GSTA3_RAT
ID GSTA3_RAT Reviewed; 221 AA.
AC P04904; Q6LD92;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Glutathione S-transferase alpha-3 {ECO:0000305};
DE EC=2.5.1.18;
DE AltName: Full=GST 2-2;
DE AltName: Full=GST A3-3;
DE AltName: Full=GST AA;
DE AltName: Full=Glutathione S-transferase Yc-1;
DE Short=GST Yc1;
GN Name=Gsta3 {ECO:0000312|RGD:1591980}; Synonyms=Gstyc1;
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=2985614; DOI=10.1016/s0021-9258(18)89095-0;
RA Telakowski-Hopkins C.A., Rodkey K.A., Bennett C.D., Lu A.Y.H.,
RA Pickett C.B.;
RT "Rat liver glutathione S-transferases. Construction of a cDNA clone
RT complementary to a Yc mRNA and prediction of the complete amino acid
RT sequence of a Yc subunit.";
RL J. Biol. Chem. 260:5820-5825(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer; TISSUE=Liver;
RX PubMed=10215608; DOI=10.1042/bj3390685;
RA Fotouhi-Ardakani N., Batist G.;
RT "Genomic cloning and characterization of the rat glutathione S-transferase-
RT A3-subunit gene.";
RL Biochem. J. 339:685-693(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Pituitary;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-13; 21-36; 70-78; 142-152; 156-182; 188-195 AND
RP 197-204, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-221.
RX PubMed=6204982; DOI=10.1016/s0021-9258(17)42719-0;
RA Tu C.-P.D., Lai H.-C.J., Li N.-Q., Weiss M.J., Reddy C.C.;
RT "The Yc and Ya subunits of rat liver glutathione S-transferases are the
RT products of separate genes.";
RL J. Biol. Chem. 259:9434-9439(1984).
RN [7]
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).
RN [8]
RP PROTEIN SEQUENCE OF 2-31.
RX PubMed=2186703; DOI=10.1016/0003-9861(90)90470-j;
RA Huskey S.E., Wang R.W., Linemeyer D.L., Pickett C.B., Lu A.Y.H.;
RT "Expression in Escherichia coli of rat liver cytosolic glutathione S-
RT transferase Yc cDNA.";
RL Arch. Biochem. Biophys. 279:116-121(1990).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Catalyzes
CC isomerization reactions that contribute to the biosynthesis of steroid
CC hormones. Efficiently catalyze obligatory double-bond isomerizations of
CC delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,20-dione,
CC precursors to testosterone and progesterone, respectively (By
CC similarity). Has substantial activity toward aflatoxin B1-8,9-epoxide
CC (By similarity). {ECO:0000250|UniProtKB:P30115,
CC ECO:0000250|UniProtKB:Q16772}.
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 Evidence={ECO:0000250|UniProtKB:Q16772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000250|UniProtKB:Q16772};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione;
CC Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865;
CC Evidence={ECO:0000250|UniProtKB:Q16772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937;
CC Evidence={ECO:0000250|UniProtKB:Q16772};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pregn-5-ene-3,20-dione = progesterone; Xref=Rhea:RHEA:43928,
CC ChEBI:CHEBI:17026, ChEBI:CHEBI:63837;
CC Evidence={ECO:0000250|UniProtKB:Q16772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43929;
CC Evidence={ECO:0000250|UniProtKB:Q16772};
CC -!- SUBUNIT: Heterodimer of YC1 and YC2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Liver from adult female rats contains about 2-fold
CC greater levels of YC1 than is found in liver from adult male rats.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X78848; CAA55405.1; -; mRNA.
DR EMBL; S72505; AAP21064.1; -; mRNA.
DR EMBL; K01932; AAA41294.1; -; mRNA.
DR EMBL; AF111160; AAD28714.1; -; mRNA.
DR EMBL; BC059128; AAH59128.1; -; mRNA.
DR EMBL; BC088127; AAH88127.1; -; mRNA.
DR PIR; A26753; A26753.
DR RefSeq; NP_113697.1; NM_031509.2.
DR RefSeq; XP_017452251.1; XM_017596762.1.
DR AlphaFoldDB; P04904; -.
DR SMR; P04904; -.
DR STRING; 10116.ENSRNOP00000018325; -.
DR ChEMBL; CHEMBL4436; -.
DR iPTMnet; P04904; -.
DR PhosphoSitePlus; P04904; -.
DR SwissPalm; P04904; -.
DR World-2DPAGE; 0004:P04904; -.
DR PaxDb; P04904; -.
DR PRIDE; P04904; -.
DR Ensembl; ENSRNOT00000018325; ENSRNOP00000018325; ENSRNOG00000013484.
DR GeneID; 24421; -.
DR KEGG; rno:24421; -.
DR CTD; 2938; -.
DR RGD; 1591980; Gsta3.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000163367; -.
DR HOGENOM; CLU_039475_4_0_1; -.
DR OMA; QMPMVKI; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P04904; -.
DR TreeFam; TF105321; -.
DR BRENDA; 2.5.1.18; 5301.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000013484; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; P04904; baseline and differential.
DR Genevisible; P04904; RN.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0043295; F:glutathione binding; IDA:CAFA.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:CAFA.
DR GO; GO:0046223; P:aflatoxin catabolic process; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001657; P:ureteric bud development; ISO:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:CAFA.
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; IPR040079; Glutathione_S-Trfase.
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 SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
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; Lipid metabolism; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2186703, ECO:0000269|Ref.5"
FT CHAIN 2..221
FT /note="Glutathione S-transferase alpha-3"
FT /id="PRO_0000185794"
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"
FT CONFLICT 102
FT /note="L -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="L -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 25319 MW; C45C5AF03573707F CRC64;
MPGKPVLHYF DGRGRMEPIR WLLAAAGVEF EEQFLKTRDD LARLRNDGSL MFQQVPMVEI
DGMKLVQTRA ILNYIATKYN LYGKDMKERA LIDMYAEGVA DLDEIVLHYP YIPPGEKEAS
LAKIKDKARN RYFPAFEKVL KSHGQDYLVG NRLSRADVYL VQVLYHVEEL DPSALANFPL
LKALRTRVSN LPTVKKFLQP GSQRKPLEDE KCVESAVKIF S
