ID   GSTM3_MOUSE             Reviewed;         218 AA.
AC   P19639;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2026, entry version 187.
DE   RecName: Full=Glutathione S-transferase Mu 3 {ECO:0000305};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P21266};
DE   AltName: Full=GST class-mu 3;
DE   AltName: Full=Glutathione S-transferase GT9.3 {ECO:0000305|PubMed:6822548};
GN   Name=Gstm3 {ECO:0000312|MGI:MGI:106026};
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] 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   [3]
RP   PROTEIN SEQUENCE OF 2-26.
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-218.
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
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: Glutathione S-transferase that catalyzes the conjugation of
CC       reduced glutathione to electrophilic substrates, probably contributing
CC       to detoxification of endogenous and exogenous toxic compounds. In
CC       vitro, acts on 1-chloro-2,4-dinitrobenzene, ethacrynic acid, trans-alk-
CC       2-enals, trans-hex-2-enal, trans-oct-2-enal, trans-non-2-enal, 4-
CC       hydroxynonenal and 4-hydroxydecenal. A glutathione peroxidase activity
CC       toward H2O2 and cumene hydroperoxide has been reported, but was not
CC       confirmed in another study. May act on a broad range of exogenous and
CC       endogenous hydrophobic electrophiles, thereby making them more water-
CC       soluble and easier for the cell to handle or eliminate. May be involved
CC       in protection against carcinogens, therapeutic drugs, environmental
CC       toxins and products of oxidative stress.
CC       {ECO:0000250|UniProtKB:P21266}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RX + glutathione = an S-substituted glutathione + a halide
CC         anion + 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:P21266};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC         Evidence={ECO:0000250|UniProtKB:P21266};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-
CC         S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:133977;
CC         Evidence={ECO:0000250|UniProtKB:P21266};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51221;
CC         Evidence={ECO:0000250|UniProtKB:P21266};
CC   -!- SUBUNIT: Homodimer. Heterodimer. {ECO:0000250|UniProtKB:P21266}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z1B2}.
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; BC044927; AAH44927.1; -; mRNA.
DR   EMBL; J03953; AAA37748.1; -; mRNA.
DR   CCDS; CCDS17744.1; -.
DR   PIR; B28946; B28946.
DR   PIR; E37520; E37520.
DR   RefSeq; NP_034489.1; NM_010359.3.
DR   SMR; P19639; -.
DR   BioGRID; 200096; 2.
DR   IntAct; P19639; 1.
DR   STRING; 10090.ENSMUSP00000004136; -.
DR   iPTMnet; P19639; -.
DR   PhosphoSitePlus; P19639; -.
DR   SwissPalm; P19639; -.
DR   PaxDb; 10090-ENSMUSP00000004136; -.
DR   PeptideAtlas; P19639; -.
DR   ProteomicsDB; 271180; -.
DR   jPOST; P19639; -.
DR   DNASU; 14864; -.
DR   Ensembl; ENSMUST00000004136.10; ENSMUSP00000004136.9; ENSMUSG00000004038.10.
DR   GeneID; 14864; -.
DR   KEGG; mmu:14864; -.
DR   UCSC; uc008qxv.2; mouse.
DR   CTD; 2947; -.
DR   VEuPathDB; HostDB:ENSMUSG00000004038; -.
DR   AGR; MGI:106026; -.
DR   MGI; MGI:106026; Gstm3.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000160258; -.
DR   HOGENOM; CLU_039475_2_0_1; -.
DR   InParanoid; P19639; -.
DR   OMA; ACKHNMC; -.
DR   OrthoDB; 4951845at2759; -.
DR   PhylomeDB; P19639; -.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   PRO; PR:P19639; -.
DR   Bgee; ENSMUSG00000004038; Expressed in duodenum and 96 other cell types or tissues.
DR   CDD; cd03209; GST_C_Mu; 1.
DR   CDD; cd03075; GST_N_Mu; 1.
DR   FunFam; 3.40.30.10:FF:000019; Glutathione S-transferase Mu; 1.
DR   FunFam; 1.20.1050.10:FF:000083; Glutathione S-transferase Mu 1; 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; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR003081; GST_mu.
DR   InterPro; IPR050213; GST_superfamily.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF126; GLUTATHIONE S-TRANSFERASE MU 1-RELATED; 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   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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   GO; GO:0005737; C:cytoplasm; ISO:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; ISO:GO_Central.
DR   GO; GO:0043295; F:glutathione binding; ISO:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; ISO:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P19639; protein.
DR   BioGRID-ORCS; 14864; 2 hits in 76 CRISPR screens.
DR   AlphaFoldDB; P19639; -.
DR   FunCoup; P19639; 191.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Isopeptide bond; Reference proteome;
KW   Transferase; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3864155"
FT   CHAIN           2..218
FT                   /note="Glutathione S-transferase Mu 3"
FT                   /id="PRO_0000185828"
FT   DOMAIN          2..88
FT                   /note="GST N-terminal"
FT   DOMAIN          90..208
FT                   /note="GST C-terminal"
FT   BINDING         7
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         46
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         59
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         60
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         72
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         73
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   CROSSLNK        50
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P21266"
FT   CROSSLNK        69
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P21266"
SQ   SEQUENCE   218 AA;  25702 MW;  F4989897BE817868 CRC64;
     MPMTLGYWNT RGLTHSIRLL LEYTDSSYEE KRYVMGDAPN FDRSQWLSEK FNLGLDFPNL
     PYLIDGSHKV TQSNAILRYL GRKHNLCGET EEERIRVDTL ENQVMDTRIQ LMIVCCSPDF
     EKQKPEFLKA IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN
     LRDFLARFEG LKKISAYMKS SRFLPRPVFT KIAQWGTD
//