ID   GSTA2_CHICK             Reviewed;         222 AA.
AC   Q08393;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
DE   AltName: Full=Class-alpha;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Tam M.F., Liu L.-F.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 30-222.
RC   TISSUE=Liver;
RX   MEDLINE=94060114; PubMed=8241281; DOI=10.1016/0167-4781(93)90168-D;
RA   Liu L.-F., Wu S.-H., Tam M.F.;
RT   "Nucleotide sequence of class-alpha glutathione S-transferases from
RT   chicken liver.";
RL   Biochim. Biophys. Acta 1216:332-334(1993).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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; L15387; AAA16573.2; -; mRNA.
DR   IPI; IPI00587274; -.
DR   PIR; S43432; S43432.
DR   RefSeq; NP_001001776.1; -.
DR   UniGene; Gga.39241; -.
DR   HSSP; P08263; 1K3O.
DR   SMR; Q08393; 3-220.
DR   Ensembl; ENSGALG00000016328; Gallus gallus.
DR   GeneID; 414895; -.
DR   KEGG; gga:414895; -.
DR   HOGENOM; Q08393; -.
DR   HOVERGEN; Q08393; -.
DR   OMA; Q08393; DMYADGT.
DR   BRENDA; 2.5.1.18; 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Transferase.
FT   CHAIN         1    222       Glutathione S-transferase.
FT                                /FTId=PRO_0000185802.
FT   DOMAIN        3     83       GST N-terminal.
FT   DOMAIN       85    208       GST C-terminal.
SQ   SEQUENCE   222 AA;  25414 MW;  7B25B823051C9B8A CRC64;
     MAGKPKLHYT RGRGKMESIR WLLAAAGVEF EEEFIEKKED LEKLRNDGSL LFQQVPMVEI
     DGMKMVQSRA ILCYIAGKYN LYGKDLKERA WIDMYVEGTT DLMGMIMALP FQAADVKEKN
     IALITERATT RYFPVYEKAL KDHGQDYLVG NKLSWADIHL LEAILMTEEL KSDILSAFPL
     LQAFKGRMSN VPTIKKFLQP GSQRKPPLDE KSIANVRKIF SF
//