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 24-JAN-2024, entry version 112.
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.ENSMAUP00000014487; -.
DR GeneID; 101829268; -.
DR KEGG; maua:101829268; -.
DR eggNOG; KOG1695; Eukaryota.
DR OrthoDB; 5488107at2759; -.
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 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; 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 PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF247; GLUTATHIONE S-TRANSFERASE MU 1; 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; 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.
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
//
