ID   GSTT1_MOUSE             Reviewed;         240 AA.
AC   Q64471; Q91X50;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 4.
DT   27-MAR-2024, entry version 161.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X C3H; TISSUE=Liver, and Lung;
RX   PubMed=8761485; DOI=10.1042/bj3180297;
RA   Mainwaring G.W., Williams S.M., Foster J.R., Tugwood J., Green T.;
RT   "The distribution of theta-class glutathione S-transferases in the liver
RT   and lung of mouse, rat and human.";
RL   Biochem. J. 318:297-303(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-234.
RX   PubMed=20097269; DOI=10.1016/j.bbagen.2010.01.003;
RA   Shokeer A., Mannervik B.;
RT   "Residue 234 is a master switch of the alternative-substrate activity
RT   profile of human and rodent theta class glutathione transferase T1-1.";
RL   Biochim. Biophys. Acta 1800:466-473(2010).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:20097269}.
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:0000269|PubMed:20097269};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: In liver, highest expression found in central vein
CC       limiting plate hepatocytes. Also expressed in interlobular bile duct
CC       epithelial cells. In lung, expressed in club cells and ciliated cells
CC       of the bronchiolar epithelium and in type II alveolar cells of the lung
CC       parenchyma.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; X98055; CAA66665.1; -; mRNA.
DR   EMBL; AC142499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466553; EDL31888.1; -; Genomic_DNA.
DR   EMBL; BC012254; AAH12254.1; -; mRNA.
DR   EMBL; BC055020; AAH55020.1; -; mRNA.
DR   CCDS; CCDS23932.1; -.
DR   PIR; S71878; S71878.
DR   RefSeq; NP_032211.3; NM_008185.3.
DR   AlphaFoldDB; Q64471; -.
DR   SMR; Q64471; -.
DR   BioGRID; 200102; 5.
DR   STRING; 10090.ENSMUSP00000001713; -.
DR   iPTMnet; Q64471; -.
DR   PhosphoSitePlus; Q64471; -.
DR   SwissPalm; Q64471; -.
DR   EPD; Q64471; -.
DR   jPOST; Q64471; -.
DR   PaxDb; 10090-ENSMUSP00000001713; -.
DR   PeptideAtlas; Q64471; -.
DR   ProteomicsDB; 271357; -.
DR   Pumba; Q64471; -.
DR   DNASU; 14871; -.
DR   Ensembl; ENSMUST00000001713.10; ENSMUSP00000001713.4; ENSMUSG00000001663.11.
DR   GeneID; 14871; -.
DR   KEGG; mmu:14871; -.
DR   UCSC; uc007frc.2; mouse.
DR   AGR; MGI:107379; -.
DR   CTD; 2952; -.
DR   MGI; MGI:107379; Gstt1.
DR   VEuPathDB; HostDB:ENSMUSG00000001663; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   GeneTree; ENSGT00940000156366; -.
DR   InParanoid; Q64471; -.
DR   OMA; LMDGEHF; -.
DR   OrthoDB; 1199296at2759; -.
DR   PhylomeDB; Q64471; -.
DR   TreeFam; TF325759; -.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   Reactome; R-MMU-9753281; Paracetamol ADME.
DR   SABIO-RK; Q64471; -.
DR   BioGRID-ORCS; 14871; 2 hits in 77 CRISPR screens.
DR   PRO; PR:Q64471; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q64471; Protein.
DR   Bgee; ENSMUSG00000001663; Expressed in left lobe of liver and 235 other cell types or tissues.
DR   ExpressionAtlas; Q64471; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0047651; F:alkylhalidase activity; ISO:MGI.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR   GO; GO:0018900; P:dichloromethane metabolic process; ISO:MGI.
DR   GO; GO:0006304; P:DNA modification; ISO:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR   GO; GO:0009751; P:response to salicylic acid; IEA:Ensembl.
DR   GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR   GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
DR   CDD; cd03183; GST_C_Theta; 1.
DR   CDD; cd03050; GST_N_Theta; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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   PANTHER; PTHR43917; -; 1.
DR   PANTHER; PTHR43917:SF9; GLUTATHIONE S-TRANSFERASE THETA-1; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01153; Main.4:_Theta-like; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   SWISS-2DPAGE; Q64471; -.
DR   Genevisible; Q64471; MM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..240
FT                   /note="Glutathione S-transferase theta-1"
FT                   /id="PRO_0000185940"
FT   DOMAIN          2..82
FT                   /note="GST N-terminal"
FT   DOMAIN          88..222
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"
FT   MUTAGEN         234
FT                   /note="R->W: Strongly reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:20097269"
FT   CONFLICT        53
FT                   /note="R -> K (in Ref. 1; CAA66665)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="A -> T (in Ref. 1; CAA66665)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   240 AA;  27374 MW;  EDCB477D557466DB CRC64;
     MVLELYLDLL SQPCRAIYIF AKKNNIPFQM HTVELRKGEH LSDAFARVNP MKRVPAMMDG
     GFTLCESVAI LLYLAHKYKV PDHWYPQDLQ ARARVDEYLA WQHTGLRRSC LRALWHKVMF
     PVFLGEQIPP ETLAATLAEL DVNLQVLEDK FLQDKDFLVG PHISLADLVA ITELMHPVGG
     GCPVFEGHPR LAAWYQRVEA AVGKDLFREA HEVILKVKDC PPADLIIKQK LMPRVLAMIQ
//