GSTT1_MOUSE
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 03-AUG-2022, entry version 152.
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, Pancreas,
RC 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 Clara 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 SWISS-2DPAGE; Q64471; -.
DR EPD; Q64471; -.
DR jPOST; Q64471; -.
DR PaxDb; Q64471; -.
DR PeptideAtlas; Q64471; -.
DR PRIDE; Q64471; -.
DR ProteomicsDB; 271357; -.
DR DNASU; 14871; -.
DR Ensembl; ENSMUST00000001713; ENSMUSP00000001713; ENSMUSG00000001663.
DR GeneID; 14871; -.
DR KEGG; mmu:14871; -.
DR UCSC; uc007frc.2; mouse.
DR CTD; 2952; -.
DR MGI; MGI:107379; Gstt1.
DR VEuPathDB; HostDB:ENSMUSG00000001663; -.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000156366; -.
DR InParanoid; Q64471; -.
DR OMA; GCQVFKG; -.
DR OrthoDB; 1231780at2759; -.
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 72 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 232 other tissues.
DR ExpressionAtlas; Q64471; baseline and differential.
DR Genevisible; Q64471; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0007568; P:aging; IEA:Ensembl.
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 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 Pfam; PF02798; GST_N; 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; 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
