ID   GSTA2_MOUSE             Reviewed;         222 AA.
AC   P10648; Q6P8Q1;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 3.
DT   24-JAN-2024, entry version 175.
DE   RecName: Full=Glutathione S-transferase A2;
DE            EC=2.5.1.18 {ECO:0000269|PubMed:9606968};
DE   AltName: Full=GST class-alpha member 2;
DE   AltName: Full=Glutathione S-transferase GT41A;
GN   Name=Gsta2;
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 [MRNA].
RX   PubMed=3417659; DOI=10.1016/s0021-9258(18)37708-1;
RA   Pearson W.R., Reinhart J., Sisk S.C., Anderson K.S., Adler P.N.;
RT   "Tissue-specific induction of murine glutathione transferase mRNAs by
RT   butylated hydroxyanisole.";
RL   J. Biol. Chem. 263:13324-13332(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=9606968; DOI=10.1006/abbi.1998.0668;
RA   Xia H., Pan S.S., Hu X., Srivastava S.K., Pal A., Singh S.V.;
RT   "Cloning, expression, and biochemical characterization of a functionally
RT   novel alpha class glutathione S-transferase with exceptional activity in
RT   the glutathione conjugation of (+)-anti-7,8-dihydroxy-9,10-oxy-7,8,9,10-
RT   tetrahydrobenzo(a)pyrene.";
RL   Arch. Biochem. Biophys. 353:337-348(1998).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND
RP   SUBSTRATE ANALOG, AND SUBUNIT.
RX   PubMed=12549910; DOI=10.1021/bi026778+;
RA   Gu Y., Xiao B., Wargo H.L., Bucher M.H., Singh S.V., Ji X.;
RT   "Residues 207, 216, and 221 and the catalytic activity of mGSTA1-1 and
RT   mGSTA2-2 toward benzo[a]pyrene-(7R,8S)-diol-(9S,10R)-epoxide.";
RL   Biochemistry 42:917-921(2003).
CC   -!- FUNCTION: Catalyzes the conjugation of glutathione to a large variety
CC       of electrophilic compounds. {ECO:0000269|PubMed:9606968}.
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:9606968};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC         Evidence={ECO:0000305|PubMed:9606968};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=31 uM for
CC         7,8-Dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene
CC         {ECO:0000269|PubMed:9606968};
CC         Vmax=1295 nmol/min/mg enzyme for
CC         7,8-Dihydroxy-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene
CC         {ECO:0000269|PubMed:9606968};
CC   -!- SUBUNIT: Homodimer (PubMed:12549910). Heterodimer of GSTA1 and GSTA2
CC       (By similarity). {ECO:0000250|UniProtKB:P09210,
CC       ECO:0000269|PubMed:12549910}.
CC   -!- TISSUE SPECIFICITY: Expressed in the kidney.
CC       {ECO:0000269|PubMed:9606968}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha 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; J03958; AAA37749.1; -; mRNA.
DR   EMBL; AC138587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466522; EDL26384.1; -; Genomic_DNA.
DR   EMBL; CH466522; EDL26385.1; -; Genomic_DNA.
DR   EMBL; CH466522; EDL26386.1; -; Genomic_DNA.
DR   EMBL; CH466522; EDL26387.1; -; Genomic_DNA.
DR   EMBL; BC061133; AAH61133.1; -; mRNA.
DR   CCDS; CCDS23359.1; -.
DR   RefSeq; NP_032208.2; NM_008182.3.
DR   RefSeq; XP_006510877.1; XM_006510814.2.
DR   PDB; 1ML6; X-ray; 1.90 A; A/B=2-222.
DR   PDBsum; 1ML6; -.
DR   AlphaFoldDB; P10648; -.
DR   SMR; P10648; -.
DR   STRING; 10090.ENSMUSP00000034902; -.
DR   iPTMnet; P10648; -.
DR   PhosphoSitePlus; P10648; -.
DR   jPOST; P10648; -.
DR   PaxDb; 10090-ENSMUSP00000034902; -.
DR   PeptideAtlas; P10648; -.
DR   DNASU; 14858; -.
DR   Ensembl; ENSMUST00000034902.12; ENSMUSP00000034902.6; ENSMUSG00000057933.11.
DR   GeneID; 14858; -.
DR   KEGG; mmu:14858; -.
DR   UCSC; uc009quf.1; mouse.
DR   AGR; MGI:95863; -.
DR   CTD; 2939; -.
DR   MGI; MGI:95863; Gsta2.
DR   VEuPathDB; HostDB:ENSMUSG00000057933; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000154526; -.
DR   InParanoid; P10648; -.
DR   OMA; EMIMQLP; -.
DR   OrthoDB; 3412208at2759; -.
DR   PhylomeDB; P10648; -.
DR   TreeFam; TF105321; -.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   Reactome; R-MMU-189483; Heme degradation.
DR   Reactome; R-MMU-9748787; Azathioprine ADME.
DR   BioGRID-ORCS; 14858; 2 hits in 41 CRISPR screens.
DR   ChiTaRS; Gsta2; mouse.
DR   EvolutionaryTrace; P10648; -.
DR   PRO; PR:P10648; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P10648; Protein.
DR   Bgee; ENSMUSG00000057933; Expressed in epithelium of stomach and 94 other cell types or tissues.
DR   ExpressionAtlas; P10648; baseline and differential.
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; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0004769; F:steroid delta-isomerase activity; ISO:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR   GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
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; SFLDG01205; AMPS.1; 1.
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.
DR   Genevisible; P10648; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
FT   CHAIN           2..222
FT                   /note="Glutathione S-transferase A2"
FT                   /id="PRO_0000185789"
FT   DOMAIN          3..83
FT                   /note="GST N-terminal"
FT   DOMAIN          85..208
FT                   /note="GST C-terminal"
FT   BINDING         9
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   BINDING         45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:12549910"
FT   BINDING         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:12549910"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:12549910"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
FT   MOD_RES         4
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
FT   CONFLICT        199
FT                   /note="H -> Q (in Ref. 1; AAA37749)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..12
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           14..16
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           17..26
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   STRAND          31..35
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           38..46
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           68..78
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           86..108
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           117..130
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           132..143
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           155..171
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           179..190
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           192..198
FT                   /evidence="ECO:0007829|PDB:1ML6"
FT   HELIX           210..219
FT                   /evidence="ECO:0007829|PDB:1ML6"
SQ   SEQUENCE   222 AA;  25542 MW;  837FFFC49C56F70F CRC64;
     MAGKPVLHYF NARGRMECIR WLLAAAGVEF EEKFIQSPED LEKLKKDGNL MFDQVPMVEI
     DGMKLVQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL DLTEMIGQLV LCPPDQREAK
     TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDVHL LELLLYVEEL DASLLTPFPL
     LKAFKSRISS LPNVKKFLHP GSQRKPPLDA KQIEEARKVF KF
//