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P04905

- GSTM1_RAT

UniProt

P04905 - GSTM1_RAT

Protein

Glutathione S-transferase Mu 1

Gene

Gstm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (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. The olfactory GST may be crucial for the acuity of the olfactory process.

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei116 – 1161SubstrateBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: RGD
    2. nickel cation binding Source: RGD
    3. protein homodimerization activity Source: RGD
    4. steroid binding Source: RGD

    GO - Biological processi

    1. glutathione metabolic process Source: UniProtKB
    2. response to amino acid Source: RGD
    3. response to antibiotic Source: RGD
    4. response to axon injury Source: RGD
    5. response to drug Source: RGD
    6. response to ethanol Source: RGD
    7. response to lead ion Source: RGD
    8. response to lithium ion Source: RGD
    9. response to metal ion Source: RGD
    10. sensory perception of smell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Olfaction, Sensory transduction

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase Mu 1 (EC:2.5.1.18)
    Alternative name(s):
    GST 3-3
    GSTM1-1
    Glutathione S-transferase Yb-1
    Short name:
    GST Yb1
    Gene namesi
    Name:Gstm1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2755. Gstm1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular region Source: RGD
    3. protein complex Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71Y → F or L: Reduces catalytic activity about 100-fold. 1 Publication
    Mutagenesisi87 – 871C → S: No change in activity. 1 Publication
    Mutagenesisi116 – 1161Y → F: Reduces enzyme activity about 100-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed6 Publications
    Chaini2 – 218217Glutathione S-transferase Mu 1PRO_0000185831Add
    BLAST

    Proteomic databases

    PaxDbiP04905.
    PRIDEiP04905.

    PTM databases

    PhosphoSiteiP04905.

    Expressioni

    Gene expression databases

    GenevestigatoriP04905.

    Interactioni

    Subunit structurei

    Homodimer or heterodimer.3 Publications

    Protein-protein interaction databases

    MINTiMINT-4564586.

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 108
    Turni12 – 143
    Helixi15 – 239
    Beta strandi28 – 336
    Turni38 – 414
    Helixi44 – 474
    Turni48 – 514
    Beta strandi60 – 656
    Beta strandi68 – 725
    Helixi73 – 8311
    Helixi91 – 11525
    Helixi120 – 14223
    Beta strandi146 – 1527
    Helixi155 – 17016
    Turni172 – 1754
    Helixi179 – 18911
    Helixi192 – 1987
    Beta strandi200 – 2023
    Beta strandi213 – 2164

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GSBX-ray2.50A/B/C/D2-218[»]
    1GSCX-ray2.50A/B/C/D2-218[»]
    1MTCX-ray2.20A/B2-218[»]
    2GSTX-ray1.80A/B2-218[»]
    3FYGX-ray2.20A/B2-218[»]
    3GSTX-ray1.90A/B2-218[»]
    4GSTX-ray1.90A/B2-218[»]
    5FWGX-ray2.00A/B2-218[»]
    5GSTX-ray2.00A/B2-218[»]
    6GSTX-ray2.20A/B2-218[»]
    6GSUX-ray1.85A/B2-218[»]
    6GSVX-ray1.75A/B2-218[»]
    6GSWX-ray1.85A/B2-218[»]
    6GSXX-ray1.91A/B2-218[»]
    6GSYX-ray2.20A/B2-218[»]
    ProteinModelPortaliP04905.
    SMRiP04905. Positions 2-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04905.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8887GST N-terminalAdd
    BLAST
    Domaini90 – 208119GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 82Glutathione binding
    Regioni43 – 508Glutathione binding
    Regioni59 – 602Glutathione binding
    Regioni72 – 732Glutathione binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiKOG1695.
    HOGENOMiHOG000115735.
    HOVERGENiHBG106842.
    InParanoidiP04905.
    KOiK00799.
    PhylomeDBiP04905.

    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.
    IPR003081. GST_mu.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01267. GSTRNSFRASEM.
    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.

    P04905-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPMILGYWNV RGLTHPIRLL LEYTDSSYEE KRYAMGDAPD YDRSQWLNEK    50
    FKLGLDFPNL PYLIDGSRKI TQSNAIMRYL ARKHHLCGET EEERIRADIV 100
    ENQVMDNRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG 150
    DKVTYVDFLA YDILDQYHIF EPKCLDAFPN LKDFLARFEG LKKISAYMKS 200
    SRYLSTPIFS KLAQWSNK 218
    Length:218
    Mass (Da):25,914
    Last modified:January 23, 2007 - v2
    Checksum:i1A8E80D09A5CACA8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti199 – 2002KS → NC in AAA41287. (PubMed:3840477)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04229 mRNA. Translation: CAA27811.1.
    M11719 mRNA. Translation: AAA41287.1.
    J02810 mRNA. Translation: AAA41293.1.
    BC063172 mRNA. Translation: AAH63172.1.
    PIRiA29794.
    RefSeqiNP_058710.1. NM_017014.1.
    UniGeneiRn.202944.

    Genome annotation databases

    GeneIDi24423.
    KEGGirno:24423.
    UCSCiRGD:2755. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04229 mRNA. Translation: CAA27811.1 .
    M11719 mRNA. Translation: AAA41287.1 .
    J02810 mRNA. Translation: AAA41293.1 .
    BC063172 mRNA. Translation: AAH63172.1 .
    PIRi A29794.
    RefSeqi NP_058710.1. NM_017014.1.
    UniGenei Rn.202944.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GSB X-ray 2.50 A/B/C/D 2-218 [» ]
    1GSC X-ray 2.50 A/B/C/D 2-218 [» ]
    1MTC X-ray 2.20 A/B 2-218 [» ]
    2GST X-ray 1.80 A/B 2-218 [» ]
    3FYG X-ray 2.20 A/B 2-218 [» ]
    3GST X-ray 1.90 A/B 2-218 [» ]
    4GST X-ray 1.90 A/B 2-218 [» ]
    5FWG X-ray 2.00 A/B 2-218 [» ]
    5GST X-ray 2.00 A/B 2-218 [» ]
    6GST X-ray 2.20 A/B 2-218 [» ]
    6GSU X-ray 1.85 A/B 2-218 [» ]
    6GSV X-ray 1.75 A/B 2-218 [» ]
    6GSW X-ray 1.85 A/B 2-218 [» ]
    6GSX X-ray 1.91 A/B 2-218 [» ]
    6GSY X-ray 2.20 A/B 2-218 [» ]
    ProteinModelPortali P04905.
    SMRi P04905. Positions 2-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4564586.

    Chemistry

    ChEMBLi CHEMBL2209.

    PTM databases

    PhosphoSitei P04905.

    Proteomic databases

    PaxDbi P04905.
    PRIDEi P04905.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24423.
    KEGGi rno:24423.
    UCSCi RGD:2755. rat.

    Organism-specific databases

    CTDi 2944.
    RGDi 2755. Gstm1.

    Phylogenomic databases

    eggNOGi KOG1695.
    HOGENOMi HOG000115735.
    HOVERGENi HBG106842.
    InParanoidi P04905.
    KOi K00799.
    PhylomeDBi P04905.

    Miscellaneous databases

    EvolutionaryTracei P04905.
    NextBioi 603287.

    Gene expression databases

    Genevestigatori P04905.

    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.
    IPR003081. GST_mu.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01267. GSTRNSFRASEM.
    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. "Cloning and sequence analysis of a cDNA for a rat liver glutathione S-transferase Yb subunit."
      Lai H.-C.J., Grove G., Tu C.-P.D.
      Nucleic Acids Res. 14:6101-6114(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Rat liver glutathione S-transferases. Nucleotide sequence analysis of a Yb1 cDNA clone and prediction of the complete amino acid sequence of the Yb1 subunit."
      Ding G.J.-F., Lu A.Y.H., Pickett C.B.
      J. Biol. Chem. 260:13268-13271(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Rat liver glutathione S-transferases. DNA sequence analysis of a Yb2 cDNA clone and regulation of the Yb1 and Yb2 mRNAs by phenobarbital."
      Ding G.J.-F., Ding V.D.-H., Rodkey J.A., Bennett C.D., Lu A.Y.H., Pickett C.B.
      J. Biol. Chem. 261:7952-7957(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-24, SUBUNIT.
    4. "Identification of glutathione S-transferase Yb1 mRNA as the androgen-repressed mRNA by cDNA cloning and sequence analysis."
      Chang C., Saltzman A.G., Sorensen N.S., Hiipakka R.A., Liao S.
      J. Biol. Chem. 262:11901-11903(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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: Pituitary.
    6. "Identification of Tyr115 labeled by S-(4-bromo-2,3-dioxobutyl)glutathione in the hydrophobic substrate binding site of glutathione S-transferase, isoenzyme 3-3."
      Katusz R.M., Bono B., Colman R.F.
      Arch. Biochem. Biophys. 298:667-677(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20; 83-96 AND 109-122.
    7. "Expression of Yb1 glutathione S-transferase using a baculovirus expression system."
      Hsieh J.C., Liu L.F., Chen W.L., Tam M.F.
      Biochem. Biophys. Res. Commun. 162:1147-1154(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21 AND 212-218.
    8. "Identification of rat liver glutathione S-transferase Yb subunits by partial N-terminal sequencing after electroblotting of proteins onto a polyvinylidene difluoride membrane from an analytical isoelectric focusing gel."
      Chang L.H., Hsieh J.C., Chen W.L., Tam M.F.
      Electrophoresis 11:589-593(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-26.
    9. "Glutathione S-transferases in rat olfactory epithelium: purification, molecular properties and odorant biotransformation."
      Ben-Arie N., Khen M., Lancet D.
      Biochem. J. 292:379-384(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-24.
      Strain: Wistar.
      Tissue: Olfactory epithelium.
    10. "Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties."
      Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H.
      Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-20.
    11. Lubec G., Chen W.-Q., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 19-32; 33-50; 53-68; 70-78; 97-108; 137-144; 174-187 AND 203-218, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Hippocampus.
    12. "Cysteine-86 is not needed for the enzymic activity of glutathione S-transferase 3-3."
      Hsieh J.-C., Huang S.-C., Chen W.-L., Lai Y.-C., Tam M.F.
      Biochem. J. 278:293-297(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-87.
    13. "The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolution."
      Ji X., Zhang P., Armstrong R.N., Gilliland G.L.
      Biochemistry 31:10169-10184(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
    14. "New crystal forms of a mu-class glutathione S-transferase from rat liver."
      Fu J.-H., Rose J., Tam M.F., Wang B.-C.
      Acta Crystallogr. D 50:219-224(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    15. "Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene."
      Ji X., Johnson W.W., Sesay M.A., Dickert L., Prasad S.M., Ammon H.L., Armstrong R.N., Gilliland G.L.
      Biochemistry 33:1043-1052(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-116.
    16. "First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase."
      Xiao G., Liu S., Ji X., Johnson W.W., Chen J., Parsons J.F., Stevens W.J., Gilliland G.L., Armstrong R.N.
      Biochemistry 35:4753-4765(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT PHE-7 IN COMPLEXES WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-7.

    Entry informationi

    Entry nameiGSTM1_RAT
    AccessioniPrimary (citable) accession number: P04905
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Yb subclass selectively binds steroid hormones.

    Keywords - Technical termi

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