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 27-MAR-2024, entry version 178.
DE RecName: Full=Glutathione S-transferase Mu 3;
DE EC=2.5.1.18;
DE AltName: Full=GST class-mu 3;
DE AltName: Full=Glutathione S-transferase GT9.3;
GN Name=Gstm3;
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 [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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-41.
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 [4]
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 [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: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37748.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC044927; AAH44927.1; -; mRNA.
DR EMBL; J03953; AAA37748.1; ALT_INIT; mRNA.
DR CCDS; CCDS17744.1; -.
DR PIR; B28946; B28946.
DR PIR; E37520; E37520.
DR RefSeq; NP_034489.1; NM_010359.2.
DR AlphaFoldDB; P19639; -.
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 jPOST; P19639; -.
DR MaxQB; P19639; -.
DR PaxDb; 10090-ENSMUSP00000004136; -.
DR PeptideAtlas; P19639; -.
DR ProteomicsDB; 271180; -.
DR DNASU; 14864; -.
DR Ensembl; ENSMUST00000004136.10; ENSMUSP00000004136.9; ENSMUSG00000004038.10.
DR GeneID; 14864; -.
DR KEGG; mmu:14864; -.
DR UCSC; uc008qxv.2; mouse.
DR AGR; MGI:106026; -.
DR CTD; 2947; -.
DR MGI; MGI:106026; Gstm3.
DR VEuPathDB; HostDB:ENSMUSG00000004038; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000160258; -.
DR HOGENOM; CLU_039475_2_0_1; -.
DR InParanoid; P19639; -.
DR OMA; ADFIMYE; -.
DR OrthoDB; 5488107at2759; -.
DR PhylomeDB; P19639; -.
DR TreeFam; TF353040; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR BioGRID-ORCS; 14864; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Gstm3; mouse.
DR PRO; PR:P19639; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P19639; Protein.
DR Bgee; ENSMUSG00000004038; Expressed in duodenum and 96 other cell types or tissues.
DR Genevisible; P19639; 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 GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP: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:SF219; GLUTATHIONE S-TRANSFERASE MU 3; 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; 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..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 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
//
