ID   GSTA5_RAT               Reviewed;         221 AA.
AC   P46418; Q6LD91;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 72.
DE   RecName: Full=Glutathione S-transferase alpha-5;
DE            EC=2.5.1.18;
DE   AltName: Full=Glutathione S-transferase Yc-2;
DE            Short=GST Yc2;
DE   AltName: Full=GST A5-5;
GN   Name=Gsta5; Synonyms=Gstyc2;
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=Fischer 344; TISSUE=Liver;
RX   MEDLINE=94327654; PubMed=8051171;
RA   Hayes J.D., Nguyen T., Judah D.J., Petersson D.G., Neal G.E.;
RT   "Cloning of cDNAs from fetal rat liver encoding glutathione S-
RT   transferase Yc polypeptides. The Yc2 subunit is expressed in adult rat
RT   liver resistant to the hepatocarcinogen aflatoxin B1.";
RL   J. Biol. Chem. 269:20707-20717(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96358489; PubMed=8761455;
RA   Pulford D.J., Hayes J.D.;
RT   "Characterization of the rat glutathione S-transferase Yc2 subunit
RT   gene, GSTA5: identification of a putative antioxidant-responsive
RT   element in the 5'-flanking region of rat GSTA5 that may mediate
RT   chemoprotection against aflatoxin B1.";
RL   Biochem. J. 318:75-84(1996).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Fischer 344; TISSUE=Liver;
RX   MEDLINE=92061940; PubMed=1953636;
RA   Hayes J.D., Judah D.J., McLellan L.I., Kerr L.A., Peacock S.D.,
RA   Neal G.E.;
RT   "Ethoxyquin-induced resistance to aflatoxin B1 in the rat is
RT   associated with the expression of a novel alpha-class glutathione S-
RT   transferase subunit, Yc2, which possesses high catalytic activity for
RT   aflatoxin B1-8,9-epoxide.";
RL   Biochem. J. 279:385-398(1991).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. Has
CC       substantial activity toward aflatoxin B1-8,9-epoxide.
CC   -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
CC   -!- SUBUNIT: Heterodimer of YC1 and YC2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Liver, nasal mucosa and epididymis.
CC   -!- DEVELOPMENTAL STAGE: Liver from adult female rats contains about
CC       10-fold greater levels of YC2 than is found in liver from adult
CC       male rats.
CC   -!- INDUCTION: By ethoxyquin, oltipraz, butylated hydroxyanisole, and
CC       phenobarbitol.
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; X78847; CAA55404.1; -; mRNA.
DR   EMBL; S72506; AAP21065.1; -; mRNA.
DR   EMBL; S82820; AAB46796.1; -; mRNA.
DR   IPI; IPI00211897; -.
DR   PIR; A54858; A54858.
DR   RefSeq; NP_001009920.1; -.
DR   UniGene; Rn.120929; -.
DR   HSSP; P08263; 1K3O.
DR   SMR; P46418; 4-220.
DR   PRIDE; P46418; -.
DR   Ensembl; ENSRNOG00000029711; Rattus norvegicus.
DR   GeneID; 494500; -.
DR   KEGG; rno:494500; -.
DR   NMPDR; fig|10116.3.peg.29792; -.
DR   RGD; 2753; Gsta5.
DR   HOVERGEN; P46418; -.
DR   OMA; P46418; KCVESAK.
DR   BRENDA; 2.5.1.18; 248.
DR   NextBio; 697639; -.
DR   ArrayExpress; P46418; -.
DR   GermOnline; ENSRNOG00000029711; 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   Cytoplasm; Direct protein sequencing; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    221       Glutathione S-transferase alpha-5.
FT                                /FTId=PRO_0000185796.
FT   DOMAIN        3     83       GST N-terminal.
FT   DOMAIN       85    207       GST C-terminal.
SQ   SEQUENCE   221 AA;  25347 MW;  EEDE9873765BFDB5 CRC64;
     MPGKPVLHYF DGRGRMEPIR WLLAAAGVEF EENFLKTRDD LARLRSDGSL MFEQVPMVEI
     DGMKLVQTKA ILNYIATKYN LYGKDMKERA LIDMYAEGVA DLELMVLYYP YMPPGEKEAS
     LAKIKDKARN RYFPAYEKVL KSHGQDYLVG NKLSRADVSL VELLYHVEEM DPGIVDNFPL
     LKALRTRVSN LPTVKKFLQP GSQRKPFDDE KCVESAKKIF S
//