GSTM1_BOVIN
ID GSTM1_BOVIN Reviewed; 218 AA.
AC Q9N0V4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Glutathione S-transferase Mu 1 {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P09488};
DE AltName: Full=GST class-mu 1;
DE AltName: Full=GSTM1-1;
GN Name=GSTM1; Synonyms=GSTM;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP SUBUNIT.
RC TISSUE=Lens;
RX PubMed=10973735; DOI=10.1006/exer.2000.0876;
RA Jimenez-Asensio J., Garland D.;
RT "A lens glutathione S-transferase, class mu, with thiol-specific
RT antioxidant activity.";
RL Exp. Eye Res. 71:255-265(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Protects against
CC the thiol-mediated metal-catalyzed oxidative inactivation of enzymes.
CC Involved in the formation of glutathione conjugates of both
CC prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in
CC the formation of novel hepoxilin regioisomers (By similarity).
CC {ECO:0000250|UniProtKB:P09488, ECO:0000269|PubMed:10973735}.
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. {ECO:0000269|PubMed:10973735}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; BC102050; AAI02051.1; -; mRNA.
DR EMBL; AF249588; AAF64308.1; -; mRNA.
DR RefSeq; NP_787019.1; NM_175825.3.
DR AlphaFoldDB; Q9N0V4; -.
DR SMR; Q9N0V4; -.
DR STRING; 9913.ENSBTAP00000023627; -.
DR PaxDb; Q9N0V4; -.
DR PeptideAtlas; Q9N0V4; -.
DR PRIDE; Q9N0V4; -.
DR GeneID; 327709; -.
DR KEGG; bta:327709; -.
DR CTD; 2944; -.
DR eggNOG; KOG1695; Eukaryota.
DR HOGENOM; CLU_039475_2_0_1; -.
DR InParanoid; Q9N0V4; -.
DR OrthoDB; 1162336at2759; -.
DR TreeFam; TF353040; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
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 Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase Mu 1"
FT /id="PRO_0000240625"
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"
SQ SEQUENCE 218 AA; 25635 MW; 3D02EA0F43C07B0A CRC64;
MPMILGYWDI RGLAHAIRLL LEYTDTNYEE RQYSVGDAPD YDRSQWLNEK FKLGLDFPNL
PYLIDGTHKL TQSNAILRYI ARKHNLCGET EEEMIRVDIL ENQVMDVRLA MARICYSPDF
EKLKPGFLKE IPEKIKLFSE FLGKRPWFAG DKLTYVDFLV YDVLDMHRIF EPKCLDAFPN
LKDFISRFEG LKKISAYMKS SRFLPGPLFM KLAVWGNK
