GSTT1_RAT
ID GSTT1_RAT Reviewed; 240 AA.
AC Q01579;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Glutathione S-transferase theta-1;
DE EC=2.5.1.18;
DE AltName: Full=GST 5-5;
DE AltName: Full=GST class-theta-1;
DE AltName: Full=Glutathione S-transferase 5;
GN Name=Gstt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=1445253; DOI=10.1042/bj2870957;
RA Pemble S.E., Taylor J.B.;
RT "An evolutionary perspective on glutathione transferases inferred from
RT class-theta glutathione transferase cDNA sequences.";
RL Biochem. J. 287:957-963(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-47; 58-95; 120-131 AND 176-193.
RC TISSUE=Liver;
RX PubMed=1848757; DOI=10.1042/bj2740409;
RA Meyer D.J., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M., Ketterer B.;
RT "Theta, a new class of glutathione transferases purified from rat and
RT man.";
RL Biochem. J. 274:409-414(1991).
RN [4]
RP TISSUE SPECIFICITY.
RC 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 [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
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.
CC -!- TISSUE SPECIFICITY: In liver, highest expression found in central vein
CC limiting plate hepatocytes. In lung, expressed mainly in Clara cells of
CC the bronchiolar epithelium and, at low levels, in type II alveolar
CC cells. {ECO:0000269|PubMed:8761485}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000305}.
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DR EMBL; X67654; CAA47896.1; -; mRNA.
DR EMBL; BC086426; AAH86426.1; -; mRNA.
DR PIR; S27161; S27161.
DR RefSeq; NP_445745.1; NM_053293.2.
DR AlphaFoldDB; Q01579; -.
DR SMR; Q01579; -.
DR STRING; 10116.ENSRNOP00000001669; -.
DR BindingDB; Q01579; -.
DR ChEMBL; CHEMBL2423; -.
DR iPTMnet; Q01579; -.
DR PhosphoSitePlus; Q01579; -.
DR PaxDb; Q01579; -.
DR PRIDE; Q01579; -.
DR Ensembl; ENSRNOT00000001669; ENSRNOP00000001669; ENSRNOG00000049771.
DR GeneID; 25260; -.
DR KEGG; rno:25260; -.
DR UCSC; RGD:2765; rat.
DR CTD; 2952; -.
DR RGD; 2765; Gstt1.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000156366; -.
DR HOGENOM; CLU_011226_2_0_1; -.
DR InParanoid; Q01579; -.
DR OMA; GCQVFKG; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q01579; -.
DR Reactome; R-RNO-156590; Glutathione conjugation.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR SABIO-RK; Q01579; -.
DR PRO; PR:Q01579; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000049771; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; Q01579; baseline and differential.
DR Genevisible; Q01579; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0047651; F:alkylhalidase activity; IDA:RGD.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0018900; P:dichloromethane metabolic process; IDA:RGD.
DR GO; GO:0006304; P:DNA modification; IDA:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009751; P:response to salicylic acid; IEP:RGD.
DR GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR GO; GO:0033197; P:response to vitamin E; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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; Direct protein sequencing; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..240
FT /note="Glutathione S-transferase theta-1"
FT /id="PRO_0000185942"
FT DOMAIN 2..82
FT /note="GST N-terminal"
FT DOMAIN 88..223
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; 27468 MW; 09583ACF9C85DF8F CRC64;
MVLELYLDLL SQPCRAIYIF AKKNNIPFQM HTVELRKGEH LSDAFAQVNP MKKVPAMKDG
GFTLCESVAI LLYLAHKYKV PDHWYPQDLQ ARARVDEYLA WQHTTLRRSC LRTLWHKVMF
PVFLGEQIRP EMLAATLADL DVNVQVLEDQ FLQDKDFLVG PHISLADVVA ITELMHPVGG
GCPVFEGRPR LAAWYRRVEA AVGKDLFLEA HEVILKVRDC PPADPVIKQK LMPRVLTMIQ
