GSTM2_MACFA
ID GSTM2_MACFA Reviewed; 218 AA.
AC Q9TSM4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
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 fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=10869451; DOI=10.1093/toxsci/56.1.26;
RA Wang C., Bammler T.K., Guo Y., Kelly E.J., Eaton D.L.;
RT "Mu-class GSTs are responsible for aflatoxin B(1)-8,9-epoxide-conjugating
RT activity in the nonhuman primate Macaca fascicularis liver.";
RL Toxicol. Sci. 56:26-36(2000).
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) (PubMed:10869451).
CC {ECO:0000250|UniProtKB:P28161, ECO:0000269|PubMed:10869451}.
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; AF200710; AAF08540.1; -; mRNA.
DR RefSeq; NP_001274584.1; NM_001287655.1.
DR AlphaFoldDB; Q9TSM4; -.
DR SMR; Q9TSM4; -.
DR STRING; 9541.XP_005542505.1; -.
DR GeneID; 102146720; -.
DR CTD; 2946; -.
DR VEuPathDB; HostDB:ENSMFAG00000038873; -.
DR eggNOG; KOG1695; Eukaryota.
DR OMA; NRLPEMM; -.
DR Proteomes; UP000233100; Chromosome 1.
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 1: Evidence at protein level;
KW Cytoplasm; Lipid metabolism; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase Mu 2"
FT /id="PRO_0000185819"
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
