GSTA2_MOUSE
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 03-AUG-2022, entry version 167.
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 7,8-Dihydroxy-9,10-epoxy-7,8,9,10-
CC tetrahydrobenzo[a]pyrene {ECO:0000269|PubMed:9606968};
CC Vmax=1295 nmol/min/mg enzyme for 7,8-Dihydroxy-9,10-epoxy-7,8,9,10-
CC tetrahydrobenzo[a]pyrene {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}.
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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; P10648; -.
DR PeptideAtlas; P10648; -.
DR PRIDE; P10648; -.
DR DNASU; 14858; -.
DR Ensembl; ENSMUST00000034902; ENSMUSP00000034902; ENSMUSG00000057933.
DR GeneID; 14858; -.
DR KEGG; mmu:14858; -.
DR UCSC; uc009quf.1; mouse.
DR CTD; 2939; -.
DR MGI; MGI:95863; Gsta2.
DR VEuPathDB; HostDB:ENSMUSG00000057933; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000154526; -.
DR InParanoid; P10648; -.
DR OMA; CKPDILA; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P10648; -.
DR TreeFam; TF105321; -.
DR BioGRID-ORCS; 14858; 2 hits in 36 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 93 other tissues.
DR ExpressionAtlas; P10648; baseline and differential.
DR Genevisible; P10648; 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; 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:0042178; P:xenobiotic catabolic process; ISO:MGI.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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 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; 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 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
