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Database: UniProt
Entry: Q6P8Q0_MOUSE
LinkDB: Q6P8Q0_MOUSE
Original site: Q6P8Q0_MOUSE 
ID   Q6P8Q0_MOUSE            Unreviewed;       223 AA.
AC   Q6P8Q0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU003494};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU003494};
GN   Name=Gsta13 {ECO:0000313|Ensembl:ENSMUSP00000150224.2};
GN   Synonyms=Gsta1 {ECO:0000313|EMBL:AAH61134.1};
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:0000313|EMBL:AAH61134.1};
RN   [1] {ECO:0000313|EMBL:AAH61134.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:AAH61134.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [2] {ECO:0000313|Ensembl:ENSMUSP00000150224.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000150224.2,
RC   ECO:0000313|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   [3] {ECO:0000313|Ensembl:ENSMUSP00000150224.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000150224.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|RuleBase:RU003494};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000256|ARBA:ARBA00011055, ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; BC061134; AAH61134.1; -; mRNA.
DR   RefSeq; NP_001230021.1; NM_001243092.1.
DR   STRING; 10090.ENSMUSP00000150224; -.
DR   ProteomicsDB; 337093; -.
DR   Ensembl; ENSMUST00000217203.2; ENSMUSP00000150224.2; ENSMUSG00000111709.2.
DR   GeneID; 100042295; -.
DR   KEGG; mmu:100042295; -.
DR   UCSC; uc009qub.2; mouse.
DR   AGR; MGI:3826440; -.
DR   CTD; 100042295; -.
DR   MGI; MGI:3826440; Gsta13.
DR   VEuPathDB; HostDB:ENSMUSG00000111709; -.
DR   GeneTree; ENSGT00940000154526; -.
DR   OMA; FTEMIMN; -.
DR   OrthoDB; 3412208at2759; -.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   Reactome; R-MMU-189483; Heme degradation.
DR   Reactome; R-MMU-9748787; Azathioprine ADME.
DR   BioGRID-ORCS; 100042295; 1 hit in 26 CRISPR screens.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000111709; Expressed in duodenum and 49 other cell types or tissues.
DR   Genevisible; Q6P8Q0; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0035731; F:dinitrosyl-iron complex binding; ISO:MGI.
DR   GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR   GO; GO:0043295; F:glutathione binding; ISO:MGI.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR   GO; GO:0004364; F:glutathione transferase activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0004769; F:steroid delta-isomerase activity; ISO:MGI.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd03208; GST_C_Alpha; 1.
DR   CDD; cd03077; GST_N_Alpha; 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; IPR003080; GST_alpha.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF233; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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.
PE   2: Evidence at transcript level;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transferase {ECO:0000256|RuleBase:RU003494, ECO:0000313|EMBL:AAH61134.1}.
FT   DOMAIN          3..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          85..208
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   223 AA;  25582 MW;  B9E9016B225AF17D CRC64;
     MAGKPVLHHF NARGRMECIR WLLAAAGVEF EEKFIQSPED LEKLKKDGNL MFDQVPMVEI
     DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYSEGIL DLTEMIGQLV LCPPDQREAK
     TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LEVLLYVEEF DASLLTPFPL
     LKAFKSRISS LPNVKKFLQP GSQRKPPMDA KQIQEARKAF KIQ
//
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