ID   GSTM6_MOUSE             Reviewed;         218 AA.
AC   O35660; O35661; Q8K0C3;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 4.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Glutathione S-transferase Mu 6;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-mu 6;
DE   AltName: Full=Glutathione-S-transferase class M5;
GN   Name=Gstm6; Synonyms=Gstm5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv, C57BL/6J, and FVB/NJ; TISSUE=Liver;
RX   PubMed=9480867; DOI=10.1042/bj3300623;
RA   De Bruin W.C.C., te Morsche R.H.M., Wagenmans M.J.M., Alferink J.C.,
RA   Townsend A.J., Wieringa B., Peters W.H.M.;
RT   "Identification of a novel murine glutathione S-transferase class mu
RT   gene.";
RL   Biochem. J. 330:623-626(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, stomach and small intestine.
CC       Not expressed in spleen, kidney, colon, heart, muscle, brain or lung.
CC       {ECO:0000269|PubMed:9480867}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ000413; CAA04061.1; -; mRNA.
DR   EMBL; AJ000412; CAA04060.1; -; Genomic_DNA.
DR   EMBL; AC079042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC031818; AAH31818.1; -; mRNA.
DR   CCDS; CCDS38596.1; -.
DR   RefSeq; NP_032210.3; NM_008184.3.
DR   AlphaFoldDB; O35660; -.
DR   SMR; O35660; -.
DR   BioGRID; 200099; 2.
DR   STRING; 10090.ENSMUSP00000102296; -.
DR   iPTMnet; O35660; -.
DR   PhosphoSitePlus; O35660; -.
DR   SwissPalm; O35660; -.
DR   jPOST; O35660; -.
DR   PaxDb; 10090-ENSMUSP00000102295; -.
DR   ProteomicsDB; 271181; -.
DR   DNASU; 14867; -.
DR   Ensembl; ENSMUST00000106685.9; ENSMUSP00000102296.3; ENSMUSG00000068762.12.
DR   GeneID; 14867; -.
DR   KEGG; mmu:14867; -.
DR   AGR; MGI:1309467; -.
DR   CTD; 14867; -.
DR   MGI; MGI:1309467; Gstm6.
DR   VEuPathDB; HostDB:ENSMUSG00000068762; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000160258; -.
DR   HOGENOM; CLU_039475_2_0_1; -.
DR   InParanoid; O35660; -.
DR   OMA; WPVWSEL; -.
DR   OrthoDB; 5488107at2759; -.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   BioGRID-ORCS; 14867; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Gstm6; mouse.
DR   PRO; PR:O35660; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; O35660; Protein.
DR   Bgee; ENSMUSG00000068762; Expressed in duodenum and 103 other cell types or tissues.
DR   ExpressionAtlas; O35660; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0043295; F:glutathione binding; ISO:MGI.
DR   GO; GO:0004364; F:glutathione transferase activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   CDD; cd03209; GST_C_Mu; 1.
DR   CDD; cd03075; GST_N_Mu; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR003081; GST_mu.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF211; GLUTATHIONE S-TRANSFERASE MU 6; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01267; GSTRNSFRASEM.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   Genevisible; O35660; MM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..218
FT                   /note="Glutathione S-transferase Mu 6"
FT                   /id="PRO_0000185830"
FT   DOMAIN          1..88
FT                   /note="GST N-terminal"
FT   DOMAIN          90..208
FT                   /note="GST C-terminal"
FT   BINDING         7..8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         46..50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         59..60
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         72..73
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        31
FT                   /note="K -> R (in Ref. 1; CAA04060/CAA04061)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="D -> G (in Ref. 1; CAA04060)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102..103
FT                   /note="KQ -> NR (in Ref. 1; CAA04061)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   218 AA;  25621 MW;  DEA0AF7056F88638 CRC64;
     MPVTLGYWDI RGLGHAIRLL LEYTETGYEE KRYAMGDAPD YDRSQWLNDK FKLDLDFPNL
     PYLIDGSHKV TQSNAILRYL GRKHNLCGET EEERIRVDIL EKQVMDTRIQ MGMLCYSADF
     EKRKPEFLKG LPDQLKLYSE FLGKQPWFAG DKITFADFLV YDVLDQHRMF EPTCLDAFPN
     LKDFMARFEG LRKISAYMKT SRFLPSPVYL KQATWGNE
//