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Protein

Glutathione S-transferase Mu 5

Gene

Gstm5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Kineticsi

  1. KM=0.14 mM for glutathione1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei120 – 1201SubstrateBy similarity

    GO - Molecular functioni

    • glutathione transferase activity Source: MGI
    • protein homodimerization activity Source: MGI

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_316307. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase Mu 5 (EC:2.5.1.18)
    Alternative name(s):
    GST class-mu 5
    Gene namesi
    Name:Gstm5
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494 Componenti: Chromosome 2

    Organism-specific databases

    RGDi61964. Gstm5.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 225225Glutathione S-transferase Mu 5PRO_0000271421Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.Curated

    Proteomic databases

    PaxDbiQ9Z1B2.
    PRIDEiQ9Z1B2.

    2D gel databases

    World-2DPAGE0004:Q9Z1B2.

    Expressioni

    Tissue specificityi

    Expressed in testis and brain. Very low expression in liver, kidney, heart and lung.1 Publication

    Gene expression databases

    GenevisibleiQ9Z1B2. RN.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi249037. 1 interaction.
    STRINGi10116.ENSRNOP00000065389.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z1B2.
    SMRiQ9Z1B2. Positions 2-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 9288GST N-terminalAdd
    BLAST
    Domaini94 – 212119GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 122Glutathione bindingBy similarity
    Regioni50 – 545Glutathione bindingBy similarity
    Regioni63 – 642Glutathione bindingBy similarity
    Regioni76 – 772Glutathione bindingBy similarity

    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.
    InParanoidiQ9Z1B2.
    KOiK00799.
    OMAiCYSSDHE.
    OrthoDBiEOG7KH9M3.
    PhylomeDBiQ9Z1B2.
    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.

    Q9Z1B2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSCSKSMVLG YWDIRGLAHA IRMLLEFTDT SYEEKQYTCG EAPDYDRSQW
    60 70 80 90 100
    LDVKFKLDLD FPNLPYLMDG KNKITQSNAI LRYIARKHNM CGDTEEEKIR
    110 120 130 140 150
    VDIMENQIMD FRMQLVRLCY NSNHESLKPQ YLEQLPAQLK QFSLFLGKFT
    160 170 180 190 200
    WFAGEKLTFV DFLTYDVLDQ NRMFEPKCLD EFPNLKAFMC RFEALEKIAA
    210 220
    FLQSDRCFKM PINNKMAKWG NKSIC
    Length:225
    Mass (Da):26,629
    Last modified:January 23, 2007 - v3
    Checksum:i45A2DC2DDCE5ACA4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U86635 mRNA. Translation: AAD00603.1.
    RefSeqiNP_742035.1. NM_172038.1.
    XP_003749426.1. XM_003749378.3.
    UniGeneiRn.9158.

    Genome annotation databases

    EnsembliENSRNOT00000072342; ENSRNOP00000065389; ENSRNOG00000049743.
    ENSRNOT00000090430; ENSRNOP00000070934; ENSRNOG00000058357.
    GeneIDi100912430.
    64352.
    KEGGirno:100912430.
    rno:64352.
    UCSCiRGD:61964. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U86635 mRNA. Translation: AAD00603.1.
    RefSeqiNP_742035.1. NM_172038.1.
    XP_003749426.1. XM_003749378.3.
    UniGeneiRn.9158.

    3D structure databases

    ProteinModelPortaliQ9Z1B2.
    SMRiQ9Z1B2. Positions 2-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi249037. 1 interaction.
    STRINGi10116.ENSRNOP00000065389.

    2D gel databases

    World-2DPAGE0004:Q9Z1B2.

    Proteomic databases

    PaxDbiQ9Z1B2.
    PRIDEiQ9Z1B2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000072342; ENSRNOP00000065389; ENSRNOG00000049743.
    ENSRNOT00000090430; ENSRNOP00000070934; ENSRNOG00000058357.
    GeneIDi100912430.
    64352.
    KEGGirno:100912430.
    rno:64352.
    UCSCiRGD:61964. rat.

    Organism-specific databases

    CTDi2949.
    RGDi61964. Gstm5.

    Phylogenomic databases

    eggNOGiNOG300089.
    GeneTreeiENSGT00550000074559.
    HOGENOMiHOG000115735.
    HOVERGENiHBG106842.
    InParanoidiQ9Z1B2.
    KOiK00799.
    OMAiCYSSDHE.
    OrthoDBiEOG7KH9M3.
    PhylomeDBiQ9Z1B2.
    TreeFamiTF353040.

    Enzyme and pathway databases

    ReactomeiREACT_316307. Glutathione conjugation.

    Miscellaneous databases

    NextBioi613032.
    PROiQ9Z1B2.

    Gene expression databases

    GenevisibleiQ9Z1B2. RN.

    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]
    ProtoNetiSearch...

    Publicationsi

    1. "Rationale for reclassification of a distinctive subdivision of mammalian class Mu glutathione S-transferases that are primarily expressed in testis."
      Rowe J.D., Patskovsky Y.V., Patskovska L.N., Novikova E., Listowsky I.
      J. Biol. Chem. 273:9593-9601(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 6-27; 36-50; 57-71; 74-87; 89-120; 157-177; 179-186; 198-215 AND 219-224, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, KINETIC PARAMETERS.
      Strain: Sprague-Dawley.
      Tissue: Testis.
    2. Lubec G., Afjehi-Sadat L.
      Submitted (NOV-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 157-172, INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Spinal cord.

    Entry informationi

    Entry nameiGSTM5_RAT
    AccessioniPrimary (citable) accession number: Q9Z1B2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: January 23, 2007
    Last modified: July 22, 2015
    This is version 104 of the entry and version 3 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.