ID   GSTMU_RABIT             Reviewed;         218 AA.
AC   P46409;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Glutathione S-transferase Mu 1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST Mu I;
DE   AltName: Full=GST class-mu;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7733673; DOI=10.1006/abbi.1995.1250;
RA   Lee S.H., Lee S.H., Han J.S., Kim Y.S., Koh J.K.;
RT   "Cloning and expression of a cDNA for mu-class glutathione S-transferase
RT   from rabbit liver.";
RL   Arch. Biochem. Biophys. 318:424-429(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21.
RC   TISSUE=Liver;
RX   PubMed=8460949; DOI=10.1006/abbi.1993.1163;
RA   Primiano T., Novak R.F.;
RT   "Purification and characterization of class mu glutathione S-transferase
RT   isozymes from rabbit hepatic tissue.";
RL   Arch. Biochem. Biophys. 301:404-410(1993).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Well expressed in rabbit liver, brain and kidney.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L23766; AAA69665.1; -; mRNA.
DR   PIR; S65674; S65674.
DR   RefSeq; NP_001075721.1; NM_001082252.1.
DR   AlphaFoldDB; P46409; -.
DR   SMR; P46409; -.
DR   GeneID; 100009073; -.
DR   KEGG; ocu:100009073; -.
DR   CTD; 2946; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   OrthoDB; 1162336at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
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   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
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; Reference proteome; Transferase.
FT   CHAIN           1..218
FT                   /note="Glutathione S-transferase Mu 1"
FT                   /id="PRO_0000185837"
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:P08515"
FT   BINDING         46..50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         59..60
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         72..73
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   218 AA;  25417 MW;  481EA4AB85671102 CRC64;
     MPMTLGYWDV RGLALPIRML LEYTDTSYEE KKYTMGDAPN YDQSKWLSEK FTLGLDFPNL
     PYLIDGTHKL TQSNAILRYL ARKHGLCGET EEERIRVDIL ENQLMDNRFQ LVNVCYSPDF
     EKLKPEYLKG LPEKLQLYSQ FLGSLPWFAG DKITFADFLV YDVLDQNRIF VPGCLDAFPN
     LKDFHVRFEG LPKISAYMKS SRFIRVPVFL KKATWTGI