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Glutathione S-transferase alpha-1 (EC 2.5.1.18) (13-hydroperoxyoctadecadienoate peroxidase) (EC 1.11.1.-) (Androst-5-ene-3,17-dione isomerase) (EC 5.3.3.-) (GST 1-1) (GST 1a-1a) (GST A1-1) (GST B) (Glutathione S-transferase Ya-1) (GST Ya1) (Ligandin)

 GSTA1_RAT               Reviewed;         222 AA.
P00502; Q6AZ72;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
26-FEB-2020, entry version 165.
RecName: Full=Glutathione S-transferase alpha-1 {ECO:0000305};
EC=2.5.1.18 {ECO:0000269|PubMed:11119643};
AltName: Full=13-hydroperoxyoctadecadienoate peroxidase {ECO:0000250|UniProtKB:P08263};
EC=1.11.1.- {ECO:0000250|UniProtKB:P08263};
AltName: Full=Androst-5-ene-3,17-dione isomerase {ECO:0000250|UniProtKB:P08263};
EC=5.3.3.- {ECO:0000250|UniProtKB:P08263};
AltName: Full=GST 1-1;
AltName: Full=GST 1a-1a;
AltName: Full=GST A1-1;
AltName: Full=GST B;
AltName: Full=Glutathione S-transferase Ya-1;
Short=GST Ya1;
AltName: Full=Ligandin;
Name=Gsta1;
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=Sprague-Dawley; TISSUE=Liver;
PubMed=6201485;
Lai H.-C.J., Li N.-Q., Weiss M.J., Reddy C.C., Tu C.-P.D.;
"The nucleotide sequence of a rat liver glutathione S-transferase subunit
cDNA clone.";
J. Biol. Chem. 259:5536-5542(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 46-197.
PubMed=6273441;
Kalinyak J.E., Taylor J.M.;
"Rat glutathione S-transferase. Cloning of double-stranded cDNA and
induction of its mRNA.";
J. Biol. Chem. 257:523-530(1982).
[4]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=11119643;
DOI=10.1002/1097-0134(20010201)42:2<192::aid-prot60>3.0.co;2-#;
Adman E.T., Le Trong I., Stenkamp R.E., Nieslanik B.S., Dietze E.C.,
Tai G., Ibarra C., Atkins W.M.;
"Localization of the C-terminus of rat glutathione S-transferase A1-1:
crystal structure of mutants W21F and W21F/F220Y.";
Proteins 42:192-200(2001).
-!- FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic
attack of the sulfur atom of glutathione on the electrophilic groups of
a wide range of exogenous and endogenous compounds (Probable). Involved
in the formation of glutathione conjugates of both prostaglandin A2
(PGA2) and prostaglandin J2 (PGJ2). It also catalyzes the isomerization
of D5-androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may
therefore play an important role in hormone biosynthesis. Through its
glutathione-dependent peroxidase activity toward the fatty acid
hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it
is also involved in the metabolism of oxidized linoleic acid (By
similarity). {ECO:0000250|UniProtKB:P08263,
ECO:0000305|PubMed:11119643}.
-!- CATALYTIC ACTIVITY:
Reaction=glutathione + RX = a halide anion + an S-substituted
glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
ChEBI:CHEBI:90779; EC=2.5.1.18;
Evidence={ECO:0000269|PubMed:11119643};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
Evidence={ECO:0000305|PubMed:11119643};
-!- CATALYTIC ACTIVITY:
Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-
glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925,
ChEBI:CHEBI:133370, ChEBI:CHEBI:133768;
Evidence={ECO:0000250|UniProtKB:P08263};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797;
Evidence={ECO:0000250|UniProtKB:P08263};
-!- CATALYTIC ACTIVITY:
Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-
glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925,
ChEBI:CHEBI:133396, ChEBI:CHEBI:133771;
Evidence={ECO:0000250|UniProtKB:P08263};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
Evidence={ECO:0000250|UniProtKB:P08263};
-!- CATALYTIC ACTIVITY:
Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione =
(13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide +
H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466,
ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850;
Evidence={ECO:0000250|UniProtKB:P08263};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889;
Evidence={ECO:0000250|UniProtKB:P08263};
-!- CATALYTIC ACTIVITY:
Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione;
Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865;
Evidence={ECO:0000250|UniProtKB:P08263};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937;
Evidence={ECO:0000250|UniProtKB:P08263};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11119643}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MISCELLANEOUS: In addition to its enzymatic activity, the homodimer of
Ya chains, called ligandin, binds various organic anions, xenobiotics,
and azocarcinogen dyes.
-!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
{ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; K01931; AAA41283.1; -; mRNA.
EMBL; BC078706; AAH78706.1; -; mRNA.
PIR; A24735; A24735.
PIR; A92479; XURTG.
RefSeq; NP_058709.2; NM_017013.4.
PDB; 1EV4; X-ray; 2.20 A; A/C/D=2-222.
PDB; 1EV9; X-ray; 2.20 A; A/C/D=2-222.
PDBsum; 1EV4; -.
PDBsum; 1EV9; -.
SMR; P00502; -.
ChEMBL; CHEMBL2390; -.
iPTMnet; P00502; -.
PhosphoSitePlus; P00502; -.
PRIDE; P00502; -.
GeneID; 24422; -.
KEGG; rno:24422; -.
CTD; 2939; -.
RGD; 2753; Gsta1.
eggNOG; KOG1695; Eukaryota.
eggNOG; ENOG4111VAU; LUCA.
InParanoid; P00502; -.
KO; K00799; -.
OrthoDB; 1162336at2759; -.
PhylomeDB; P00502; -.
TreeFam; TF105321; -.
EvolutionaryTrace; P00502; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:CAFA.
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:CAFA.
GO; GO:0004602; F:glutathione peroxidase activity; ISO:RGD.
GO; GO:0004364; F:glutathione transferase activity; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0004769; F:steroid delta-isomerase activity; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
GO; GO:0006749; P:glutathione metabolic process; ISO:RGD.
GO; GO:0043651; P:linoleic acid metabolic process; ISO:RGD.
GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
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:CAFA.
GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
Gene3D; 3.40.30.10; -; 1.
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; PF14497; GST_C_3; 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;
3D-structure; Acetylation; Cytoplasm; Isomerase; Oxidoreductase;
Peroxidase; Reference proteome; Transferase.
CHAIN 1..222
/note="Glutathione S-transferase alpha-1"
/id="PRO_0000185792"
DOMAIN 3..83
/note="GST N-terminal"
DOMAIN 85..208
/note="GST C-terminal"
REGION 54..55
/note="Glutathione binding"
/evidence="ECO:0000269|PubMed:11119643"
REGION 67..68
/note="Glutathione binding"
/evidence="ECO:0000269|PubMed:11119643"
BINDING 9
/note="Glutathione"
/evidence="ECO:0000269|PubMed:11119643"
BINDING 45
/note="Glutathione"
/evidence="ECO:0000269|PubMed:11119643"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000250|UniProtKB:P80894"
MOD_RES 4
/note="N6-succinyllysine"
/evidence="ECO:0000250|UniProtKB:P30115"
CONFLICT 152
/note="R -> K (in Ref. 1 and 3)"
/evidence="ECO:0000305"
CONFLICT 208
/note="V -> M (in Ref. 1; AAA41283)"
/evidence="ECO:0000305"
STRAND 6..12
/evidence="ECO:0000244|PDB:1EV4"
HELIX 16..25
/evidence="ECO:0000244|PDB:1EV4"
STRAND 31..35
/evidence="ECO:0000244|PDB:1EV4"
HELIX 38..46
/evidence="ECO:0000244|PDB:1EV4"
STRAND 57..60
/evidence="ECO:0000244|PDB:1EV4"
STRAND 63..67
/evidence="ECO:0000244|PDB:1EV4"
HELIX 68..79
/evidence="ECO:0000244|PDB:1EV4"
HELIX 86..109
/evidence="ECO:0000244|PDB:1EV4"
HELIX 114..116
/evidence="ECO:0000244|PDB:1EV4"
HELIX 117..130
/evidence="ECO:0000244|PDB:1EV4"
HELIX 132..143
/evidence="ECO:0000244|PDB:1EV4"
STRAND 146..149
/evidence="ECO:0000244|PDB:1EV4"
HELIX 155..171
/evidence="ECO:0000244|PDB:1EV4"
HELIX 172..175
/evidence="ECO:0000244|PDB:1EV4"
HELIX 179..190
/evidence="ECO:0000244|PDB:1EV4"
HELIX 192..198
/evidence="ECO:0000244|PDB:1EV4"
HELIX 211..219
/evidence="ECO:0000244|PDB:1EV4"
SEQUENCE 222 AA; 25607 MW; AE43A1BEBE8549CF CRC64;
MSGKPVLHYF NARGRMECIR WLLAAAGVEF DEKFIQSPED LEKLKKDGNL MFDQVPMVEI
DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYTEGIL DLTEMIMQLV ICPPDQKEAK
TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LELLLYVEEF DASLLTSFPL
LKAFKSRISS LPNVKKFLQP GSQRKLPVDA KQIEEARKIF KF


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