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Microsomal glutathione S-transferase 1 (Microsomal GST-1) (EC 2.5.1.18) (Microsomal GST-I)

 MGST1_RAT               Reviewed;         155 AA.
P08011;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-JUL-2017, entry version 134.
RecName: Full=Microsomal glutathione S-transferase 1;
Short=Microsomal GST-1;
EC=2.5.1.18;
AltName: Full=Microsomal GST-I;
Name=Mgst1; Synonyms=Gst12;
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=3372534;
Dejong J.L., Morgenstern R., Joernvall H., Depierre J.W., Tu C.-P.D.;
"Gene expression of rat and human microsomal glutathione S-
transferases.";
J. Biol. Chem. 263:8430-8436(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
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]
PROTEIN SEQUENCE OF 2-155.
PubMed=3932348;
Morgenstern R., Depierre J.W., Joernvall H.;
"Microsomal glutathione transferase. Primary structure.";
J. Biol. Chem. 260:13976-13983(1985).
[4]
SUBCELLULAR LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=6439207; DOI=10.1016/0006-2952(84)90145-X;
Morgenstern R., Lundqvist G., Andersson G., Balk L., Depierre J.W.;
"The distribution of microsomal glutathione transferase among
different organelles, different organs, and different organisms.";
Biochem. Pharmacol. 33:3609-3614(1984).
[5]
ROLE OF CYS-50 IN ENZYME REGULATION.
PubMed=11106493; DOI=10.1021/bi001764u;
Svensson R., Rinaldi R., Swedmark S., Morgenstern R.;
"Reactivity of cysteine-49 and its influence on the activation of
microsomal glutathione transferase 1: evidence for subunit
interaction.";
Biochemistry 39:15144-15149(2000).
[6]
NITRATION AT TYR-93, AND ENZYME REGULATION.
PubMed=16314419; DOI=10.1074/jbc.M509480200;
Ji Y., Neverova I., Van Eyk J.E., Bennett B.M.;
"Nitration of tyrosine 92 mediates the activation of rat microsomal
glutathione s-transferase by peroxynitrite.";
J. Biol. Chem. 281:1986-1991(2006).
[7]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 2-154 IN COMPLEX WITH
GLUTATHIONE, SUBUNIT, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY,
MUTAGENESIS OF HIS-76 AND GLU-81, AND GLUTATHIONE BINDING SITES.
PubMed=16806268; DOI=10.1016/j.jmb.2006.05.056;
Holm P.J., Bhakat P., Jegerschold C., Gyobu N., Mitsuoka K.,
Fujiyoshi Y., Morgenstern R., Hebert H.;
"Structural basis for detoxification and oxidative stress protection
in membranes.";
J. Mol. Biol. 360:934-945(2006).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- ENZYME REGULATION: Can be activated by reagents that attack Cys-50
sulfhydryl, such as N-ethylmaleimide, except in the testis.
Activation also occurs via nitration of Tyr-93 by peroxynitrite.
{ECO:0000269|PubMed:16314419}.
-!- SUBUNIT: Homotrimer; The trimer binds only one molecule of
glutathione. {ECO:0000269|PubMed:16806268}.
-!- SUBCELLULAR LOCATION: Microsome. Mitochondrion outer membrane;
Peripheral membrane protein. Endoplasmic reticulum membrane;
Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Highest in the liver, followed by kidney and
testis and much lower in seminal vesicles, spleen, lung and brain.
-!- PTM: Peroxynitrite induces nitration at Tyr-93 which activates the
enzyme. {ECO:0000269|PubMed:16314419}.
-!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J03752; AAA41281.1; -; mRNA.
EMBL; BC063150; AAH63150.1; -; mRNA.
PIR; A28083; A28083.
RefSeq; NP_599176.1; NM_134349.3.
UniGene; Rn.2580; -.
PDB; 2H8A; EM; 3.20 A; A=2-155.
PDBsum; 2H8A; -.
ProteinModelPortal; P08011; -.
SMR; P08011; -.
MINT; MINT-4575717; -.
STRING; 10116.ENSRNOP00000010579; -.
iPTMnet; P08011; -.
PhosphoSitePlus; P08011; -.
PaxDb; P08011; -.
PRIDE; P08011; -.
Ensembl; ENSRNOT00000010579; ENSRNOP00000010579; ENSRNOG00000007743.
GeneID; 171341; -.
KEGG; rno:171341; -.
UCSC; RGD:70927; rat.
CTD; 4257; -.
RGD; 70927; Mgst1.
eggNOG; ENOG410IXE1; Eukaryota.
eggNOG; ENOG4111VJG; LUCA.
GeneTree; ENSGT00390000011980; -.
HOGENOM; HOG000231759; -.
HOVERGEN; HBG052470; -.
InParanoid; P08011; -.
KO; K00799; -.
OMA; FYRMTRK; -.
OrthoDB; EOG091G14I4; -.
PhylomeDB; P08011; -.
TreeFam; TF105327; -.
BRENDA; 2.5.1.18; 5301.
Reactome; R-RNO-156590; Glutathione conjugation.
Reactome; R-RNO-5423646; Aflatoxin activation and detoxification.
Reactome; R-RNO-6798695; Neutrophil degranulation.
SABIO-RK; P08011; -.
EvolutionaryTrace; P08011; -.
PRO; PR:P08011; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000007743; -.
ExpressionAtlas; P08011; baseline and differential.
Genevisible; P08011; RN.
GO; GO:0045177; C:apical part of cell; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005778; C:peroxisomal membrane; IDA:RGD.
GO; GO:0043295; F:glutathione binding; IDA:UniProtKB.
GO; GO:0004602; F:glutathione peroxidase activity; IEA:Ensembl.
GO; GO:0004364; F:glutathione transferase activity; IDA:RGD.
GO; GO:0042802; F:identical protein binding; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0071449; P:cellular response to lipid hydroperoxide; IEA:Ensembl.
GO; GO:0033327; P:Leydig cell differentiation; IEP:RGD.
GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IDA:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IDA:RGD.
Gene3D; 1.20.120.550; -; 1.
InterPro; IPR023352; MAPEG-like_dom.
InterPro; IPR001129; Membr-assoc_MAPEG.
Pfam; PF01124; MAPEG; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; Membrane; Microsome;
Mitochondrion; Mitochondrion outer membrane; Nitration;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3932348}.
CHAIN 2 155 Microsomal glutathione S-transferase 1.
/FTId=PRO_0000217739.
TOPO_DOM 3 9 Lumenal.
TRANSMEM 10 33 Helical.
TOPO_DOM 34 62 Cytoplasmic.
TRANSMEM 63 96 Helical.
TOPO_DOM 97 99 Lumenal.
TRANSMEM 100 123 Helical.
TOPO_DOM 124 128 Cytoplasmic.
TRANSMEM 129 148 Helical.
TOPO_DOM 149 155 Lumenal.
BINDING 38 38 Glutathione.
{ECO:0000269|PubMed:16806268}.
BINDING 73 73 Glutathione.
{ECO:0000269|PubMed:16806268}.
BINDING 74 74 Glutathione.
{ECO:0000269|PubMed:16806268}.
BINDING 76 76 Glutathione.
{ECO:0000269|PubMed:16806268}.
BINDING 81 81 Glutathione.
{ECO:0000269|PubMed:16806268}.
BINDING 121 121 Glutathione.
{ECO:0000269|PubMed:16806268}.
SITE 50 50 Activates the enzyme when modified.
MOD_RES 42 42 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VS7}.
MOD_RES 55 55 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VS7}.
MOD_RES 60 60 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91VS7}.
MOD_RES 93 93 Nitrated tyrosine.
{ECO:0000269|PubMed:16314419}.
MUTAGEN 76 76 H->Q: Decreased enzyme activity.
{ECO:0000269|PubMed:16806268}.
MUTAGEN 81 81 E->Q: Loss of enzyme activity.
{ECO:0000269|PubMed:16806268}.
CONFLICT 27 27 M -> V (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 55 55 K -> G (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 68 68 K -> T (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 97 97 G -> A (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 101 101 S -> P (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 134 134 F -> K (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 141 141 T -> D (in Ref. 3; AA sequence).
{ECO:0000305}.
HELIX 11 24 {ECO:0000244|PDB:2H8A}.
HELIX 27 30 {ECO:0000244|PDB:2H8A}.
HELIX 31 33 {ECO:0000244|PDB:2H8A}.
HELIX 64 81 {ECO:0000244|PDB:2H8A}.
HELIX 84 92 {ECO:0000244|PDB:2H8A}.
TURN 93 95 {ECO:0000244|PDB:2H8A}.
HELIX 103 122 {ECO:0000244|PDB:2H8A}.
HELIX 127 137 {ECO:0000244|PDB:2H8A}.
HELIX 139 146 {ECO:0000244|PDB:2H8A}.
SEQUENCE 155 AA; 17472 MW; 8FB62EEDF5A74489 CRC64;
MADLKQLMDN EVLMAFTSYA TIILAKMMFL SSATAFQRLT NKVFANPEDC AGFGKGENAK
KFLRTDEKVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDL STALIHFRIF VGARIYHTIA
YLTPLPQPNR GLAFFVGYGV TLSMAYRLLR SRLYL


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