GSTM3_MACFU
ID GSTM3_MACFU Reviewed; 225 AA.
AC Q9BEA9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Glutathione S-transferase Mu 3;
DE EC=2.5.1.18;
DE AltName: Full=GST class-mu 3;
DE AltName: Full=GSTM3-3;
GN Name=GSTM3;
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 M3.";
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. May govern uptake
CC and detoxification of both endogenous compounds and xenobiotics at the
CC testis and brain blood barriers (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; AB025800; BAB40443.1; -; mRNA.
DR AlphaFoldDB; Q9BEA9; -.
DR SMR; Q9BEA9; -.
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 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; Isopeptide bond; Transferase; Ubl conjugation.
FT CHAIN 1..225
FT /note="Glutathione S-transferase Mu 3"
FT /id="PRO_0000185823"
FT DOMAIN 5..92
FT /note="GST N-terminal"
FT DOMAIN 94..212
FT /note="GST C-terminal"
FT BINDING 11..12
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 50..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 63..64
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 76..77
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CROSSLNK 54
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P21266"
FT CROSSLNK 73
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P21266"
SQ SEQUENCE 225 AA; 26604 MW; 675126079D89398A CRC64;
MSCESSMVLG YWDIRGLAHA IRLLLEFTDT SYEEKRYTCG EAPDYDRSQW LDVKFKLDLD
FPNLPYLMDG KNKITQSNAI LRYIARKHNM CGETEEEKIR VDIIENQVMD FRTQLIRLCY
SSDHEKLKPQ YLEELPGQLK QFSVFLGKFS WFAGEKLTFV DFLTYDILDQ NRIFEPKCLD
EFPNLKAFMC RFEALEKIAA YIQSDQFFKM PINNKMAQWG NKPVC
