GSTM2_MOUSE
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 03-AUG-2022, entry version 178.
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, Pancreas,
RC 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; 3.
DR IntAct; P15626; 2.
DR STRING; 10090.ENSMUSP00000012348; -.
DR iPTMnet; P15626; -.
DR PhosphoSitePlus; P15626; -.
DR REPRODUCTION-2DPAGE; IPI00228820; -.
DR REPRODUCTION-2DPAGE; P15626; -.
DR SWISS-2DPAGE; P15626; -.
DR jPOST; P15626; -.
DR MaxQB; P15626; -.
DR PaxDb; P15626; -.
DR PeptideAtlas; P15626; -.
DR PRIDE; P15626; -.
DR ProteomicsDB; 271342; -.
DR DNASU; 14863; -.
DR Ensembl; ENSMUST00000012348; ENSMUSP00000012348; ENSMUSG00000040562.
DR GeneID; 14863; -.
DR KEGG; mmu:14863; -.
DR UCSC; uc008qxw.1; mouse.
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; RITESWA; -.
DR OrthoDB; 1162336at2759; -.
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 72 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 131 other tissues.
DR ExpressionAtlas; P15626; baseline and differential.
DR Genevisible; P15626; MM.
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:0005886; C:plasma membrane; 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 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 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
