GSTM5_MESAU
ID GSTM5_MESAU Reviewed; 138 AA.
AC P86214;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Glutathione S-transferase Mu 5 {ECO:0000250|UniProtKB:Q9Z1B2};
DE EC=2.5.1.18;
DE AltName: Full=GST class-mu 5 {ECO:0000250|UniProtKB:Q9Z1B2};
DE Flags: Fragments;
GN Name=GSTM5 {ECO:0000250|UniProtKB:Q9Z1B2};
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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000250|UniProtKB:Q9Z1B2}.
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:Q9Z1B2};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P21266}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z1B2}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000255}.
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DR AlphaFoldDB; P86214; -.
DR SMR; P86214; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..>138
FT /note="Glutathione S-transferase Mu 5"
FT /id="PRO_0000394302"
FT DOMAIN <1..>71
FT /note="GST N-terminal"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B2"
FT DOMAIN <72..135
FT /note="GST C-terminal"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B2"
FT BINDING 6..7
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 39..43
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 52..53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 65..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT MOD_RES 1
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1B2"
FT NON_CONS 10..11
FT /evidence="ECO:0000305"
FT NON_CONS 71..72
FT /evidence="ECO:0000305"
FT NON_CONS 85..86
FT /evidence="ECO:0000305"
FT NON_CONS 93..94
FT /evidence="ECO:0000305"
FT NON_CONS 129..130
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 138
SQ SEQUENCE 138 AA; 16658 MW; 68C99F8E788423A8 CRC64;
SMVLGYWDIR RMLLEFTDTS YEEKRYICGE APDYDRSQWL DVKFKLDLDF PNLPYLMDGK
NKITQSNAIL RIRVDIMENQ IMDFRQFSLF LGKKLTFVDF LTYDVLDQNR MFEPKCLDEF
PNLKAFMCRC FKMPINNK
