GSTT3_MOUSE
ID GSTT3_MOUSE Reviewed; 241 AA.
AC Q99L20; Q6P6I4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Glutathione S-transferase theta-3 {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000269|PubMed:12038961};
GN Name=Gstt3 {ECO:0000303|PubMed:12038961};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:AAM33420.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAM33420.1};
RX PubMed=12038961; DOI=10.1042/bj20011878;
RA Coggan M., Flanagan J.U., Parker M.W., Vichai V., Pearson W.R., Board P.G.;
RT "Identification and characterization of GSTT3, a third murine Theta class
RT glutathione transferase.";
RL Biochem. J. 366:323-332(2002).
RN [2] {ECO:0000312|EMBL:BAE23741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589}, and NOD;
RC TISSUE=Spinal cord {ECO:0000312|Proteomes:UP000000589};
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 [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [4] {ECO:0000312|EMBL:EDL31889.1}
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAH03903.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH03903.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH03903.1}, and
RC Salivary gland {ECO:0000312|EMBL:AAH62201.1};
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC 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. Shows high activity
CC towards 4-nitrobenzyl chloride (4-NBC). Also has lower activity towards
CC 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP), cumene hydroperoxide, 1-
CC chloro-2,4-dinitrobenzene (CDNB), 7-chloro-4-nitrobenzo-2-oxa-1,3-
CC diazole (NBD-Cl), and ethacrynic acid. {ECO:0000269|PubMed:12038961}.
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:12038961};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in liver, and at lower levels in
CC kidney and testis. {ECO:0000269|PubMed:12038961}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000305}.
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DR EMBL; AF508157; AAM33420.1; -; mRNA.
DR EMBL; AK138669; BAE23741.1; -; mRNA.
DR EMBL; AK154161; BAE32415.1; -; mRNA.
DR EMBL; AK168226; BAE40180.1; -; mRNA.
DR EMBL; AC142499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466553; EDL31889.1; -; Genomic_DNA.
DR EMBL; BC003903; AAH03903.1; -; mRNA.
DR EMBL; BC057964; AAH57964.1; -; mRNA.
DR EMBL; BC062201; AAH62201.1; -; mRNA.
DR CCDS; CCDS23931.1; -.
DR RefSeq; NP_001333452.1; NM_001346523.1.
DR RefSeq; NP_598755.1; NM_133994.3.
DR AlphaFoldDB; Q99L20; -.
DR SMR; Q99L20; -.
DR STRING; 10090.ENSMUSP00000001715; -.
DR iPTMnet; Q99L20; -.
DR PhosphoSitePlus; Q99L20; -.
DR SwissPalm; Q99L20; -.
DR EPD; Q99L20; -.
DR jPOST; Q99L20; -.
DR MaxQB; Q99L20; -.
DR PaxDb; Q99L20; -.
DR PRIDE; Q99L20; -.
DR ProteomicsDB; 271482; -.
DR DNASU; 103140; -.
DR Ensembl; ENSMUST00000001715; ENSMUSP00000001715; ENSMUSG00000001665.
DR GeneID; 103140; -.
DR KEGG; mmu:103140; -.
DR UCSC; uc007frb.1; mouse.
DR CTD; 103140; -.
DR MGI; MGI:2143526; Gstt3.
DR VEuPathDB; HostDB:ENSMUSG00000001665; -.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000156366; -.
DR InParanoid; Q99L20; -.
DR OMA; NYSYIAH; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q99L20; -.
DR TreeFam; TF325759; -.
DR BioGRID-ORCS; 103140; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Gstt3; mouse.
DR PRO; PR:Q99L20; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q99L20; protein.
DR Bgee; ENSMUSG00000001665; Expressed in prostate gland ventral lobe and 167 other tissues.
DR ExpressionAtlas; Q99L20; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IDA: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; Reference proteome; Transferase.
FT CHAIN 1..241
FT /note="Glutathione S-transferase theta-3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437667"
FT DOMAIN 2..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 88..222
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT BINDING 53..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P30711"
FT BINDING 66..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P30711"
FT CONFLICT 134
FT /note="A -> V (in Ref. 5; AAH62201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 27403 MW; 529FAA54F355D0A0 CRC64;
MGLELYLDLM SQPCRAVYIF AKKNGIPFQL RTIELLKGQQ YTDSFAQVNP LRKVPALKDG
DFVLAESVAI LLYLSRKYKA PDHWYPQDLQ TRARVDEYLA WQHTALRSCC TRAMWQKMMF
PVFLGQPVPP EMLASTLAEL DGCLQVLEDK FLRNQAFLTG SHISVADLVA ITELMHPVSA
GCKIFESRPK LAAWRQRVEA EVGESLFQEA HEVVLKAKDM PPLMDPALKE KLKLSVQCLL
H
