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}.
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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 Genevisible; O35660; MM.
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.
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
//
