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Glutathione S-transferase theta-2 (EC 2.5.1.18) (GST 12-12) (GST class-theta-2) (Glutathione S-transferase 12) (Glutathione S-transferase Yrs-Yrs)

 GSTT2_RAT               Reviewed;         244 AA.
P30713; P36971;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 143.
RecName: Full=Glutathione S-transferase theta-2;
EC=2.5.1.18;
AltName: Full=GST 12-12;
AltName: Full=GST class-theta-2;
AltName: Full=Glutathione S-transferase 12;
AltName: Full=Glutathione S-transferase Yrs-Yrs;
Name=Gstt2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=1764080; DOI=10.1016/0006-291X(91)92079-Y;
Ogura K., Nishiyama T., Okada T., Kajita J., Narihata H., Watabe T.,
Hiratsuka A., Watabe T.;
"Molecular cloning and amino acid sequencing of rat liver class theta
glutathione S-transferase Yrs-Yrs inactivating reactive sulfate esters
of carcinogenic arylmethanols.";
Biochem. Biophys. Res. Commun. 181:1294-1300(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=7802657; DOI=10.1006/bbrc.1994.2799;
Ogura K., Nishiyama T., Hiratsuka A., Watabe T., Watabe T.;
"Isolation and characterization of the gene encoding rat class theta
glutathione S-transferase subunit yrs.";
Biochem. Biophys. Res. Commun. 205:1250-1256(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-26, AND CHARACTERIZATION.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=2114406;
Hiratsuka A., Sebata N., Kawashima K., Okuda H., Ogura K., Watabe T.,
Satoh K., Hatayama I., Tsuchida S., Ishikawa T., Sato K.;
"A new class of rat glutathione S-transferase Yrs-Yrs inactivating
reactive sulfate esters as metabolites of carcinogenic
arylmethanols.";
J. Biol. Chem. 265:11973-11981(1990).
[5]
PROTEIN SEQUENCE OF 2-47; 140-162; 222-234 AND 238-244.
TISSUE=Liver;
PubMed=1848757; DOI=10.1042/bj2740409;
Meyer D.J., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M.,
Ketterer B.;
"Theta, a new class of glutathione transferases purified from rat and
man.";
Biochem. J. 274:409-414(1991).
[6]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Liver, and Lung;
PubMed=8761485; DOI=10.1042/bj3180297;
Mainwaring G.W., Williams S.M., Foster J.R., Tugwood J., Green T.;
"The distribution of theta-class glutathione S-transferases in the
liver and lung of mouse, rat and human.";
Biochem. J. 318:297-303(1996).
-!- FUNCTION: Catalyzes the inactivation of reactive sulfate esters in
carcinogenic arylmethanols. Highest activity towards ethacrynic
acid and cumene hydroperoxide.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8761485}.
Nucleus {ECO:0000269|PubMed:8761485}.
-!- TISSUE SPECIFICITY: Highest values found in liver followed by
testis, adrenal gland, kidney, lung, brain and skeletal muscle. In
liver, highest expression found in central vein limiting plate
hepatocytes. In lung, expressed mainly in Clara cells of the
bronchiolar epithelium and, at low levels, in type II alveolar
cells. {ECO:0000269|PubMed:8761485}.
-!- SIMILARITY: Belongs to the GST superfamily. Theta family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D10026; BAA00916.1; -; mRNA.
EMBL; D38556; BAA07559.1; -; Genomic_DNA.
EMBL; BC061856; AAH61856.1; -; mRNA.
PIR; JC2425; JC2425.
PIR; S14346; S14346.
RefSeq; NP_036928.1; NM_012796.2.
UniGene; Rn.87212; -.
ProteinModelPortal; P30713; -.
SMR; P30713; -.
STRING; 10116.ENSRNOP00000033158; -.
iPTMnet; P30713; -.
PhosphoSitePlus; P30713; -.
PaxDb; P30713; -.
PRIDE; P30713; -.
Ensembl; ENSRNOT00000080203; ENSRNOP00000074436; ENSRNOG00000052415.
Ensembl; ENSRNOT00000081140; ENSRNOP00000071112; ENSRNOG00000052415.
GeneID; 29487; -.
KEGG; rno:29487; -.
UCSC; RGD:69362; rat.
CTD; 2953; -.
RGD; 69362; Gstt2.
eggNOG; KOG0867; Eukaryota.
eggNOG; COG0625; LUCA.
GeneTree; ENSGT00540000069741; -.
HOGENOM; HOG000125747; -.
HOVERGEN; HBG051854; -.
InParanoid; P30713; -.
KO; K00799; -.
OMA; VEEYLSW; -.
OrthoDB; EOG091G0PCG; -.
PhylomeDB; P30713; -.
TreeFam; TF325759; -.
Reactome; R-RNO-156590; Glutathione conjugation.
PRO; PR:P30713; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000052415; -.
ExpressionAtlas; P30713; baseline and differential.
Genevisible; P30713; RN.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD.
GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
GO; GO:0009751; P:response to salicylic acid; IEP:RGD.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00043; GST_C; 1.
Pfam; PF13417; GST_N_3; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1848757,
ECO:0000269|PubMed:2114406}.
CHAIN 2 244 Glutathione S-transferase theta-2.
/FTId=PRO_0000185943.
DOMAIN 2 82 GST N-terminal.
DOMAIN 88 230 GST C-terminal.
REGION 53 54 Glutathione binding. {ECO:0000250}.
REGION 66 67 Glutathione binding. {ECO:0000250}.
BINDING 40 40 Glutathione. {ECO:0000250}.
CONFLICT 14 14 S -> C (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 36 37 LK -> RC (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 42 42 S -> C (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 44 44 Missing (in Ref. 5; AA sequence).
{ECO:0000305}.
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


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