ID   GSTA1_RAT               Reviewed;         222 AA.
AC   P00502; Q6AZ72;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 87.
DE   RecName: Full=Glutathione S-transferase alpha-1;
DE            EC=2.5.1.18;
DE   AltName: Full=Glutathione S-transferase Ya-1;
DE            Short=GST Ya1;
DE   AltName: Full=Ligandin;
DE   AltName: Full=GST 1a-1a;
DE   AltName: Full=GST B;
DE   AltName: Full=GST 1-1;
DE   AltName: Full=GST A1-1;
GN   Name=Gsta1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   MEDLINE=84185691; PubMed=6201485;
RA   Lai H.-C.J., Li N.-Q., Weiss M.J., Reddy C.C., Tu C.-P.D.;
RT   "The nucleotide sequence of a rat liver glutathione S-transferase
RT   subunit cDNA clone.";
RL   J. Biol. Chem. 259:5536-5542(1984).
RN   [2]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 46-197.
RX   MEDLINE=82075944; PubMed=6273441;
RA   Kalinyak J.E., Taylor J.M.;
RT   "Rat glutathione S-transferase. Cloning of double-stranded cDNA and
RT   induction of its mRNA.";
RL   J. Biol. Chem. 257:523-530(1982).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC   -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: In addition to its enzymatic activity, the
CC       homodimer of Ya chains, called ligandin, binds various organic
CC       anions, xenobiotics, and azocarcinogen dyes.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC   -!- SIMILARITY: Contains 1 GST N-terminal domain.
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DR   EMBL; K01931; AAA41283.1; -; mRNA.
DR   EMBL; BC078706; AAH78706.1; -; mRNA.
DR   IPI; IPI00231638; -.
DR   PIR; A24735; A24735.
DR   PIR; A92479; XURTG.
DR   RefSeq; NP_058709.2; -.
DR   UniGene; Rn.144550; -.
DR   PDB; 1EV4; X-ray; 2.20 A; A/C/D=2-219.
DR   PDB; 1EV9; X-ray; 2.20 A; A/C/D=2-221.
DR   PDBsum; 1EV4; -.
DR   PDBsum; 1EV9; -.
DR   PRIDE; P00502; -.
DR   Ensembl; ENSRNOG00000000201; Rattus norvegicus.
DR   GeneID; 24422; -.
DR   KEGG; rno:24422; -.
DR   RGD; 2753; Gsta1.
DR   HOVERGEN; P00502; -.
DR   OMA; P00502; QSHGQDY.
DR   BRENDA; 2.5.1.18; 248.
DR   NextBio; 603283; -.
DR   ArrayExpress; P00502; -.
DR   GermOnline; ENSRNOG00000000201; Rattus norvegicus.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005640; C:nuclear outer membrane; IDA:RGD.
DR   GO; GO:0008144; F:drug binding; IDA:RGD.
DR   GO; GO:0043295; F:glutathione binding; IDA:RGD.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:RGD.
DR   GO; GO:0042493; P:response to drug; NAS:RGD.
DR   GO; GO:0042178; P:xenobiotic catabolic process; IDA:RGD.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
DR   InterPro; IPR003080; GST_alpha.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR11571:SF4; GST_alpha; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Transferase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    222       Glutathione S-transferase alpha-1.
FT                                /FTId=PRO_0000185792.
FT   DOMAIN        3     83       GST N-terminal.
FT   DOMAIN       85    208       GST C-terminal.
FT   CONFLICT    152    152       R -> K (in Ref. 1 and 3).
FT   CONFLICT    208    208       V -> M (in Ref. 1; AAA41283).
FT   STRAND        6     12
FT   HELIX        16     25
FT   STRAND       31     35
FT   HELIX        38     46
FT   STRAND       57     60
FT   STRAND       63     67
FT   HELIX        68     79
FT   HELIX        86    109
FT   HELIX       114    116
FT   HELIX       117    130
FT   HELIX       132    143
FT   STRAND      146    149
FT   HELIX       155    171
FT   HELIX       172    175
FT   HELIX       179    190
FT   HELIX       192    198
FT   HELIX       211    219
SQ   SEQUENCE   222 AA;  25607 MW;  AE43A1BEBE8549CF CRC64;
     MSGKPVLHYF NARGRMECIR WLLAAAGVEF DEKFIQSPED LEKLKKDGNL MFDQVPMVEI
     DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL DLTEMIMQLV ICPPDQKEAK
     TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LELLLYVEEF DASLLTSFPL
     LKAFKSRISS LPNVKKFLQP GSQRKLPVDA KQIEEARKIF KF
//