ID GSTA2_RAT Reviewed; 222 AA.
AC P04903; Q63715;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 24-JAN-2024, entry version 162.
DE RecName: Full=Glutathione S-transferase alpha-2;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P10648};
DE AltName: Full=GST 1b-1b;
DE AltName: Full=GST A2-2;
DE AltName: Full=Glutathione S-transferase Ya-2;
DE Short=GST Ya2;
GN Name=Gsta2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=6325423; DOI=10.1016/s0021-9258(17)42973-5;
RA Pickett C.B., Telakowski-Hopkins C.A., Ding G.J.-F., Argenbright L.,
RA Lu A.Y.H.;
RT "Rat liver glutathione S-transferases. Complete nucleotide sequence of a
RT glutathione S-transferase mRNA and the regulation of the Ya, Yb, and Yc
RT mRNAs by 3-methylcholanthrene and phenobarbital.";
RL J. Biol. Chem. 259:5182-5188(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3766257; DOI=10.1007/978-1-4684-5134-4_15;
RA Pickett C.B., Telakowsi-Hopkins C.A., Ding G.J.-F., Ding V.D.-H.;
RT "Expression and sequence analysis of rat liver glutathione S-transferase
RT genes.";
RL Adv. Exp. Med. Biol. 197:185-193(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3025841; DOI=10.1073/pnas.83.24.9393;
RA Telakowski-Hopkins C.A., Rothkopf G.S., Pickett C.B.;
RT "Structural analysis of a rat liver glutathione S-transferase Ya gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9393-9397(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-129.
RX PubMed=6547043; DOI=10.1042/bj2190223;
RA Taylor J.B., Craig R.K., Beale D., Ketterer B.;
RT "Construction and characterization of a plasmid containing complementary
RT DNA to mRNA encoding the N-terminal amino acid sequence of the rat
RT glutathione transferase Ya subunit.";
RL Biochem. J. 219:223-231(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
RC TISSUE=Liver;
RX PubMed=2645828; DOI=10.1016/0003-9861(89)90137-9;
RA Wang R.W., Pickett C.B., Lu A.Y.H.;
RT "Expression of a cDNA encoding a rat liver glutathione S-transferase Ya
RT subunit in Escherichia coli.";
RL Arch. Biochem. Biophys. 269:536-543(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 81-222.
RX PubMed=6292839; DOI=10.1093/nar/10.18.5407;
RA Tu C.-P.D., Weiss M.J., Karakawa W.W., Reddy C.C.;
RT "Cloning and sequence analysis of a cDNA plasmid for one of the rat liver
RT glutathione S-transferase subunits.";
RL Nucleic Acids Res. 10:5407-5419(1982).
CC -!- FUNCTION: Catalyzes the conjugation of glutathione to a large variety
CC of electrophilic compounds. {ECO:0000250|UniProtKB:P10648}.
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:0000250|UniProtKB:P10648};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000250|UniProtKB:P10648};
CC -!- SUBUNIT: Homodimer or heterodimer of GSTA1 and GSTA2.
CC {ECO:0000250|UniProtKB:P09210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: In addition to its enzymatic activity, the homodimer of
CC Ya chains, called ligandin, binds various organic anions, xenobiotics,
CC and azocarcinogen dyes.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
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DR EMBL; K00136; AAA41282.1; -; mRNA.
DR EMBL; M25891; AAA41290.1; -; mRNA.
DR EMBL; M14991; AAA41295.1; -; Genomic_DNA.
DR EMBL; M14986; AAA41295.1; JOINED; Genomic_DNA.
DR EMBL; M14987; AAA41295.1; JOINED; Genomic_DNA.
DR EMBL; M14988; AAA41295.1; JOINED; Genomic_DNA.
DR EMBL; M14989; AAA41295.1; JOINED; Genomic_DNA.
DR EMBL; M14990; AAA41295.1; JOINED; Genomic_DNA.
DR EMBL; X00520; CAA25203.1; -; mRNA.
DR EMBL; M27446; AAA41291.1; -; mRNA.
DR PIR; A24735; A24735.
DR PIR; A26653; A26653.
DR PIR; A92479; XURTG.
DR RefSeq; NP_001010921.1; NM_001010921.1.
DR PDB; 5LCZ; X-ray; 2.33 A; A/B=54-65, A/B=86-213.
DR PDB; 5LD0; X-ray; 1.60 A; A=86-213.
DR PDBsum; 5LCZ; -.
DR PDBsum; 5LD0; -.
DR AlphaFoldDB; P04903; -.
DR SMR; P04903; -.
DR BioGRID; 268945; 1.
DR STRING; 10116.ENSRNOP00000043510; -.
DR CarbonylDB; P04903; -.
DR PaxDb; 10116-ENSRNOP00000043510; -.
DR Ensembl; ENSRNOT00055007487; ENSRNOP00055005614; ENSRNOG00055004709.
DR Ensembl; ENSRNOT00060033749; ENSRNOP00060027638; ENSRNOG00060019510.
DR Ensembl; ENSRNOT00065028083; ENSRNOP00065022199; ENSRNOG00065016820.
DR GeneID; 494499; -.
DR KEGG; rno:494499; -.
DR UCSC; RGD:2754; rat.
DR AGR; RGD:1593189; -.
DR CTD; 221357; -.
DR RGD; 2754; Gsta2.
DR eggNOG; KOG1695; Eukaryota.
DR InParanoid; P04903; -.
DR OrthoDB; 3412208at2759; -.
DR PhylomeDB; P04903; -.
DR BRENDA; 2.5.1.18; 5301.
DR Reactome; R-RNO-156590; Glutathione conjugation.
DR Reactome; R-RNO-189483; Heme degradation.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR PRO; PR:P04903; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0035731; F:dinitrosyl-iron complex binding; IPI:RGD.
DR GO; GO:0043295; F:glutathione binding; IDA:CAFA.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:CAFA.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0035634; P:response to stilbenoid; ISO:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:CAFA.
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; 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 3D-structure; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="Glutathione S-transferase alpha-2"
FT /id="PRO_0000185793"
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:0000250|UniProtKB:P13745"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P30711"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P13745"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT HELIX 86..111
FT /evidence="ECO:0007829|PDB:5LD0"
FT HELIX 114..130
FT /evidence="ECO:0007829|PDB:5LD0"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:5LD0"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:5LD0"
FT HELIX 155..171
FT /evidence="ECO:0007829|PDB:5LD0"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:5LD0"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:5LD0"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:5LD0"
SQ SEQUENCE 222 AA; 25559 MW; AA342417E9857A9F CRC64;
MSGKPVLHYF NARGRMECIR WLLAAAGVEF EEKLIQSPED LEKLKKDGNL MFDQVPMVEI
DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYSEGIL DLTEMIIQLV ICPPDQREAK
TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LELLLYVEEF DASLLTSFPL
LKAFKSRISS LPNVKKFLQP GSQRKPAMDA KQIEEARKVF KF
//
