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Database: UniProt
Entry: D3YZV3_MOUSE
LinkDB: D3YZV3_MOUSE
Original site: D3YZV3_MOUSE 
ID   D3YZV3_MOUSE            Unreviewed;       182 AA.
AC   D3YZV3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU003494};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU003494};
DE   Flags: Fragment;
GN   Name=Gsta2 {ECO:0000313|Ensembl:ENSMUSP00000115517.2,
GN   ECO:0000313|MGI:MGI:95863};
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|Ensembl:ENSMUSP00000115517.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000115517.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000115517.2,
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   [2] {ECO:0000313|Ensembl:ENSMUSP00000115517.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000115517.2};
RG   Ensembl;
RL   Submitted (JUL-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|ARBA:ARBA00035754};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC         Evidence={ECO:0000256|ARBA:ARBA00035754};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000256|ARBA:ARBA00011055, ECO:0000256|RuleBase:RU003494}.
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DR   AlphaFoldDB; D3YZV3; -.
DR   SMR; D3YZV3; -.
DR   jPOST; D3YZV3; -.
DR   MaxQB; D3YZV3; -.
DR   PeptideAtlas; D3YZV3; -.
DR   Ensembl; ENSMUST00000125479.8; ENSMUSP00000115517.2; ENSMUSG00000057933.11.
DR   AGR; MGI:95863; -.
DR   MGI; MGI:95863; Gsta2.
DR   VEuPathDB; HostDB:ENSMUSG00000057933; -.
DR   GeneTree; ENSGT00940000154526; -.
DR   HOGENOM; CLU_039475_4_0_1; -.
DR   OMA; EMIMQLP; -.
DR   ChiTaRS; Gsta2; mouse.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000057933; Expressed in epithelium of stomach and 94 other cell types or tissues.
DR   ExpressionAtlas; D3YZV3; baseline and differential.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
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; 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; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 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   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|PeptideAtlas:D3YZV3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transferase {ECO:0000256|RuleBase:RU003494}.
FT   DOMAIN          3..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          85..182
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   NON_TER         182
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000115517.2"
SQ   SEQUENCE   182 AA;  20936 MW;  7DDF69CFE04FAF73 CRC64;
     MAGKPVLHYF NARGRMECIR WLLAAAGVEF EEKFIQSPED LEKLKKDGNL MFDQVPMVEI
     DGMKLVQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL DLTEMIGQLV LCPPDQREAK
     TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDVHL LELLLYVEEL DASLLTPFPL
     LK
//
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