ID   GSTT1_BOVIN             Reviewed;         240 AA.
AC   Q2NL00;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Glutathione S-transferase theta-1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-theta-1;
GN   Name=GSTT1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. Also binds
CC       steroids, bilirubin, carcinogens and numerous organic anions. Has
CC       dichloromethane dehalogenase activity.
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. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; BC111289; AAI11290.1; -; mRNA.
DR   RefSeq; NP_001039697.1; NM_001046232.2.
DR   AlphaFoldDB; Q2NL00; -.
DR   SMR; Q2NL00; -.
DR   STRING; 9913.ENSBTAP00000007403; -.
DR   PaxDb; Q2NL00; -.
DR   PRIDE; Q2NL00; -.
DR   Ensembl; ENSBTAT00000007403; ENSBTAP00000007403; ENSBTAG00000040298.
DR   GeneID; 517724; -.
DR   KEGG; bta:517724; -.
DR   CTD; 2952; -.
DR   VEuPathDB; HostDB:ENSBTAG00000040298; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   GeneTree; ENSGT00940000156366; -.
DR   HOGENOM; CLU_011226_2_0_1; -.
DR   InParanoid; Q2NL00; -.
DR   OMA; GCQVFKG; -.
DR   OrthoDB; 1231780at2759; -.
DR   TreeFam; TF325759; -.
DR   Reactome; R-BTA-156590; Glutathione conjugation.
DR   Reactome; R-BTA-9753281; Paracetamol ADME.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Bgee; ENSBTAG00000040298; Expressed in cortex of kidney and 102 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   CDD; cd03183; GST_C_Theta; 1.
DR   CDD; cd03050; GST_N_Theta; 1.
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; IPR040077; GST_C_Theta.
DR   InterPro; IPR040075; GST_N_Theta.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
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..240
FT                   /note="Glutathione S-transferase theta-1"
FT                   /id="PRO_0000245031"
FT   DOMAIN          2..82
FT                   /note="GST N-terminal"
FT   DOMAIN          88..226
FT                   /note="GST C-terminal"
FT   BINDING         40
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         53..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   240 AA;  27149 MW;  B4128AEAB8785F31 CRC64;
     MGLELYLDLL SQPCRAIYIF AKKNRIPFEL RTVDLRKGQH LSDAFAQVNP LQKVPILKDG
     DFILTESVAI LLYLARKYKV PDHWYPQDLQ ACARVDEYLA WQHTALRRNC LRALWHKVML
     PVFLGEPVSP EMLATTLAEL DMALQVLEGK FLQDKAFLTG SHISLADLVA ITELMHPVGA
     GCQVFKGRPK LAAWRQRVEA AVGEVLFQEA HEVILKAKDS QPADPTLKQK MLPKVLAMIQ