ID   GSTM2_MACFU             Reviewed;         218 AA.
AC   Q9BEB0;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Glutathione S-transferase Mu 2 {ECO:0000305};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P28161};
DE   AltName: Full=GST class-mu 2;
DE   AltName: Full=GSTM2-2;
GN   Name=GSTM2;
OS   Macaca fuscata fuscata (Japanese macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Beuckmann C.T., Fujimori K., Urade Y.;
RT   "Macaca fuscata glutathione transferase M2.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. Participates in the
CC       formation of novel hepoxilin regioisomers (By similarity). Has activity
CC       toward aflatoxin B(1)-8,9-epoxide (AFBO) (By similarity).
CC       {ECO:0000250|UniProtKB:P28161, ECO:0000250|UniProtKB:Q9TSM4}.
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:P28161};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC         Evidence={ECO:0000250|UniProtKB:P28161};
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:P28161};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261;
CC         Evidence={ECO:0000250|UniProtKB:P28161};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR   EMBL; AB025799; BAB40442.1; -; mRNA.
DR   AlphaFoldDB; Q9BEB0; -.
DR   SMR; Q9BEB0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045171; C:intercellular bridge; IEA:UniProt.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   GO; GO:0051122; P:hepoxilin biosynthetic 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; PF00043; GST_C; 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   2: Evidence at transcript level;
KW   Cytoplasm; Lipid metabolism; Phosphoprotein; Transferase.
FT   CHAIN           1..218
FT                   /note="Glutathione S-transferase Mu 2"
FT                   /id="PRO_0000185820"
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:P08010"
FT   BINDING         43..46
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   BINDING         50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   BINDING         59..60
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   BINDING         72..73
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            210
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
SQ   SEQUENCE   218 AA;  25709 MW;  F2E509C3949F9051 CRC64;
     MPMTLGYWNI RGLAHSIRLL LEYTGSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL
     PYLIDGTHKI TQSNAILRYI ARKHNLCGET EKEKIREDIL ENQLMDNRMQ LARLCYDPDF
     EKLKPEYLEG LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN
     LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK