ID   GSTMU_MESAU             Reviewed;         218 AA.
AC   P30116;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-mu;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Smooth muscle;
RX   PubMed=1631097; DOI=10.1073/pnas.89.13.6104;
RA   Fan W.M., Trifiletti R., Norris J.S., Cooper T.M.;
RT   "Cloning of a mu-class glutathione S-transferase gene and identification of
RT   the glucocorticoid regulatory domains in its 5' flanking sequence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6104-6108(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Smooth muscle;
RX   PubMed=1944302; DOI=10.1210/mend-5-7-979;
RA   Norris J.S., Schwartz D.A., Macleod S.L., Fan W.M., O'Brien T.J.,
RA   Harris S.E., Trifiletti R., Cornett L.E., Cooper T.M., Levi W.M.,
RA   Smith R.G.;
RT   "Cloning of a mu-class glutathione S-transferase complementary DNA and
RT   characterization of its glucocorticoid inducibility in a smooth muscle
RT   tumor cell line.";
RL   Mol. Endocrinol. 5:979-986(1991).
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}.
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DR   EMBL; M59772; AAA37075.1; -; mRNA.
DR   EMBL; X61033; CAA43368.1; -; Genomic_DNA.
DR   PIR; A23732; A23732.
DR   RefSeq; NP_001268559.1; NM_001281630.1.
DR   AlphaFoldDB; P30116; -.
DR   SMR; P30116; -.
DR   STRING; 10036.XP_005076677.1; -.
DR   GeneID; 101829268; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   OrthoDB; 1162336at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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; PF00043; GST_C; 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   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..218
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185836"
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   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   218 AA;  25690 MW;  F5D81F3DE32F9EC5 CRC64;
     MPVTLGYWDI RGLAHAIRLL LEYTDTSYEE KKYTMGDAPN FDRSQWLNEK FKLGLDFPNL
     PYLIDGSHKI TQSNAILRYI ARKHDLCGET EEERIQLDIL ENQAMDTRMQ LAMVCYSPDF
     EKRKPEYLEG LPEKMKLYSE FLGKRSWFAG DKITYVDFLI YDVLDQHRIF APKCLDAFPN
     LKDFLARFEG LKKISDYMKS SRFSCKQIFA KMAVWNSK