ID   GSTT2_RAT               Reviewed;         244 AA.
AC   P30713; P36971;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Glutathione S-transferase theta-2;
DE            EC=2.5.1.18 {ECO:0000269|PubMed:2114406};
DE   AltName: Full=GST 12-12;
DE   AltName: Full=GST class-theta-2;
DE   AltName: Full=Glutathione S-transferase 12;
DE   AltName: Full=Glutathione S-transferase Yrs-Yrs;
GN   Name=Gstt2;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=1764080; DOI=10.1016/0006-291x(91)92079-y;
RA   Ogura K., Nishiyama T., Okada T., Kajita J., Narihata H., Watabe T.,
RA   Hiratsuka A., Watabe T.;
RT   "Molecular cloning and amino acid sequencing of rat liver class theta
RT   glutathione S-transferase Yrs-Yrs inactivating reactive sulfate esters of
RT   carcinogenic arylmethanols.";
RL   Biochem. Biophys. Res. Commun. 181:1294-1300(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=7802657; DOI=10.1006/bbrc.1994.2799;
RA   Ogura K., Nishiyama T., Hiratsuka A., Watabe T., Watabe T.;
RT   "Isolation and characterization of the gene encoding rat class theta
RT   glutathione S-transferase subunit yrs.";
RL   Biochem. Biophys. Res. Commun. 205:1250-1256(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [4]
RP   PROTEIN SEQUENCE OF 2-26, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=2114406; DOI=10.1016/s0021-9258(19)38496-0;
RA   Hiratsuka A., Sebata N., Kawashima K., Okuda H., Ogura K., Watabe T.,
RA   Satoh K., Hatayama I., Tsuchida S., Ishikawa T., Sato K.;
RT   "A new class of rat glutathione S-transferase Yrs-Yrs inactivating reactive
RT   sulfate esters as metabolites of carcinogenic arylmethanols.";
RL   J. Biol. Chem. 265:11973-11981(1990).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-47; 140-162; 222-234 AND 238-244.
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   [6]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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).
CC   -!- FUNCTION: Catalyzes the inactivation of reactive sulfate esters in
CC       carcinogenic arylmethanols (PubMed:2114406). Highest activity towards
CC       ethacrynic acid and cumene hydroperoxide (PubMed:2114406).
CC       {ECO:0000269|PubMed:2114406}.
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:2114406};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2114406}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8761485}.
CC       Nucleus {ECO:0000269|PubMed:8761485}.
CC   -!- TISSUE SPECIFICITY: Highest values found in liver followed by testis,
CC       adrenal gland, kidney, lung, brain and skeletal muscle. In liver,
CC       highest expression found in central vein limiting plate hepatocytes. In
CC       lung, expressed mainly in club cells of the bronchiolar epithelium and,
CC       at low levels, in type II alveolar cells. {ECO:0000269|PubMed:8761485}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; D10026; BAA00916.1; -; mRNA.
DR   EMBL; D38556; BAA07559.1; -; Genomic_DNA.
DR   EMBL; BC061856; AAH61856.1; -; mRNA.
DR   PIR; JC2425; JC2425.
DR   PIR; S14346; S14346.
DR   RefSeq; NP_036928.1; NM_012796.2.
DR   AlphaFoldDB; P30713; -.
DR   SMR; P30713; -.
DR   STRING; 10116.ENSRNOP00000071112; -.
DR   iPTMnet; P30713; -.
DR   PhosphoSitePlus; P30713; -.
DR   PaxDb; 10116-ENSRNOP00000033158; -.
DR   GeneID; 29487; -.
DR   KEGG; rno:29487; -.
DR   UCSC; RGD:69362; rat.
DR   AGR; RGD:69362; -.
DR   CTD; 2953; -.
DR   RGD; 69362; Gstt2.
DR   VEuPathDB; HostDB:ENSRNOG00000052415; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_2_0_1; -.
DR   InParanoid; P30713; -.
DR   OMA; INDNGYK; -.
DR   OrthoDB; 1199296at2759; -.
DR   PhylomeDB; P30713; -.
DR   TreeFam; TF325759; -.
DR   Reactome; R-RNO-156590; Glutathione conjugation.
DR   PRO; PR:P30713; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000052415; Expressed in liver and 18 other cell types or tissues.
DR   ExpressionAtlas; P30713; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:RGD.
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:SF4; GLUTATHIONE S-TRANSFERASE THETA-2-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 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   Genevisible; P30713; RN.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Nucleus; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1848757,
FT                   ECO:0000269|PubMed:2114406"
FT   CHAIN           2..244
FT                   /note="Glutathione S-transferase theta-2"
FT                   /id="PRO_0000185943"
FT   DOMAIN          2..82
FT                   /note="GST N-terminal"
FT   DOMAIN          88..230
FT                   /note="GST C-terminal"
FT   BINDING         40..41
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG30"
FT   BINDING         53..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG30"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG30"
FT   BINDING         104..107
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0CG30"
FT   CONFLICT        14
FT                   /note="S -> C (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36..37
FT                   /note="LK -> RC (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="S -> C (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="Missing (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   244 AA;  27439 MW;  B8FCC8B15F003679 CRC64;
     MGLELYLDLL SQPSRAVYIF AKKNGIPFQL RTVDLLKGQH LSEQFSQVNC LKKVPVLKDG
     SFVLTESTAI LIYLSSKYQV ADHWYPADLQ ARAQVHEYLG WHADNIRGTF GVLLWTKVLG
     PLIGVQVPEE KVERNRNSMV LALQRLEDKF LRDRAFIAGQ QVTLADLMSL EELIQPVALG
     CNLFEGRPQL TAWRERVEAF LGAELCQEAH NPIMSVLGQA AKKTLPVPPP EAHASMMLRI
     ARIP
//