GSTM2_RAT
ID GSTM2_RAT Reviewed; 218 AA.
AC P08010;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Glutathione S-transferase Mu 2 {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P28161};
DE AltName: Full=GST 4-4;
DE AltName: Full=GSTM2-2;
DE AltName: Full=Glutathione S-transferase Yb-2;
DE Short=GST Yb2;
GN Name=Gstm2 {ECO:0000312|RGD:2756};
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 [GENOMIC DNA].
RX PubMed=3403534; DOI=10.1016/s0021-9258(18)37969-9;
RA Lai H.-C.J., Qian B., Grove G., Tu C.-P.D.;
RT "Gene expression of rat glutathione S-transferases. Evidence for gene
RT conversion in the evolution of the Yb multigene family.";
RL J. Biol. Chem. 263:11389-11395(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-218.
RC STRAIN=Sprague-Dawley;
RX PubMed=3699019; DOI=10.1111/j.1432-1033.1986.tb09588.x;
RA Alin P., Mannervik B., Joernvall H.;
RT "Cytosolic rat liver glutathione transferase 4-4. Primary structure of the
RT protein reveals extensive differences between homologous glutathione
RT transferases of classes alpha and mu.";
RL Eur. J. Biochem. 156:343-350(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-218.
RX PubMed=3011803; DOI=10.1016/s0021-9258(19)57495-6;
RA Ding G.J.-F., Ding V.D.-H., Rodkey J.A., Bennett C.D., Lu A.Y.H.,
RA Pickett C.B.;
RT "Rat liver glutathione S-transferases. DNA sequence analysis of a Yb2 cDNA
RT clone and regulation of the Yb1 and Yb2 mRNAs by phenobarbital.";
RL J. Biol. Chem. 261:7952-7957(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-218.
RX PubMed=3020050; DOI=10.1016/s0021-9258(18)67089-9;
RA Lai H.-C.J., Tu C.-P.D.;
RT "Rat glutathione S-transferases supergene family. Characterization of an
RT anionic Yb subunit cDNA clone.";
RL J. Biol. Chem. 261:13793-13799(1986).
RN [5]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=3864155; DOI=10.1073/pnas.82.21.7202;
RA Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M.,
RA Joernvall H.;
RT "Identification of three classes of cytosolic glutathione transferase
RT common to several mammalian species: correlation between structural data
RT and enzymatic properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985).
RN [6]
RP PROTEIN SEQUENCE OF 2-28.
RX PubMed=2226415; DOI=10.1002/elps.1150110710;
RA Chang L.H., Hsieh J.C., Chen W.L., Tam M.F.;
RT "Identification of rat liver glutathione S-transferase Yb subunits by
RT partial N-terminal sequencing after electroblotting of proteins onto a
RT polyvinylidene difluoride membrane from an analytical isoelectric focusing
RT gel.";
RL Electrophoresis 11:589-593(1990).
RN [7]
RP PROTEIN SEQUENCE OF 2-22.
RC STRAIN=Wistar; TISSUE=Olfactory epithelium;
RX PubMed=8503873; DOI=10.1042/bj2920379;
RA Ben-Arie N., Khen M., Lancet D.;
RT "Glutathione S-transferases in rat olfactory epithelium: purification,
RT molecular properties and odorant biotransformation.";
RL Biochem. J. 292:379-384(1993).
RN [8]
RP PROTEIN SEQUENCE OF 33-43; 137-144; 153-168 AND 174-182, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-44, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.
RX PubMed=8664265; DOI=10.1021/bi960189k;
RA Xiao G., Liu S., Ji X., Johnson W.W., Chen J., Parsons J.F., Stevens W.J.,
RA Gilliland G.L., Armstrong R.N.;
RT "First-sphere and second-sphere electrostatic effects in the active site of
RT a class mu gluthathione transferase.";
RL Biochemistry 35:4753-4765(1996).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Participates in the
CC formation of novel hepoxilin regioisomers.
CC {ECO:0000250|UniProtKB:P28161}.
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:P28161};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000250|UniProtKB:P28161};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate +
CC glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-
CC eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:132200, ChEBI:CHEBI:132201;
CC Evidence={ECO:0000250|UniProtKB:P28161};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261;
CC Evidence={ECO:0000250|UniProtKB:P28161};
CC -!- SUBUNIT: Homodimer or heterodimer. {ECO:0000269|PubMed:8664265}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Yb subclass selectively binds steroid hormones.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; J02592; AAA41285.1; -; mRNA.
DR EMBL; M13590; AAA42351.1; -; mRNA.
DR EMBL; J03914; AAA41296.1; -; Genomic_DNA.
DR PIR; A29231; XURTG4.
DR RefSeq; NP_803175.1; NM_177426.1.
DR PDB; 1B4P; X-ray; 1.70 A; A=2-218.
DR PDBsum; 1B4P; -.
DR AlphaFoldDB; P08010; -.
DR SMR; P08010; -.
DR BioGRID; 246589; 1.
DR IntAct; P08010; 2.
DR STRING; 10116.ENSRNOP00000025939; -.
DR ChEMBL; CHEMBL2504; -.
DR iPTMnet; P08010; -.
DR PhosphoSitePlus; P08010; -.
DR jPOST; P08010; -.
DR PaxDb; P08010; -.
DR PRIDE; P08010; -.
DR GeneID; 24424; -.
DR KEGG; rno:24424; -.
DR UCSC; RGD:2756; rat.
DR CTD; 2946; -.
DR RGD; 2756; Gstm2.
DR VEuPathDB; HostDB:ENSRNOG00000060939; -.
DR eggNOG; KOG1695; Eukaryota.
DR InParanoid; P08010; -.
DR OMA; RITESWA; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P08010; -.
DR TreeFam; TF353040; -.
DR BRENDA; 2.5.1.18; 5301.
DR Reactome; R-RNO-156590; Glutathione conjugation.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR EvolutionaryTrace; P08010; -.
DR PRO; PR:P08010; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000018937; Expressed in liver and 20 other tissues.
DR ExpressionAtlas; P08010; baseline and differential.
DR Genevisible; P08010; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0005504; F:fatty acid binding; ISO:RGD.
DR GO; GO:0043295; F:glutathione binding; IDA:CAFA.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISO:RGD.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; ISO:RGD.
DR GO; GO:0071313; P:cellular response to caffeine; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; IMP:RGD.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043651; P:linoleic acid metabolic process; ISO:RGD.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISO:RGD.
DR GO; GO:0018916; P:nitrobenzene metabolic process; ISO:RGD.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISO:RGD.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:1902168; P:response to catechin; IEP:RGD.
DR GO; GO:0033595; P:response to genistein; IEP:RGD.
DR GO; GO:0010038; P:response to metal ion; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:CAFA.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:RGD.
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; IPR004046; GST_C.
DR InterPro; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
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 3D-structure; Cytoplasm; Direct protein sequencing; Lipid metabolism;
KW Olfaction; Phosphoprotein; Reference proteome; Sensory transduction;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2226415,
FT ECO:0000269|PubMed:3699019, ECO:0000269|PubMed:3864155,
FT ECO:0000269|PubMed:8503873"
FT CHAIN 2..218
FT /note="Glutathione S-transferase Mu 2"
FT /id="PRO_0000185832"
FT DOMAIN 2..88
FT /note="GST N-terminal"
FT DOMAIN 90..214
FT /note="GST C-terminal"
FT BINDING 7..8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000305|PubMed:8664265"
FT BINDING 43..46
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000305|PubMed:8664265"
FT BINDING 50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000305|PubMed:8664265"
FT BINDING 59..60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000305|PubMed:8664265"
FT BINDING 72..73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000305|PubMed:8664265"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15626"
FT CONFLICT 147
FT /note="W -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1B4P"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1B4P"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:1B4P"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1B4P"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1B4P"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:1B4P"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1B4P"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1B4P"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:1B4P"
FT HELIX 91..116
FT /evidence="ECO:0007829|PDB:1B4P"
FT HELIX 120..142
FT /evidence="ECO:0007829|PDB:1B4P"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1B4P"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:1B4P"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:1B4P"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:1B4P"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:1B4P"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1B4P"
SQ 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
