ID   GSTT4_MOUSE             Reviewed;         240 AA.
AC   Q9D4P7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 151.
DE   RecName: Full=Glutathione S-transferase theta-4 {ECO:0000305};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P30711};
DE   AltName: Full=GST class-theta-4;
GN   Name=Gstt4 {ECO:0000312|MGI:MGI:1923136};
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000250|UniProtKB:P30711}.
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:P30711};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; AK016340; BAB30196.1; -; mRNA.
DR   EMBL; BC061011; AAH61011.1; -; mRNA.
DR   CCDS; CCDS23933.1; -.
DR   RefSeq; NP_083748.3; NM_029472.3.
DR   AlphaFoldDB; Q9D4P7; -.
DR   SMR; Q9D4P7; -.
DR   STRING; 10090.ENSMUSP00000125604; -.
DR   PhosphoSitePlus; Q9D4P7; -.
DR   PaxDb; 10090-ENSMUSP00000125604; -.
DR   ProteomicsDB; 271344; -.
DR   Antibodypedia; 78380; 7 antibodies from 4 providers.
DR   DNASU; 75886; -.
DR   Ensembl; ENSMUST00000160211.2; ENSMUSP00000125604.2; ENSMUSG00000009093.8.
DR   GeneID; 75886; -.
DR   KEGG; mmu:75886; -.
DR   UCSC; uc007fre.2; mouse.
DR   AGR; MGI:1923136; -.
DR   CTD; 25774; -.
DR   MGI; MGI:1923136; Gstt4.
DR   VEuPathDB; HostDB:ENSMUSG00000009093; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   GeneTree; ENSGT00940000161301; -.
DR   HOGENOM; CLU_011226_2_0_1; -.
DR   InParanoid; Q9D4P7; -.
DR   OMA; IQQPMSK; -.
DR   OrthoDB; 1199296at2759; -.
DR   PhylomeDB; Q9D4P7; -.
DR   TreeFam; TF325759; -.
DR   BioGRID-ORCS; 75886; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Gstt4; mouse.
DR   PRO; PR:Q9D4P7; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9D4P7; Protein.
DR   Bgee; ENSMUSG00000009093; Expressed in seminiferous tubule of testis and 10 other cell types or tissues.
DR   ExpressionAtlas; Q9D4P7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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:SF13; GLUTATHIONE S-TRANSFERASE THETA-4-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 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; Q9D4P7; MM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..240
FT                   /note="Glutathione S-transferase theta-4"
FT                   /id="PRO_0000329076"
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT   DOMAIN          88..217
FT                   /note="GST C-terminal"
FT   BINDING         40
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
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"
SQ   SEQUENCE   240 AA;  28099 MW;  C07B5C904C4A0C7E CRC64;
     MGLELYMDLL SAPCRAVYIF ARKNGIPFDF QFVDLLKGHH HSKEYIEINP LRKLPSLKDG
     KFILSESVAI LFYLCRKYSA PSHWYPPDLH MRARVDEFMA WQHTAIQVPM SKILWIKLII
     PMITGEEVPT ERLEKTLDEV KRNLQQFEEK FLQDKMFITG DHISLADLVA LVEMMQPMGS
     NHNVFVSSKL AEWRMRVELA IGSGLFWEAH ERLVKLPNWD CSTLDPTIKM RICDFLQKFK
//