ID   GSTM2_MOUSE             Reviewed;         218 AA.
AC   P15626;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Glutathione S-transferase Mu 2 {ECO:0000305};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P28161};
DE   AltName: Full=GST 5-5;
DE   AltName: Full=GST class-mu 2;
DE   AltName: Full=Glutathione S-transferase pmGT2;
GN   Name=Gstm2 {ECO:0000312|MGI:MGI:95861};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2689439; DOI=10.1016/s0021-9258(20)88223-4;
RA   Townsend A.J., Goldsmith M.E., Pickett C.B., Cowan K.H.;
RT   "Isolation, characterization, and expression in Escherichia coli of two
RT   murine Mu class glutathione S-transferase cDNAs homologous to the rat
RT   subunits 3 (Yb1) and 4 (Yb2).";
RL   J. Biol. Chem. 264:21582-21590(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=11404019; DOI=10.1016/s0378-1119(01)00473-5;
RA   Kumar A., Reddy E.P.;
RT   "Genomic organization and characterization of the promoter region of murine
RT   GSTM2 gene.";
RL   Gene 270:221-229(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-25.
RX   PubMed=8442656; DOI=10.1006/abbi.1993.1126;
RA   Awasthi S., Singhal S.S., Srivastava S.K., Awasthi Y.C.;
RT   "Purification and characterization of glutathione S-transferase of murine
RT   ovary and testis.";
RL   Arch. Biochem. Biophys. 301:143-150(1993).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR   EMBL; J04696; AAA37706.1; -; mRNA.
DR   EMBL; AF319526; AAK28508.1; -; Genomic_DNA.
DR   EMBL; BC037068; AAH37068.1; -; mRNA.
DR   CCDS; CCDS17746.1; -.
DR   PIR; B34159; B34159.
DR   RefSeq; NP_032209.1; NM_008183.3.
DR   AlphaFoldDB; P15626; -.
DR   SMR; P15626; -.
DR   BioGRID; 200095; 4.
DR   IntAct; P15626; 2.
DR   STRING; 10090.ENSMUSP00000012348; -.
DR   GlyGen; P15626; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P15626; -.
DR   PhosphoSitePlus; P15626; -.
DR   SwissPalm; P15626; -.
DR   REPRODUCTION-2DPAGE; IPI00228820; -.
DR   REPRODUCTION-2DPAGE; P15626; -.
DR   jPOST; P15626; -.
DR   MaxQB; P15626; -.
DR   PaxDb; 10090-ENSMUSP00000012348; -.
DR   PeptideAtlas; P15626; -.
DR   ProteomicsDB; 271342; -.
DR   Pumba; P15626; -.
DR   DNASU; 14863; -.
DR   Ensembl; ENSMUST00000012348.9; ENSMUSP00000012348.3; ENSMUSG00000040562.13.
DR   GeneID; 14863; -.
DR   KEGG; mmu:14863; -.
DR   UCSC; uc008qxw.1; mouse.
DR   AGR; MGI:95861; -.
DR   CTD; 2946; -.
DR   MGI; MGI:95861; Gstm2.
DR   VEuPathDB; HostDB:ENSMUSG00000040562; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000160258; -.
DR   HOGENOM; CLU_039475_2_0_1; -.
DR   InParanoid; P15626; -.
DR   OMA; FAKMALW; -.
DR   OrthoDB; 5488107at2759; -.
DR   PhylomeDB; P15626; -.
DR   TreeFam; TF353040; -.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   Reactome; R-MMU-9748787; Azathioprine ADME.
DR   Reactome; R-MMU-9753281; Paracetamol ADME.
DR   BioGRID-ORCS; 14863; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Gstm2; mouse.
DR   PRO; PR:P15626; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P15626; Protein.
DR   Bgee; ENSMUSG00000040562; Expressed in uterus and 134 other cell types or tissues.
DR   ExpressionAtlas; P15626; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0043295; F:glutathione binding; ISO:MGI.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
DR   GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0042178; P:xenobiotic catabolic process; ISO:MGI.
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   SWISS-2DPAGE; P15626; -.
DR   Genevisible; P15626; MM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Lipid metabolism; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8442656"
FT   CHAIN           2..218
FT                   /note="Glutathione S-transferase Mu 2"
FT                   /id="PRO_0000185827"
FT   DOMAIN          2..88
FT                   /note="GST N-terminal"
FT   DOMAIN          90..208
FT                   /note="GST C-terminal"
FT   BINDING         7..8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   BINDING         43..46
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   BINDING         50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   BINDING         59..60
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   BINDING         72..73
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08010"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   218 AA;  25717 MW;  93D790DD75CBF51E CRC64;
     MPMTLGYWDI RGLAHAIRLL LEYTDTSYED KKYTMGDAPD YDRSQWLSEK FKLGLDFPNL
     PYLIDGSHKI TQSNAILRYL ARKHNLCGET EEERIRVDIL ENQAMDTRIQ LAMVCYSPDF
     EKKKPEYLEG LPEKMKLYSE FLGKQPWFAG NKVTYVDFLV YDVLDQHRIF EPKCLDAFPN
     LKDFMGRFEG LKKISDYMKS SRFLSKPIFA KMAFWNPK
//