GSTT2_MOUSE
ID GSTT2_MOUSE Reviewed; 244 AA.
AC Q61133; Q61134; Q64472; Q91VB0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Glutathione S-transferase theta-2;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P0CG29};
DE AltName: Full=GST class-theta-2 {ECO:0000303|PubMed:8617493};
GN Name=Gstt2 {ECO:0000303|PubMed:8617493, ECO:0000312|MGI:MGI:106188};
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv, and C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=8617493; DOI=10.1006/geno.1996.0165;
RA Whittington A.T., Webb G.C., Baker R.T., Board P.G.;
RT "Characterization of a cDNA and gene encoding the mouse theta class
RT glutathione transferase mGSTT2 and its localization to chromosome 10B5-
RT C1.";
RL Genomics 33:105-111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
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.
CC {ECO:0000250|UniProtKB:P0CG29}.
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:0000250|UniProtKB:P0CG29};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30713}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8761485}.
CC Nucleus {ECO:0000269|PubMed:8761485}.
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. {ECO:0000269|PubMed:8761485}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U48419; AAB03533.1; -; Genomic_DNA.
DR EMBL; U48420; AAB03534.1; -; mRNA.
DR EMBL; X98056; CAA66666.1; -; mRNA.
DR EMBL; AK002392; BAB22065.1; -; mRNA.
DR EMBL; AK158939; BAE34734.1; -; mRNA.
DR EMBL; AC142499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466553; EDL31881.1; -; Genomic_DNA.
DR EMBL; BC012707; AAH12707.1; -; mRNA.
DR CCDS; CCDS48601.1; -.
DR PIR; S71879; S71879.
DR RefSeq; NP_034491.2; NM_010361.2.
DR RefSeq; XP_006513303.1; XM_006513240.1.
DR AlphaFoldDB; Q61133; -.
DR SMR; Q61133; -.
DR STRING; 10090.ENSMUSP00000046324; -.
DR iPTMnet; Q61133; -.
DR PhosphoSitePlus; Q61133; -.
DR EPD; Q61133; -.
DR jPOST; Q61133; -.
DR PaxDb; Q61133; -.
DR PeptideAtlas; Q61133; -.
DR PRIDE; Q61133; -.
DR ProteomicsDB; 271481; -.
DR DNASU; 14872; -.
DR Ensembl; ENSMUST00000038257; ENSMUSP00000046324; ENSMUSG00000033318.
DR Ensembl; ENSMUST00000220440; ENSMUSP00000151239; ENSMUSG00000033318.
DR GeneID; 14872; -.
DR KEGG; mmu:14872; -.
DR UCSC; uc011xgs.1; mouse.
DR CTD; 2953; -.
DR MGI; MGI:106188; Gstt2.
DR VEuPathDB; HostDB:ENSMUSG00000033318; -.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000162786; -.
DR HOGENOM; CLU_011226_2_0_1; -.
DR InParanoid; Q61133; -.
DR OMA; AYKVRLF; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q61133; -.
DR TreeFam; TF325759; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR BioGRID-ORCS; 14872; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q61133; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q61133; protein.
DR Bgee; ENSMUSG00000033318; Expressed in right kidney and 188 other tissues.
DR ExpressionAtlas; Q61133; baseline and differential.
DR Genevisible; Q61133; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR GO; GO:0004364; F:glutathione transferase activity; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
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..244
FT /note="Glutathione S-transferase theta-2"
FT /id="PRO_0000185941"
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 38
FT /note="Missing (in Ref. 1; AAB03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="S -> R (in Ref. 1; AAB03533)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="A -> G (in Ref. 1; AAB03534)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="C -> Y (in Ref. 1; AAB03534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 27634 MW; 3F45D6E12DA3DF29 CRC64;
MGLELYLDLL SQPSRAVYIF AKKNGIPFQT RTVDILKGQH MSEQFSQVNC LNKVPVLKDG
SFVLTESTAI LIYLSSKYQV ADHWYPADLQ ARAQVHEYLG WHADNIRGTF GVLLWTKVLG
PLIGVQVPQE KVERNRDRMV LVLQQLEDKF LRDRAFLVGQ QVTLADLMSL EELMQPVALG
YNLFEGRPQL TAWRERVEAF LGAELCQEAH STILSILGQA AKKMLPVPPP EVHASMQLRI
ARIP
