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Glutathione S-transferase alpha-5 (EC 2.5.1.18) (GST A5-5) (Glutathione S-transferase Yc-2) (GST Yc2)

 GSTA5_RAT               Reviewed;         221 AA.
P46418; Q6LD91;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 135.
RecName: Full=Glutathione S-transferase alpha-5;
EC=2.5.1.18;
AltName: Full=GST A5-5;
AltName: Full=Glutathione S-transferase Yc-2;
Short=GST Yc2;
Name=Gsta5; Synonyms=Gstyc2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Fischer 344; TISSUE=Liver;
PubMed=8051171;
Hayes J.D., Nguyen T., Judah D.J., Petersson D.G., Neal G.E.;
"Cloning of cDNAs from fetal rat liver encoding glutathione S-
transferase Yc polypeptides. The Yc2 subunit is expressed in adult rat
liver resistant to the hepatocarcinogen aflatoxin B1.";
J. Biol. Chem. 269:20707-20717(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8761455; DOI=10.1042/bj3180075;
Pulford D.J., Hayes J.D.;
"Characterization of the rat glutathione S-transferase Yc2 subunit
gene, GSTA5: identification of a putative antioxidant-responsive
element in the 5'-flanking region of rat GSTA5 that may mediate
chemoprotection against aflatoxin B1.";
Biochem. J. 318:75-84(1996).
[3]
PARTIAL PROTEIN SEQUENCE.
STRAIN=Fischer 344; TISSUE=Liver;
PubMed=1953636; DOI=10.1042/bj2790385;
Hayes J.D., Judah D.J., McLellan L.I., Kerr L.A., Peacock S.D.,
Neal G.E.;
"Ethoxyquin-induced resistance to aflatoxin B1 in the rat is
associated with the expression of a novel alpha-class glutathione S-
transferase subunit, Yc2, which possesses high catalytic activity for
aflatoxin B1-8,9-epoxide.";
Biochem. J. 279:385-398(1991).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles. Has
substantial activity toward aflatoxin B1-8,9-epoxide.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBUNIT: Heterodimer of YC1 and YC2.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Liver, nasal mucosa and epididymis.
-!- DEVELOPMENTAL STAGE: Liver from adult female rats contains about
10-fold greater levels of YC2 than is found in liver from adult
male rats.
-!- INDUCTION: By ethoxyquin, oltipraz, butylated hydroxyanisole, and
phenobarbitol.
-!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
{ECO:0000305}.
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EMBL; X78847; CAA55404.1; -; mRNA.
EMBL; S72506; AAP21065.1; -; mRNA.
EMBL; S82820; AAB46796.1; -; mRNA.
PIR; A54858; A54858.
RefSeq; NP_001009920.1; NM_001009920.2.
RefSeq; NP_001153211.1; NM_001159739.2.
UniGene; Rn.120929; -.
ProteinModelPortal; P46418; -.
SMR; P46418; -.
STRING; 10116.ENSRNOP00000042770; -.
iPTMnet; P46418; -.
PhosphoSitePlus; P46418; -.
PaxDb; P46418; -.
PRIDE; P46418; -.
GeneID; 494500; -.
KEGG; rno:494500; -.
UCSC; RGD:2753; rat.
CTD; 2940; -.
RGD; 2753; Gsta5.
eggNOG; KOG1695; Eukaryota.
eggNOG; ENOG4111VAU; LUCA.
HOGENOM; HOG000115734; -.
HOVERGEN; HBG053749; -.
KO; K00799; -.
PhylomeDB; P46418; -.
TreeFam; TF105321; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005640; C:nuclear outer membrane; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0043295; F:glutathione binding; IDA:RGD.
GO; GO:0004364; F:glutathione transferase activity; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0042493; P:response to drug; NAS:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0042178; P:xenobiotic catabolic process; IDA:RGD.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR003080; GST_alpha.
InterPro; IPR004046; GST_C.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01266; GSTRNSFRASEA.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing;
Reference proteome; Transferase.
CHAIN 1 221 Glutathione S-transferase alpha-5.
/FTId=PRO_0000185796.
DOMAIN 3 83 GST N-terminal.
DOMAIN 85 207 GST C-terminal.
REGION 54 55 Glutathione binding.
{ECO:0000250|UniProtKB:P30711}.
REGION 67 68 Glutathione binding.
{ECO:0000250|UniProtKB:P13745}.
BINDING 9 9 Glutathione.
{ECO:0000250|UniProtKB:P13745}.
BINDING 45 45 Glutathione.
{ECO:0000250|UniProtKB:P08263}.
MOD_RES 4 4 N6-succinyllysine.
{ECO:0000250|UniProtKB:P30115}.
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


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