GSTM1_MOUSE
ID GSTM1_MOUSE Reviewed; 218 AA.
AC P10649; A2AE90; Q58ET5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Glutathione S-transferase Mu 1 {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P09488};
DE AltName: Full=GST 1-1;
DE AltName: Full=GST class-mu 1;
DE AltName: Full=Glutathione S-transferase GT8.7;
DE AltName: Full=pmGT10;
GN Name=Gstm1 {ECO:0000312|MGI:MGI:95860};
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 [MRNA].
RX PubMed=3417659; DOI=10.1016/s0021-9258(18)37708-1;
RA Pearson W.R., Reinhart J., Sisk S.C., Anderson K.S., Adler P.N.;
RT "Tissue-specific induction of murine glutathione transferase mRNAs by
RT butylated hydroxyanisole.";
RL J. Biol. Chem. 263:13324-13332(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2689439; DOI=10.1016/s0021-9258(20)88223-4;
RA Townsend A.J., Goldsmith M.E., Pickett C.B., Cowan K.H.;
RT "Isolation, characterization, and expression in Escherichia coli of two
RT murine Mu class glutathione S-transferase cDNAs homologous to the rat
RT subunits 3 (Yb1) and 4 (Yb2).";
RL J. Biol. Chem. 264:21582-21590(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8512323; DOI=10.1006/abbi.1993.1299;
RA Reinhart J., Pearson W.R.;
RT "The structure of two murine class-mu glutathione transferase genes
RT coordinately induced by butylated hydroxyanisole.";
RL Arch. Biochem. Biophys. 303:383-393(1993).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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 [6]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-41.
RX PubMed=6822548; DOI=10.1016/s0021-9258(18)33096-5;
RA Pearson W.R., Windle J.J., Morrow J.F., Benson A.M., Talalay P.;
RT "Increased synthesis of glutathione S-transferases in response to
RT anticarcinogenic antioxidants. Cloning and measurement of messenger RNA.";
RL J. Biol. Chem. 258:2052-2062(1983).
RN [7]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-25.
RX PubMed=3864155; DOI=10.1073/pnas.82.21.7202;
RA Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M.,
RA Joernvall H.;
RT "Identification of three classes of cytosolic glutathione transferase
RT common to several mammalian species: correlation between structural data
RT and enzymatic properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985).
RN [8]
RP PROTEIN SEQUENCE OF 2-11; 19-31; 33-43; 53-78; 97-108; 137-144; 153-168;
RP 174-192 AND 203-211, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [9]
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RC STRAIN=CD-1; TISSUE=Liver;
RX PubMed=8605288; DOI=10.1021/tx00050a009;
RA Mitchell A.E., Morin D., Lame M.W., Jones A.D.;
RT "Purification, mass spectrometric characterization, and covalent
RT modification of murine glutathione S-transferases.";
RL Chem. Res. Toxicol. 8:1054-1062(1995).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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. Involved in the
CC formation of glutathione conjugates of both prostaglandin A2 (PGA2) and
CC prostaglandin J2 (PGJ2). Participates in the formation of novel
CC hepoxilin regioisomers. {ECO:0000250|UniProtKB:P09488}.
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 Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133768;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133771;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133772;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133769;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate +
CC glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-
CC eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:132200, ChEBI:CHEBI:132201;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MASS SPECTROMETRY: Mass=25838.4; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8605288};
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; J03952; AAA37747.1; -; mRNA.
DR EMBL; J04632; AAA37705.1; -; mRNA.
DR EMBL; L13448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003822; AAH03822.1; -; mRNA.
DR EMBL; BC046758; AAH46758.1; -; mRNA.
DR EMBL; BC091763; AAH91763.1; -; mRNA.
DR CCDS; CCDS17747.1; -.
DR PIR; H24735; H24735.
DR PIR; S30373; S30373.
DR PIR; S33860; S33860.
DR RefSeq; NP_034488.1; NM_010358.5.
DR AlphaFoldDB; P10649; -.
DR SMR; P10649; -.
DR BioGRID; 200094; 6.
DR IntAct; P10649; 3.
DR MINT; P10649; -.
DR STRING; 10090.ENSMUSP00000004140; -.
DR BindingDB; P10649; -.
DR ChEMBL; CHEMBL3722; -.
DR iPTMnet; P10649; -.
DR PhosphoSitePlus; P10649; -.
DR SwissPalm; P10649; -.
DR REPRODUCTION-2DPAGE; P10649; -.
DR SWISS-2DPAGE; P10649; -.
DR CPTAC; non-CPTAC-3574; -.
DR EPD; P10649; -.
DR jPOST; P10649; -.
DR MaxQB; P10649; -.
DR PaxDb; P10649; -.
DR PeptideAtlas; P10649; -.
DR PRIDE; P10649; -.
DR ProteomicsDB; 271179; -.
DR DNASU; 14862; -.
DR Ensembl; ENSMUST00000004140; ENSMUSP00000004140; ENSMUSG00000058135.
DR GeneID; 14862; -.
DR KEGG; mmu:14862; -.
DR UCSC; uc008qxx.2; mouse.
DR CTD; 2944; -.
DR MGI; MGI:95860; Gstm1.
DR VEuPathDB; HostDB:ENSMUSG00000058135; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000160258; -.
DR HOGENOM; CLU_039475_2_0_1; -.
DR InParanoid; P10649; -.
DR OMA; KRSTRWG; -.
DR PhylomeDB; P10649; -.
DR TreeFam; TF353040; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR BioGRID-ORCS; 14862; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Gstm1; mouse.
DR PRO; PR:P10649; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P10649; protein.
DR Bgee; ENSMUSG00000058135; Expressed in urinary bladder urothelium and 257 other tissues.
DR ExpressionAtlas; P10649; baseline and differential.
DR Genevisible; P10649; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; 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; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0016151; F:nickel cation binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005496; F:steroid binding; ISO:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:MGI.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Lipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8"
FT CHAIN 2..218
FT /note="Glutathione S-transferase Mu 1"
FT /id="PRO_0000185826"
FT DOMAIN 2..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:P09488"
FT BINDING 43..46
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 59..60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 72..73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09488"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04905"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04905"
SQ SEQUENCE 218 AA; 25970 MW; 91AE34A1B5B44599 CRC64;
MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL
PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF
EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN
LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK
