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Glutathione S-transferase Mu 2 (EC 2.5.1.18) (GST 4-4) (GSTM2-2) (Glutathione S-transferase Yb-2) (GST Yb2)

 GSTM2_RAT               Reviewed;         218 AA.
P08010;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 167.
RecName: Full=Glutathione S-transferase Mu 2;
EC=2.5.1.18;
AltName: Full=GST 4-4;
AltName: Full=GSTM2-2;
AltName: Full=Glutathione S-transferase Yb-2;
Short=GST Yb2;
Name=Gstm2;
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 [GENOMIC DNA].
PubMed=3403534;
Lai H.-C.J., Qian B., Grove G., Tu C.-P.D.;
"Gene expression of rat glutathione S-transferases. Evidence for gene
conversion in the evolution of the Yb multigene family.";
J. Biol. Chem. 263:11389-11395(1988).
[2]
PROTEIN SEQUENCE OF 2-218.
STRAIN=Sprague-Dawley;
PubMed=3699019; DOI=10.1111/j.1432-1033.1986.tb09588.x;
Alin P., Mannervik B., Joernvall H.;
"Cytosolic rat liver glutathione transferase 4-4. Primary structure of
the protein reveals extensive differences between homologous
glutathione transferases of classes alpha and mu.";
Eur. J. Biochem. 156:343-350(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-218.
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] OF 33-218.
PubMed=3020050;
Lai H.-C.J., Tu C.-P.D.;
"Rat glutathione S-transferases supergene family. Characterization of
an anionic Yb subunit cDNA clone.";
J. Biol. Chem. 261:13793-13799(1986).
[5]
PROTEIN SEQUENCE OF 2-26.
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).
[6]
PROTEIN SEQUENCE OF 2-28.
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).
[7]
PROTEIN SEQUENCE OF 2-22.
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).
[8]
PROTEIN SEQUENCE OF 33-43; 137-144; 153-168 AND 174-182, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
Lubec G., Afjehi-Sadat L., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-44, 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).
[10]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE
ANALOG.
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.
-!- SUBUNIT: Homodimer or heterodimer. {ECO:0000269|PubMed:8664265}.
-!- 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; J02592; AAA41285.1; -; mRNA.
EMBL; M13590; AAA42351.1; -; mRNA.
EMBL; J03914; AAA41296.1; -; Genomic_DNA.
PIR; A29231; XURTG4.
RefSeq; NP_803175.1; NM_177426.1.
UniGene; Rn.625; -.
PDB; 1B4P; X-ray; 1.70 A; A=2-218.
PDBsum; 1B4P; -.
ProteinModelPortal; P08010; -.
SMR; P08010; -.
IntAct; P08010; 1.
STRING; 10116.ENSRNOP00000025939; -.
ChEMBL; CHEMBL2504; -.
iPTMnet; P08010; -.
PhosphoSitePlus; P08010; -.
PaxDb; P08010; -.
PRIDE; P08010; -.
Ensembl; ENSRNOT00000025939; ENSRNOP00000025939; ENSRNOG00000018937.
GeneID; 24424; -.
KEGG; rno:24424; -.
UCSC; RGD:2756; rat.
CTD; 2946; -.
RGD; 2756; Gstm2.
eggNOG; ENOG410IN5J; Eukaryota.
eggNOG; ENOG4110YU0; LUCA.
GeneTree; ENSGT00550000074559; -.
HOGENOM; HOG000115735; -.
HOVERGEN; HBG106842; -.
InParanoid; P08010; -.
KO; K00799; -.
OMA; YWDIRGR; -.
OrthoDB; EOG091G0K2E; -.
PhylomeDB; P08010; -.
TreeFam; TF353040; -.
Reactome; R-RNO-156590; Glutathione conjugation.
EvolutionaryTrace; P08010; -.
PRO; PR:P08010; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000018937; -.
ExpressionAtlas; P08010; baseline and differential.
Genevisible; P08010; RN.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0043295; F:glutathione binding; IDA:CAFA.
GO; GO:0004364; F:glutathione transferase activity; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:1902168; P:response to catechin; IEP:RGD.
GO; GO:0033595; P:response to genistein; IEP:RGD.
GO; GO:0010038; P:response to metal ion; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
GO; GO:0042178; P:xenobiotic catabolic process; IDA:CAFA.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:RGD.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR003081; GST_mu.
InterPro; IPR036249; Thioredoxin-like_sf.
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:2226415,
ECO:0000269|PubMed:3699019,
ECO:0000269|PubMed:3864155,
ECO:0000269|PubMed:8503873}.
CHAIN 2 218 Glutathione S-transferase Mu 2.
/FTId=PRO_0000185832.
DOMAIN 2 88 GST N-terminal.
DOMAIN 90 214 GST C-terminal.
REGION 7 8 Glutathione binding.
{ECO:0000305|PubMed:8664265}.
REGION 43 46 Glutathione binding.
{ECO:0000305|PubMed:8664265}.
REGION 59 60 Glutathione binding.
{ECO:0000305|PubMed:8664265}.
REGION 72 73 Glutathione binding.
{ECO:0000305|PubMed:8664265}.
BINDING 50 50 Glutathione.
{ECO:0000305|PubMed:8664265}.
BINDING 116 116 Substrate. {ECO:0000250}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000250|UniProtKB:P15626}.
CONFLICT 147 147 W -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 3 10 {ECO:0000244|PDB:1B4P}.
TURN 12 14 {ECO:0000244|PDB:1B4P}.
HELIX 15 23 {ECO:0000244|PDB:1B4P}.
STRAND 28 33 {ECO:0000244|PDB:1B4P}.
TURN 38 40 {ECO:0000244|PDB:1B4P}.
HELIX 44 50 {ECO:0000244|PDB:1B4P}.
STRAND 60 65 {ECO:0000244|PDB:1B4P}.
STRAND 68 72 {ECO:0000244|PDB:1B4P}.
HELIX 73 83 {ECO:0000244|PDB:1B4P}.
HELIX 91 116 {ECO:0000244|PDB:1B4P}.
HELIX 120 142 {ECO:0000244|PDB:1B4P}.
STRAND 150 152 {ECO:0000244|PDB:1B4P}.
HELIX 155 170 {ECO:0000244|PDB:1B4P}.
TURN 172 177 {ECO:0000244|PDB:1B4P}.
HELIX 179 189 {ECO:0000244|PDB:1B4P}.
HELIX 192 198 {ECO:0000244|PDB:1B4P}.
STRAND 214 216 {ECO:0000244|PDB:1B4P}.
SEQUENCE 218 AA; 25703 MW; C23B30C171DB852F CRC64;
MPMTLGYWDI RGLAHAIRLF LEYTDTSYED KKYSMGDAPD YDRSQWLSEK FKLGLDFPNL
PYLIDGSHKI TQSNAILRYL GRKHNLCGET EEERIRVDVL ENQAMDTRLQ LAMVCYSPDF
ERKKPEYLEG LPEKMKLYSE FLGKQPWFAG NKITYVDFLV YDVLDQHRIF EPKCLDAFPN
LKDFVARFEG LKKISDYMKS GRFLSKPIFA KMAFWNPK


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