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P08010

- GSTM2_RAT

UniProt

P08010 - GSTM2_RAT

Protein

Glutathione S-transferase Mu 2

Gene

Gstm2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (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.

    Sites

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

    GO - Molecular functioni

    1. glutathione transferase activity Source: RGD
    2. protein homodimerization activity Source: RGD

    GO - Biological processi

    1. aging Source: RGD
    2. response to catechin Source: RGD
    3. response to genistein Source: RGD
    4. response to metal ion Source: RGD
    5. response to organic cyclic compound Source: RGD
    6. sensory perception of smell Source: UniProtKB-KW
    7. xenobiotic metabolic process Source: RGD

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Olfaction, Sensory transduction

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase Mu 2 (EC:2.5.1.18)
    Alternative name(s):
    GST 4-4
    GSTM2-2
    Glutathione S-transferase Yb-2
    Short name:
    GST Yb2
    Gene namesi
    Name:Gstm2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi2756. Gstm2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. plasma membrane Source: RGD
    3. protein complex Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 218217Glutathione S-transferase Mu 2PRO_0000185832Add
    BLAST

    Proteomic databases

    PaxDbiP08010.
    PRIDEiP08010.

    Expressioni

    Gene expression databases

    ArrayExpressiP08010.
    GenevestigatoriP08010.

    Interactioni

    Subunit structurei

    Homodimer or heterodimer.1 Publication

    Protein-protein interaction databases

    IntActiP08010. 1 interaction.

    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 – 403
    Helixi44 – 507
    Beta strandi60 – 656
    Beta strandi68 – 725
    Helixi73 – 8311
    Helixi91 – 11626
    Helixi120 – 14223
    Beta strandi150 – 1523
    Helixi155 – 17016
    Turni172 – 1776
    Helixi179 – 18911
    Helixi192 – 1987
    Beta strandi214 – 2163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B4PX-ray1.70A2-218[»]
    ProteinModelPortaliP08010.
    SMRiP08010. Positions 2-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08010.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8887GST N-terminalAdd
    BLAST
    Domaini90 – 214125GST 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

    eggNOGiNOG300089.
    GeneTreeiENSGT00550000074559.
    HOGENOMiHOG000115735.
    HOVERGENiHBG106842.
    InParanoidiP08010.
    KOiK00799.
    OMAiRITESWA.
    OrthoDBiEOG7KH9M3.
    PhylomeDBiP08010.
    TreeFamiTF353040.

    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.

    P08010-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPMTLGYWDI RGLAHAIRLF LEYTDTSYED KKYSMGDAPD YDRSQWLSEK    50
    FKLGLDFPNL PYLIDGSHKI TQSNAILRYL GRKHNLCGET EEERIRVDVL 100
    ENQAMDTRLQ LAMVCYSPDF ERKKPEYLEG LPEKMKLYSE FLGKQPWFAG 150
    NKITYVDFLV YDVLDQHRIF EPKCLDAFPN LKDFVARFEG LKKISDYMKS 200
    GRFLSKPIFA KMAFWNPK 218
    Length:218
    Mass (Da):25,703
    Last modified:January 23, 2007 - v2
    Checksum:iC23B30C171DB852F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471W → S AA sequence (PubMed:3699019)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02592 mRNA. Translation: AAA41285.1.
    M13590 mRNA. Translation: AAA42351.1.
    J03914 Genomic DNA. Translation: AAA41296.1.
    PIRiA29231. XURTG4.
    RefSeqiNP_803175.1. NM_177426.1.
    UniGeneiRn.625.

    Genome annotation databases

    EnsembliENSRNOT00000025939; ENSRNOP00000025939; ENSRNOG00000019094.
    GeneIDi24424.
    KEGGirno:24424.
    UCSCiRGD:2756. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02592 mRNA. Translation: AAA41285.1 .
    M13590 mRNA. Translation: AAA42351.1 .
    J03914 Genomic DNA. Translation: AAA41296.1 .
    PIRi A29231. XURTG4.
    RefSeqi NP_803175.1. NM_177426.1.
    UniGenei Rn.625.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B4P X-ray 1.70 A 2-218 [» ]
    ProteinModelPortali P08010.
    SMRi P08010. Positions 2-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08010. 1 interaction.

    Chemistry

    ChEMBLi CHEMBL2504.

    Proteomic databases

    PaxDbi P08010.
    PRIDEi P08010.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000025939 ; ENSRNOP00000025939 ; ENSRNOG00000019094 .
    GeneIDi 24424.
    KEGGi rno:24424.
    UCSCi RGD:2756. rat.

    Organism-specific databases

    CTDi 2946.
    RGDi 2756. Gstm2.

    Phylogenomic databases

    eggNOGi NOG300089.
    GeneTreei ENSGT00550000074559.
    HOGENOMi HOG000115735.
    HOVERGENi HBG106842.
    InParanoidi P08010.
    KOi K00799.
    OMAi RITESWA.
    OrthoDBi EOG7KH9M3.
    PhylomeDBi P08010.
    TreeFami TF353040.

    Miscellaneous databases

    EvolutionaryTracei P08010.
    NextBioi 603291.
    PROi P08010.

    Gene expression databases

    ArrayExpressi P08010.
    Genevestigatori P08010.

    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. "Gene expression of rat glutathione S-transferases. Evidence for gene conversion in the evolution of the Yb multigene family."
      Lai H.-C.J., Qian B., Grove G., Tu C.-P.D.
      J. Biol. Chem. 263:11389-11395(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cytosolic rat liver glutathione transferase 4-4. Primary structure of the protein reveals extensive differences between homologous glutathione transferases of classes alpha and mu."
      Alin P., Mannervik B., Joernvall H.
      Eur. J. Biochem. 156:343-350(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-218.
      Strain: Sprague-Dawley.
    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] OF 25-218.
    4. "Rat glutathione S-transferases supergene family. Characterization of an anionic Yb subunit cDNA clone."
      Lai H.-C.J., Tu C.-P.D.
      J. Biol. Chem. 261:13793-13799(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-218.
    5. "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 2-26.
    6. "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 2-28.
    7. "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 2-22.
      Strain: Wistar.
      Tissue: Olfactory epithelium.
    8. Lubec G., Afjehi-Sadat L., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 33-43; 137-144; 153-168 AND 174-182, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Spinal cord.
    9. "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 (1.7 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.

    Entry informationi

    Entry nameiGSTM2_RAT
    AccessioniPrimary (citable) accession number: P08010
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 140 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