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   24-JAN-2024, entry version 193.
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   ChEMBL; CHEMBL2504; -.
DR   iPTMnet; P08010; -.
DR   PhosphoSitePlus; P08010; -.
DR   jPOST; P08010; -.
DR   PaxDb; 10116-ENSRNOP00000025939; -.
DR   Ensembl; ENSRNOT00055036692; ENSRNOP00055029799; ENSRNOG00055021472.
DR   Ensembl; ENSRNOT00060045029; ENSRNOP00060037353; ENSRNOG00060026017.
DR   Ensembl; ENSRNOT00065040222; ENSRNOP00065032726; ENSRNOG00065023521.
DR   GeneID; 24424; -.
DR   KEGG; rno:24424; -.
DR   UCSC; RGD:2756; rat.
DR   AGR; RGD:2756; -.
DR   CTD; 2946; -.
DR   RGD; 2756; Gstm2.
DR   VEuPathDB; HostDB:ENSRNOG00000060939; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   InParanoid; P08010; -.
DR   OrthoDB; 5488107at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; P08010; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
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: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:0018916; P:nitrobenzene metabolic process; 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   CDD; cd03209; GST_C_Mu; 1.
DR   CDD; cd03075; GST_N_Mu; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF247; GLUTATHIONE S-TRANSFERASE MU 1; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01267; GSTRNSFRASEM.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   Genevisible; P08010; RN.
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
//