ID   GSTA_RABIT              Reviewed;         221 AA.
AC   Q08862;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Glutathione S-transferase Yc;
DE            EC=2.5.1.18;
DE   AltName: Full=Alpha II;
DE   AltName: Full=GST class-alpha;
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   STRAIN=New Zealand white; TISSUE=Liver;
RX   PubMed=1918075; DOI=10.1016/s0021-9258(18)55046-8;
RA   Gardlik S.J., Gasser R., Philpot R.M., Serabjit-Singh C.J.;
RT   "The major alpha-class glutathione S-transferases of rabbit lung and liver.
RT   Primary sequences, expression, and regulation.";
RL   J. Biol. Chem. 266:19681-19687(1991).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000305}.
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DR   EMBL; M74529; AAA31260.1; -; mRNA.
DR   PIR; B41031; B41031.
DR   RefSeq; NP_001164569.1; NM_001171098.2.
DR   RefSeq; XP_008260973.1; XM_008262751.2.
DR   AlphaFoldDB; Q08862; -.
DR   SMR; Q08862; -.
DR   STRING; 9986.ENSOCUP00000025810; -.
DR   GeneID; 100328911; -.
DR   KEGG; ocu:100328911; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   HOGENOM; CLU_039475_4_0_1; -.
DR   OMA; QMPMVKI; -.
DR   OrthoDB; 1162336at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   ExpressionAtlas; Q08862; baseline.
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; IPR003080; GST_alpha.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
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; Reference proteome; Transferase.
FT   CHAIN           1..221
FT                   /note="Glutathione S-transferase Yc"
FT                   /id="PRO_0000185799"
FT   DOMAIN          3..83
FT                   /note="GST N-terminal"
FT   DOMAIN          85..208
FT                   /note="GST C-terminal"
FT   BINDING         9
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   BINDING         45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08263"
FT   BINDING         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
SQ   SEQUENCE   221 AA;  25450 MW;  D475160FE1299219 CRC64;
     MAGKPKLHYF NARGRMESIR WLLTAAGVEF EEKCMKTRED LEKLRKDGVL MFQQVPMVEI
     DGMKLVQTRA IFNYIADKHN LYGKDIKERA LIDMYTEGIV DLNELILTRP FLPPEEQEAK
     LAQIKDKAKN RYFPAFEKVL KSHGQDYLVG NKLSKADILL VELLYNVEEL NPGATASFPL
     LQALKTRISN LPTVKKFLQP GSQRNPPDDE KCREEAKIIF H