GSTA1_MOUSE
ID GSTA1_MOUSE Reviewed; 223 AA.
AC P13745; A2RTN4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Glutathione S-transferase A1 {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000269|PubMed:9606968, ECO:0000305|PubMed:11027134};
DE AltName: Full=13-hydroperoxyoctadecadienoate peroxidase {ECO:0000250|UniProtKB:P08263};
DE EC=1.11.1.- {ECO:0000250|UniProtKB:P08263};
DE AltName: Full=Androst-5-ene-3,17-dione isomerase {ECO:0000250|UniProtKB:P08263};
DE EC=5.3.3.- {ECO:0000250|UniProtKB:P08263};
DE AltName: Full=GST class-alpha member 1;
DE AltName: Full=Glutathione S-transferase Ya;
DE AltName: Full=Glutathione S-transferase Ya1;
DE Contains:
DE RecName: Full=Glutathione S-transferase A1, N-terminally processed;
GN Name=Gsta1; Synonyms=Gsta, Gstya;
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 [GENOMIC DNA].
RX PubMed=3652905; DOI=10.1089/dna.1987.6.317;
RA Daniel V., Sharon R., Tichauer Y., Sarid S.;
RT "Mouse glutathione S-transferase Ya subunit: gene structure and sequence.";
RL DNA 6:317-324(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, 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 MRNA].
RC TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 16-36; 51-59; 63-165 AND 208-223, AND INDUCTION.
RC TISSUE=Liver;
RX PubMed=2049074; DOI=10.1042/bj2760461;
RA McLellan L.I., Kerr L.A., Cronshaw A.D., Hayes J.D.;
RT "Regulation of mouse glutathione S-transferases by chemoprotectors.
RT Molecular evidence for the existence of three distinct alpha-class
RT glutathione S-transferase subunits, Ya1, Ya2, and Ya3, in mouse liver.";
RL Biochem. J. 276:461-469(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND
RP SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND REGION.
RX PubMed=11027134; DOI=10.1021/bi001396u;
RA Gu Y., Singh S.V., Ji X.;
RT "Residue R216 and catalytic efficiency of a murine class alpha glutathione
RT S-transferase toward benzo[a]pyrene 7(R),8(S)-diol 9(S), 10(R)-epoxide.";
RL Biochemistry 39:12552-12557(2000).
CC -!- FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic
CC attack of the sulfur atom of glutathione on the electrophilic groups of
CC a wide range of exogenous and endogenous compounds (PubMed:9606968).
CC Involved in the formation of glutathione conjugates of both
CC prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). It also catalyzes
CC the isomerization of D5-androstene-3,17-dione (AD) into D4-androstene-
CC 3,17-dione and may therefore play an important role in hormone
CC biosynthesis. Through its glutathione-dependent peroxidase activity
CC toward the fatty acid hydroperoxide (13S)-hydroperoxy-(9Z,11E)-
CC octadecadienoate/13-HPODE it is also involved in the metabolism of
CC oxidized linoleic acid (By similarity). {ECO:0000250|UniProtKB:P08263,
CC ECO:0000269|PubMed:9606968, ECO:0000305|PubMed:11027134}.
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; Evidence={ECO:0000269|PubMed:9606968,
CC ECO:0000305|PubMed:11027134};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000305|PubMed:11027134};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133768;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133771;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione =
CC (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide +
CC H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione;
CC Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35 uM for 7,8-Dihydroxy-9,10-epoxy-7,8,9,10-
CC tetrahydrobenzo[a]pyrene {ECO:0000269|PubMed:9606968};
CC Vmax=5200 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. {ECO:0000269|PubMed:11027134}.
CC -!- TISSUE SPECIFICITY: Expressed in the liver, skin and kidney.
CC {ECO:0000269|PubMed:9606968}.
CC -!- INDUCTION: Induced in the liver by beta-naphthoflavone (BNF) and 2(3)-
CC t-butyl-4-hydroxyanisole (BHA). {ECO:0000269|PubMed:2049074}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
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DR EMBL; M19256; AAA37750.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M19251; AAA37750.1; JOINED; Genomic_DNA.
DR EMBL; M19252; AAA37750.1; JOINED; Genomic_DNA.
DR EMBL; M19253; AAA37750.1; JOINED; Genomic_DNA.
DR EMBL; M19254; AAA37750.1; JOINED; Genomic_DNA.
DR EMBL; M19255; AAA37750.1; JOINED; Genomic_DNA.
DR EMBL; BC132572; AAI32573.1; -; mRNA.
DR EMBL; BC132576; AAI32577.1; -; mRNA.
DR CCDS; CCDS23358.1; -.
DR PIR; A27848; A27848.
DR RefSeq; NP_032207.3; NM_008181.3.
DR PDB; 1F3A; X-ray; 1.90 A; A/B=2-223.
DR PDB; 1F3B; X-ray; 2.00 A; A/B=2-223.
DR PDBsum; 1F3A; -.
DR PDBsum; 1F3B; -.
DR AlphaFoldDB; P13745; -.
DR SMR; P13745; -.
DR BioGRID; 200090; 2.
DR STRING; 10090.ENSMUSP00000096139; -.
DR iPTMnet; P13745; -.
DR PhosphoSitePlus; P13745; -.
DR jPOST; P13745; -.
DR MaxQB; P13745; -.
DR PaxDb; P13745; -.
DR PeptideAtlas; P13745; -.
DR PRIDE; P13745; -.
DR DNASU; 14857; -.
DR Ensembl; ENSMUST00000098537; ENSMUSP00000096139; ENSMUSG00000074183.
DR GeneID; 14857; -.
DR KEGG; mmu:14857; -.
DR UCSC; uc009qtz.1; mouse.
DR CTD; 2938; -.
DR MGI; MGI:1095417; Gsta1.
DR VEuPathDB; HostDB:ENSMUSG00000074183; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000154526; -.
DR HOGENOM; CLU_039475_4_0_1; -.
DR InParanoid; P13745; -.
DR OMA; SEMIMLL; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P13745; -.
DR TreeFam; TF105321; -.
DR BioGRID-ORCS; 14857; 2 hits in 24 CRISPR screens.
DR EvolutionaryTrace; P13745; -.
DR PRO; PR:P13745; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P13745; protein.
DR Bgee; ENSMUSG00000074183; Expressed in duodenum and 53 other tissues.
DR Genevisible; P13745; 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; ISS:UniProtKB.
DR GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin 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; Direct protein sequencing; Isomerase;
KW Lipid metabolism; Oxidoreductase; Peroxidase; Reference proteome;
KW Transferase.
FT CHAIN 1..223
FT /note="Glutathione S-transferase A1"
FT /id="PRO_0000423204"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT CHAIN 2..223
FT /note="Glutathione S-transferase A1, N-terminally
FT processed"
FT /id="PRO_0000185788"
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:0000305|PubMed:11027134"
FT BINDING 45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:11027134"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:11027134"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:11027134"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P80894"
FT MOD_RES 2
FT /note="N-acetylalanine; in Glutathione S-transferase A1, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1F3A"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:1F3A"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:1F3A"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1F3A"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 86..108
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1F3A"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:1F3A"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 155..171
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:1F3A"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:1F3A"
SQ SEQUENCE 223 AA; 25608 MW; A348A07133FBEC1D CRC64;
MAGKPVLHYF NARGRMECIR WLLAAAGVEF EEKFIQSPED LEKLKKDGNL MFDQVPMVEI
DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYSEGIL DLTEMIGQLV LCPPDQREAK
TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LEVLLYVEEF DASLLTPFPL
LKAFKSRISS LPNVKKFLQP GSQRKPPMDA KQIQEARKAF KIQ
