GSTA5_RAT
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 03-AUG-2022, entry version 149.
DE RecName: Full=Glutathione S-transferase alpha-5;
DE EC=2.5.1.18;
DE AltName: Full=GST A5-5;
DE AltName: Full=Glutathione S-transferase Yc-2;
DE Short=GST Yc2;
GN Name=Gsta5; Synonyms=Gstyc2;
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=Fischer 344; TISSUE=Liver;
RX PubMed=8051171; DOI=10.1016/s0021-9258(17)32050-1;
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-transferase
RT Yc polypeptides. The Yc2 subunit is expressed in adult rat liver resistant
RT to the hepatocarcinogen aflatoxin B1.";
RL J. Biol. Chem. 269:20707-20717(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8761455; DOI=10.1042/bj3180075;
RA Pulford D.J., Hayes J.D.;
RT "Characterization of the rat glutathione S-transferase Yc2 subunit gene,
RT GSTA5: identification of a putative antioxidant-responsive element in the
RT 5'-flanking region of rat GSTA5 that may mediate chemoprotection against
RT aflatoxin B1.";
RL Biochem. J. 318:75-84(1996).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Fischer 344; TISSUE=Liver;
RX PubMed=1953636; DOI=10.1042/bj2790385;
RA Hayes J.D., Judah D.J., McLellan L.I., Kerr L.A., Peacock S.D., Neal G.E.;
RT "Ethoxyquin-induced resistance to aflatoxin B1 in the rat is associated
RT with the expression of a novel alpha-class glutathione S-transferase
RT subunit, Yc2, which possesses high catalytic activity for aflatoxin B1-8,9-
RT 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 substantial
CC activity toward aflatoxin B1-8,9-epoxide.
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 -!- 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 10-
CC fold greater levels of YC2 than is found in liver from adult male rats.
CC -!- INDUCTION: By ethoxyquin, oltipraz, butylated hydroxyanisole, and
CC phenobarbitol.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
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DR EMBL; X78847; CAA55404.1; -; mRNA.
DR EMBL; S72506; AAP21065.1; -; mRNA.
DR EMBL; S82820; AAB46796.1; -; mRNA.
DR PIR; A54858; A54858.
DR RefSeq; NP_001009920.1; NM_001009920.2.
DR RefSeq; NP_001153211.1; NM_001159739.2.
DR AlphaFoldDB; P46418; -.
DR SMR; P46418; -.
DR STRING; 10116.ENSRNOP00000042770; -.
DR iPTMnet; P46418; -.
DR PhosphoSitePlus; P46418; -.
DR PaxDb; P46418; -.
DR PRIDE; P46418; -.
DR Ensembl; ENSRNOT00000088416; ENSRNOP00000074697; ENSRNOG00000056847.
DR GeneID; 494500; -.
DR KEGG; rno:494500; -.
DR UCSC; RGD:2753; rat.
DR CTD; 2940; -.
DR RGD; 1593189; Gsta5.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000163367; -.
DR PhylomeDB; P46418; -.
DR TreeFam; TF105321; -.
DR Proteomes; UP000002494; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; ISO:RGD.
DR GO; GO:0046223; P:aflatoxin catabolic process; IEA:Ensembl.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0035634; P:response to stilbenoid; ISO:RGD.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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 Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01266; GSTRNSFRASEA.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Reference proteome; Transferase.
FT CHAIN 1..221
FT /note="Glutathione S-transferase alpha-5"
FT /id="PRO_0000185796"
FT DOMAIN 3..83
FT /note="GST N-terminal"
FT DOMAIN 85..207
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:P08263"
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"
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
