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Glutathione S-transferase Mu 1 (EC 2.5.1.18) (GST 3-3) (GSTM1-1) (Glutathione S-transferase Yb-1) (GST Yb1)

 GSTM1_RAT               Reviewed;         218 AA.
P04905;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
10-MAY-2017, entry version 164.
RecName: Full=Glutathione S-transferase Mu 1;
EC=2.5.1.18;
AltName: Full=GST 3-3;
AltName: Full=GSTM1-1;
AltName: Full=Glutathione S-transferase Yb-1;
Short=GST Yb1;
Name=Gstm1;
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].
PubMed=2875437; DOI=10.1093/nar/14.15.6101;
Lai H.-C.J., Grove G., Tu C.-P.D.;
"Cloning and sequence analysis of a cDNA for a rat liver glutathione
S-transferase Yb subunit.";
Nucleic Acids Res. 14:6101-6114(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3840477;
Ding G.J.-F., Lu A.Y.H., Pickett C.B.;
"Rat liver glutathione S-transferases. Nucleotide sequence analysis of
a Yb1 cDNA clone and prediction of the complete amino acid sequence of
the Yb1 subunit.";
J. Biol. Chem. 260:13268-13271(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-24, AND SUBUNIT.
PubMed=3011803;
Ding G.J.-F., Ding V.D.-H., Rodkey J.A., Bennett C.D., Lu A.Y.H.,
Pickett C.B.;
"Rat liver glutathione S-transferases. DNA sequence analysis of a Yb2
cDNA clone and regulation of the Yb1 and Yb2 mRNAs by phenobarbital.";
J. Biol. Chem. 261:7952-7957(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3040722;
Chang C., Saltzman A.G., Sorensen N.S., Hiipakka R.A., Liao S.;
"Identification of glutathione S-transferase Yb1 mRNA as the androgen-
repressed mRNA by cDNA cloning and sequence analysis.";
J. Biol. Chem. 262:11901-11903(1987).
[5]
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).
[6]
PROTEIN SEQUENCE OF 2-20; 83-96 AND 109-122.
PubMed=1416995; DOI=10.1016/0003-9861(92)90464-8;
Katusz R.M., Bono B., Colman R.F.;
"Identification of Tyr115 labeled by S-(4-bromo-2,3-
dioxobutyl)glutathione in the hydrophobic substrate binding site of
glutathione S-transferase, isoenzyme 3-3.";
Arch. Biochem. Biophys. 298:667-677(1992).
[7]
PROTEIN SEQUENCE OF 2-21 AND 212-218.
PubMed=2669745; DOI=10.1016/0006-291X(89)90793-6;
Hsieh J.C., Liu L.F., Chen W.L., Tam M.F.;
"Expression of Yb1 glutathione S-transferase using a baculovirus
expression system.";
Biochem. Biophys. Res. Commun. 162:1147-1154(1989).
[8]
PROTEIN SEQUENCE OF 2-26.
PubMed=2226415; DOI=10.1002/elps.1150110710;
Chang L.H., Hsieh J.C., Chen W.L., Tam M.F.;
"Identification of rat liver glutathione S-transferase Yb subunits by
partial N-terminal sequencing after electroblotting of proteins onto a
polyvinylidene difluoride membrane from an analytical isoelectric
focusing gel.";
Electrophoresis 11:589-593(1990).
[9]
PROTEIN SEQUENCE OF 2-24.
STRAIN=Wistar; TISSUE=Olfactory epithelium;
PubMed=8503873; DOI=10.1042/bj2920379;
Ben-Arie N., Khen M., Lancet D.;
"Glutathione S-transferases in rat olfactory epithelium: purification,
molecular properties and odorant biotransformation.";
Biochem. J. 292:379-384(1993).
[10]
PROTEIN SEQUENCE OF 2-20.
PubMed=3864155; DOI=10.1073/pnas.82.21.7202;
Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K.,
Warholm M., Joernvall H.;
"Identification of three classes of cytosolic glutathione transferase
common to several mammalian species: correlation between structural
data and enzymatic properties.";
Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985).
[11]
PROTEIN SEQUENCE OF 19-32; 33-50; 53-68; 70-78; 97-108; 137-144;
174-187 AND 203-218, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
Lubec G., Chen W.-Q., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[12]
MUTAGENESIS OF CYS-87.
PubMed=1883338; DOI=10.1042/bj2780293;
Hsieh J.-C., Huang S.-C., Chen W.-L., Lai Y.-C., Tam M.F.;
"Cysteine-86 is not needed for the enzymic activity of glutathione S-
transferase 3-3.";
Biochem. J. 278:293-297(1991).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-205 AND SER-210,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
PubMed=1420139; DOI=10.1021/bi00157a004;
Ji X., Zhang P., Armstrong R.N., Gilliland G.L.;
"The three-dimensional structure of a glutathione S-transferase from
the mu gene class. Structural analysis of the binary complex of
isoenzyme 3-3 and glutathione at 2.2-A resolution.";
Biochemistry 31:10169-10184(1992).
[15]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=15299462; DOI=10.1107/S0907444993009370;
Fu J.-H., Rose J., Tam M.F., Wang B.-C.;
"New crystal forms of a mu-class glutathione S-transferase from rat
liver.";
Acta Crystallogr. D 50:219-224(1994).
[16]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE
ANALOGS, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-116.
PubMed=8110735; DOI=10.1021/bi00171a002;
Ji X., Johnson W.W., Sesay M.A., Dickert L., Prasad S.M., Ammon H.L.,
Armstrong R.N., Gilliland G.L.;
"Structure and function of the xenobiotic substrate binding site of a
glutathione S-transferase as revealed by X-ray crystallographic
analysis of product complexes with the diastereomers of 9-(S-
glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene.";
Biochemistry 33:1043-1052(1994).
[17]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT PHE-7 IN COMPLEXES
WITH GLUTATHIONE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-7.
PubMed=8664265; DOI=10.1021/bi960189k;
Xiao G., Liu S., Ji X., Johnson W.W., Chen J., Parsons J.F.,
Stevens W.J., Gilliland G.L., Armstrong R.N.;
"First-sphere and second-sphere electrostatic effects in the active
site of a class mu gluthathione transferase.";
Biochemistry 35:4753-4765(1996).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles. The olfactory
GST may be crucial for the acuity of the olfactory process.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:8110735, ECO:0000269|PubMed:8664265}.
-!- SUBUNIT: Homodimer or heterodimer. {ECO:0000269|PubMed:1420139,
ECO:0000269|PubMed:3011803, ECO:0000269|PubMed:8110735}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MISCELLANEOUS: Yb subclass selectively binds steroid hormones.
-!- SIMILARITY: Belongs to the GST superfamily. Mu family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X04229; CAA27811.1; -; mRNA.
EMBL; M11719; AAA41287.1; -; mRNA.
EMBL; J02810; AAA41293.1; -; mRNA.
EMBL; BC063172; AAH63172.1; -; mRNA.
PIR; A29794; A29794.
RefSeq; NP_058710.1; NM_017014.1.
UniGene; Rn.202944; -.
PDB; 1GSB; X-ray; 2.50 A; A/B/C/D=2-218.
PDB; 1GSC; X-ray; 2.50 A; A/B/C/D=2-218.
PDB; 1MTC; X-ray; 2.20 A; A/B=2-218.
PDB; 2GST; X-ray; 1.80 A; A/B=2-218.
PDB; 3FYG; X-ray; 2.20 A; A/B=2-218.
PDB; 3GST; X-ray; 1.90 A; A/B=2-218.
PDB; 4GST; X-ray; 1.90 A; A/B=2-218.
PDB; 5FWG; X-ray; 2.00 A; A/B=2-218.
PDB; 5GST; X-ray; 2.00 A; A/B=2-218.
PDB; 6GST; X-ray; 2.20 A; A/B=2-218.
PDB; 6GSU; X-ray; 1.85 A; A/B=2-218.
PDB; 6GSV; X-ray; 1.75 A; A/B=2-218.
PDB; 6GSW; X-ray; 1.85 A; A/B=2-218.
PDB; 6GSX; X-ray; 1.91 A; A/B=2-218.
PDB; 6GSY; X-ray; 2.20 A; A/B=2-218.
PDBsum; 1GSB; -.
PDBsum; 1GSC; -.
PDBsum; 1MTC; -.
PDBsum; 2GST; -.
PDBsum; 3FYG; -.
PDBsum; 3GST; -.
PDBsum; 4GST; -.
PDBsum; 5FWG; -.
PDBsum; 5GST; -.
PDBsum; 6GST; -.
PDBsum; 6GSU; -.
PDBsum; 6GSV; -.
PDBsum; 6GSW; -.
PDBsum; 6GSX; -.
PDBsum; 6GSY; -.
ProteinModelPortal; P04905; -.
SMR; P04905; -.
BioGrid; 246588; 1.
MINT; MINT-4564586; -.
STRING; 10116.ENSRNOP00000039050; -.
ChEMBL; CHEMBL2209; -.
iPTMnet; P04905; -.
PhosphoSitePlus; P04905; -.
PaxDb; P04905; -.
PRIDE; P04905; -.
GeneID; 24423; -.
KEGG; rno:24423; -.
UCSC; RGD:2755; rat.
CTD; 2944; -.
RGD; 2755; Gstm1.
eggNOG; ENOG410IN5J; Eukaryota.
eggNOG; ENOG4110YU0; LUCA.
HOGENOM; HOG000115735; -.
HOVERGEN; HBG106842; -.
InParanoid; P04905; -.
KO; K00799; -.
PhylomeDB; P04905; -.
BRENDA; 2.5.1.18; 5301.
EvolutionaryTrace; P04905; -.
PRO; PR:P04905; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0005576; C:extracellular region; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0043295; F:glutathione binding; IDA:CAFA.
GO; GO:0004364; F:glutathione transferase activity; IDA:CAFA.
GO; GO:0016151; F:nickel cation binding; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0005496; F:steroid binding; IPI:RGD.
GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
GO; GO:0043200; P:response to amino acid; IEP:RGD.
GO; GO:0046677; P:response to antibiotic; IEP:RGD.
GO; GO:0048678; P:response to axon injury; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0010288; P:response to lead ion; IEP:RGD.
GO; GO:0010226; P:response to lithium ion; IEP:RGD.
GO; GO:0010038; P:response to metal ion; IEP:RGD.
GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
GO; GO:0042178; P:xenobiotic catabolic process; IDA:CAFA.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR003081; GST_mu.
InterPro; IPR012336; Thioredoxin-like_fold.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01267; GSTRNSFRASEM.
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; Complete proteome; Cytoplasm; Direct protein sequencing;
Olfaction; Phosphoprotein; Reference proteome; Sensory transduction;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1416995,
ECO:0000269|PubMed:2226415,
ECO:0000269|PubMed:2669745,
ECO:0000269|PubMed:3011803,
ECO:0000269|PubMed:3864155,
ECO:0000269|PubMed:8503873}.
CHAIN 2 218 Glutathione S-transferase Mu 1.
/FTId=PRO_0000185831.
DOMAIN 2 88 GST N-terminal.
DOMAIN 90 208 GST C-terminal.
REGION 7 8 Glutathione binding.
{ECO:0000269|PubMed:8664265,
ECO:0000305|PubMed:8110735}.
REGION 43 46 Glutathione binding.
{ECO:0000269|PubMed:8664265,
ECO:0000305|PubMed:8110735}.
REGION 59 60 Glutathione binding.
{ECO:0000269|PubMed:8664265,
ECO:0000305|PubMed:8110735}.
REGION 72 73 Glutathione binding.
{ECO:0000269|PubMed:8664265,
ECO:0000305|PubMed:8110735}.
BINDING 50 50 Glutathione. {ECO:0000269|PubMed:8664265,
ECO:0000305|PubMed:8110735}.
BINDING 116 116 Substrate. {ECO:0000250}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MUTAGEN 7 7 Y->F,L: Reduces catalytic activity about
100-fold. {ECO:0000269|PubMed:8664265}.
MUTAGEN 87 87 C->S: No change in activity.
{ECO:0000269|PubMed:1883338}.
MUTAGEN 116 116 Y->F: Reduces enzyme activity about 100-
fold. {ECO:0000269|PubMed:8110735}.
CONFLICT 199 200 KS -> NC (in Ref. 2; AAA41287).
{ECO:0000305}.
STRAND 3 10 {ECO:0000244|PDB:6GSV}.
TURN 12 14 {ECO:0000244|PDB:6GSV}.
HELIX 15 23 {ECO:0000244|PDB:6GSV}.
STRAND 28 33 {ECO:0000244|PDB:6GSV}.
TURN 38 41 {ECO:0000244|PDB:6GSV}.
HELIX 44 47 {ECO:0000244|PDB:6GSV}.
TURN 48 51 {ECO:0000244|PDB:6GSV}.
STRAND 60 65 {ECO:0000244|PDB:6GSV}.
STRAND 68 72 {ECO:0000244|PDB:6GSV}.
HELIX 73 83 {ECO:0000244|PDB:6GSV}.
HELIX 91 115 {ECO:0000244|PDB:6GSV}.
HELIX 120 142 {ECO:0000244|PDB:6GSV}.
STRAND 146 152 {ECO:0000244|PDB:6GSV}.
HELIX 155 170 {ECO:0000244|PDB:6GSV}.
TURN 172 175 {ECO:0000244|PDB:6GSV}.
HELIX 179 189 {ECO:0000244|PDB:6GSV}.
HELIX 192 198 {ECO:0000244|PDB:6GSV}.
STRAND 200 202 {ECO:0000244|PDB:6GSX}.
STRAND 213 216 {ECO:0000244|PDB:6GSV}.
SEQUENCE 218 AA; 25914 MW; 1A8E80D09A5CACA8 CRC64;
MPMILGYWNV RGLTHPIRLL LEYTDSSYEE KRYAMGDAPD YDRSQWLNEK FKLGLDFPNL
PYLIDGSRKI TQSNAIMRYL ARKHHLCGET EEERIRADIV ENQVMDNRMQ LIMLCYNPDF
EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYHIF EPKCLDAFPN
LKDFLARFEG LKKISAYMKS SRYLSTPIFS KLAQWSNK


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