGD
    2. glutathione binding Source: RGD
    3. glutathione transferase activity Source: RGD

    GO - Biological processi

    1. aging Source: RGD
    2. response to drug Source: RGD
    3. response to nutrient levels Source: RGD
    4. xenobiotic catabolic process Source: RGD

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase alpha-1 (EC:2.5.1.18)
    Alternative name(s):
    GST 1-1
    GST 1a-1a
    GST A1-1
    GST B
    Glutathione S-transferase Ya-1
    Short name:
    GST Ya1
    Ligandin
    Cleaved into the following chain:
    Gene namesi
    Name:Gsta1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2753. Gsta1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. nuclear outer membrane Source: RGD
    3. nucleus Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 222222Glutathione S-transferase alpha-1PRO_0000185792Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 222221Glutathione S-transferase alpha-1, N-terminally processedPRO_0000423205Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP00502.
    PRIDEiP00502.

    PTM databases

    PhosphoSiteiP00502.

    Expressioni

    Gene expression databases

    GenevestigatoriP00502.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    MINTiMINT-4564141.
    STRINGi10116.ENSRNOP00000043510.

    Structurei

    Secondary structure

    1
    222
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 127
    Helixi16 – 2510
    Beta strandi31 – 355
    Helixi38 – 469
    Beta strandi57 – 604
    Beta strandi63 – 675
    Helixi68 – 7912
    Helixi86 – 10924
    Helixi114 – 1163
    Helixi117 – 13014
    Helixi132 – 14312
    Beta strandi146 – 1494
    Helixi155 – 17117
    Helixi172 – 1754
    Helixi179 – 19012
    Helixi192 – 1987
    Helixi211 – 2199

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EV4X-ray2.20A/C/D2-222[»]
    1EV9X-ray2.20A/C/D2-222[»]
    DisProtiDP00731.
    ProteinModelPortaliP00502.
    SMRiP00502. Positions 2-221.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00502.

    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.
    HOGENOMiHOG000115734.
    HOVERGENiHBG053749.
    InParanoidiP00502.
    KOiK00799.
    OrthoDBiEOG79CZ0K.
    PhylomeDBiP00502.
    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.

    P00502-1 [UniParc]FASTAAdd to Basket

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    MSGKPVLHYF NARGRMECIR WLLAAAGVEF DEKFIQSPED LEKLKKDGNL    50
    MFDQVPMVEI DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL 100
    DLTEMIMQLV ICPPDQKEAK TALAKDRTKN RYLPAFEKVL KSHGQDYLVG 150
    NRLTRVDIHL LELLLYVEEF DASLLTSFPL LKAFKSRISS LPNVKKFLQP 200
    GSQRKLPVDA KQIEEARKIF KF 222
    Length:222
    Mass (Da):25,607
    Last modified:January 23, 2007 - v3
    Checksum:iAE43A1BEBE8549CF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti152 – 1521R → K(PubMed:6201485)Curated
    Sequence conflicti152 – 1521R → K(PubMed:6273441)Curated
    Sequence conflicti208 – 2081V → M in AAA41283. (PubMed:6201485)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01931 mRNA. Translation: AAA41283.1.
    BC078706 mRNA. Translation: AAH78706.1.
    PIRiA24735.
    A92479. XURTG.
    RefSeqiNP_058709.2. NM_017013.4.
    UniGeneiRn.144550.

    Genome annotation databases

    GeneIDi24422.
    KEGGirno:24422.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01931 mRNA. Translation: AAA41283.1 .
    BC078706 mRNA. Translation: AAH78706.1 .
    PIRi A24735.
    A92479. XURTG.
    RefSeqi NP_058709.2. NM_017013.4.
    UniGenei Rn.144550.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EV4 X-ray 2.20 A/C/D 2-222 [» ]
    1EV9 X-ray 2.20 A/C/D 2-222 [» ]
    DisProti DP00731.
    ProteinModelPortali P00502.
    SMRi P00502. Positions 2-221.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4564141.
    STRINGi 10116.ENSRNOP00000043510.

    Chemistry

    ChEMBLi CHEMBL2390.

    PTM databases

    PhosphoSitei P00502.

    Proteomic databases

    PaxDbi P00502.
    PRIDEi P00502.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24422.
    KEGGi rno:24422.

    Organism-specific databases

    CTDi 2939.
    RGDi 2753. Gsta1.

    Phylogenomic databases

    eggNOGi NOG266414.
    HOGENOMi HOG000115734.
    HOVERGENi HBG053749.
    InParanoidi P00502.
    KOi K00799.
    OrthoDBi EOG79CZ0K.
    PhylomeDBi P00502.
    TreeFami TF105321.

    Miscellaneous databases

    EvolutionaryTracei P00502.
    NextBioi 603283.

    Gene expression databases

    Genevestigatori P00502.

    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. "The nucleotide sequence of a rat liver glutathione S-transferase subunit cDNA clone."
      Lai H.-C.J., Li N.-Q., Weiss M.J., Reddy C.C., Tu C.-P.D.
      J. Biol. Chem. 259:5536-5542(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Liver.
    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: Kidney.
    3. "Rat glutathione S-transferase. Cloning of double-stranded cDNA and induction of its mRNA."
      Kalinyak J.E., Taylor J.M.
      J. Biol. Chem. 257:523-530(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-197.
    4. "Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y."
      Adman E.T., Le Trong I., Stenkamp R.E., Nieslanik B.S., Dietze E.C., Tai G., Ibarra C., Atkins W.M.
      Proteins 42:192-200(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, SUBUNIT.

    Entry informationi

    Entry nameiGSTA1_RAT
    AccessioniPrimary (citable) accession number: P00502
    Secondary accession number(s): Q6AZ72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In addition to its enzymatic activity, the homodimer of Ya chains, called ligandin, binds various organic anions, xenobiotics, and azocarcinogen dyes.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3