ID   GSTT1_CHICK             Reviewed;         261 AA.
AC   P20135;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Glutathione S-transferase theta-1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-theta;
DE   AltName: Full=GST-CL1;
GN   Name=GSTT1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7492340; DOI=10.1042/bj3120091;
RA   Hsiao C.D., Martsen E.O., Lee J.Y., Tsai S.-P., Tam M.F.;
RT   "Amino acid sequencing, molecular cloning and modelling of the chick liver
RT   class-theta glutathione S-transferase CL1.";
RL   Biochem. J. 312:91-98(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-24.
RC   TISSUE=Liver;
RX   PubMed=2337594; DOI=10.1021/bi00455a022;
RA   Chang L.-H., Chuang L.-F., Tsai C.-P., Tu C.-P.D., Tam M.F.;
RT   "Characterization of glutathione S-transferases from day-old chick
RT   livers.";
RL   Biochemistry 29:744-750(1990).
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   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {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; U13676; AAA91968.1; -; mRNA.
DR   PIR; S59629; S59629.
DR   RefSeq; NP_990696.1; NM_205365.1.
DR   AlphaFoldDB; P20135; -.
DR   SMR; P20135; -.
DR   STRING; 9031.ENSGALP00000010240; -.
DR   PaxDb; P20135; -.
DR   Ensembl; ENSGALT00000010254; ENSGALP00000010240; ENSGALG00000006344.
DR   GeneID; 396322; -.
DR   KEGG; gga:396322; -.
DR   CTD; 2952; -.
DR   VEuPathDB; HostDB:geneid_396322; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   GeneTree; ENSGT00940000167527; -.
DR   HOGENOM; CLU_011226_2_0_1; -.
DR   InParanoid; P20135; -.
DR   OrthoDB; 1231780at2759; -.
DR   PhylomeDB; P20135; -.
DR   TreeFam; TF325759; -.
DR   Reactome; R-GGA-156590; Glutathione conjugation.
DR   Reactome; R-GGA-9753281; Paracetamol ADME.
DR   PRO; PR:P20135; -.
DR   Proteomes; UP000000539; Chromosome 15.
DR   Bgee; ENSGALG00000006344; Expressed in heart and 11 other tissues.
DR   ExpressionAtlas; P20135; baseline and differential.
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; IPR040079; Glutathione_S-Trfase.
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   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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2337594"
FT   CHAIN           2..261
FT                   /note="Glutathione S-transferase theta-1"
FT                   /id="PRO_0000185944"
FT   DOMAIN          2..101
FT                   /note="GST N-terminal"
FT   DOMAIN          107..248
FT                   /note="GST C-terminal"
FT   BINDING         72..73
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..86
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        14..17
FT                   /note="CRSI -> SRAV (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="T -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  29823 MW;  F94EC305E4616803 CRC64;
     MGLELYLDLL SQPCRSIYIF ARTNNIPFEF KHVELFKDSV LGKKPAAASG AERPRTGPSN
     SEGDGKISLL KKVPVLKDGD FTLAECTAIL LYLSRKYNTP DHWYPSDIKK RAQVDEYLSW
     HHANIRANAP KTMWIKVLIP LFTGQPQPSE KLQEVMEGLS TSLKQFEERF LQDKAFIIGS
     EISLADLVAI VELMQPVGVG CDIFEDRPRL MEWRRRVEEA VGKELFFQAH EMILNIKELS
     NIQIDPQLKE HLAPVLMKML K