ID GSTM2_CHICK Reviewed; 220 AA. AC P20136; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 145. DE RecName: Full=Glutathione S-transferase 2 {ECO:0000305}; DE EC=2.5.1.18 {ECO:0000269|PubMed:10903867}; DE AltName: Full=GST class-mu; DE AltName: Full=GST-CL2; DE AltName: Full=GSTM1-1; GN Name=GSTM2; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=White leghorn; TISSUE=Liver; RX PubMed=1954256; DOI=10.1016/0167-4781(91)90199-v; RA Liu L.-F., Tam M.F.; RT "Nucleotide sequence of a class mu glutathione S-transferase from chicken RT liver."; RL Biochim. Biophys. Acta 1090:343-344(1991). RN [2] RP PROTEIN SEQUENCE OF 2-35. RC TISSUE=Liver; RX PubMed=2337594; DOI=10.1021/bi00455a022; RA Chang L.-H., Chuang L.-F., Tsai C.-P., Tu C.-P.D., Tam M.F.; RT "Characterization of glutathione S-transferases from day-old chick RT livers."; RL Biochemistry 29:744-750(1990). RN [3] RP SEQUENCE REVISION TO 130. RA Liu L.-F.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG. RX PubMed=9571047; DOI=10.1006/jmbi.1998.1716; RA Sun Y.-J., Kuan I.-C., Tam M.F., Hsiao C.-D.; RT "The three-dimensional structure of an avian class-mu glutathione S- RT transferase, cGSTM1-1 at 1.94-A resolution."; RL J. Mol. Biol. 278:239-252(1998). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG, RP CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-108 AND TRP-210, AND FUNCTION. RX PubMed=10903867; DOI=10.1006/jmbi.2000.3904; RA Chern M.K., Wu T.C., Hsieh C.H., Chou C.C., Liu L.F., Kuan I.C., Yeh Y.H., RA Hsiao C.D., Tam M.F.; RT "Tyr115, gln165 and trp209 contribute to the 1, 2-epoxy-3-(p- RT nitrophenoxy)propane-conjugating activity of glutathione S-transferase RT cGSTM1-1."; RL J. Mol. Biol. 300:1257-1269(2000). CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of CC exogenous and endogenous hydrophobic electrophiles (By similarity) CC (PubMed:10903867). Participates in the formation of novel hepoxilin CC regioisomers (By similarity). {ECO:0000250|UniProtKB:P28161, CC ECO:0000269|PubMed:10903867}. 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:0000269|PubMed:10903867}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; CC Evidence={ECO:0000305|PubMed:10903867}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10903867, CC ECO:0000269|PubMed:9571047}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X58248; CAA41202.1; -; mRNA. DR PIR; S18464; S18464. DR RefSeq; NP_990421.1; NM_205090.1. DR PDB; 1C72; X-ray; 2.80 A; A/B/C/D=2-220. DR PDB; 1GSU; X-ray; 1.94 A; A/B=2-220. DR PDBsum; 1C72; -. DR PDBsum; 1GSU; -. DR AlphaFoldDB; P20136; -. DR SMR; P20136; -. DR STRING; 9031.ENSGALP00000048878; -. DR Ensembl; ENSGALT00015054992; ENSGALP00015033092; ENSGALG00015022497. DR GeneID; 395976; -. DR KEGG; gga:395976; -. DR CTD; 2946; -. DR VEuPathDB; HostDB:geneid_395976; -. DR InParanoid; P20136; -. DR OMA; WRTAQWC; -. DR OrthoDB; 5488107at2759; -. DR PhylomeDB; P20136; -. DR Reactome; R-GGA-156590; Glutathione conjugation. DR Reactome; R-GGA-9026762; Biosynthesis of maresin conjugates in tissue regeneration (MCTR). DR Reactome; R-GGA-9748787; Azathioprine ADME. DR Reactome; R-GGA-9753281; Paracetamol ADME. DR EvolutionaryTrace; P20136; -. DR PRO; PR:P20136; -. DR Proteomes; UP000000539; Chromosome 26. DR Bgee; ENSGALG00000032922; Expressed in kidney and 13 other cell types or tissues. DR ExpressionAtlas; P20136; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IEA:UniProt. DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. 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:SF222; GLUTATHIONE S-TRANSFERASE 2-RELATED; 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. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Lipid metabolism; KW Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2337594" FT CHAIN 2..220 FT /note="Glutathione S-transferase 2" FT /id="PRO_0000185838" 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:0000305|PubMed:10903867, FT ECO:0000305|PubMed:9571047" FT BINDING 43..46 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000305|PubMed:10903867, FT ECO:0000305|PubMed:9571047" 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:0000305|PubMed:10903867, FT ECO:0000305|PubMed:9571047" FT BINDING 72..73 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000305|PubMed:10903867, FT ECO:0000305|PubMed:9571047" FT BINDING 116 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MUTAGEN 108 FT /note="R->E: Reduced affinity for glutathione." FT /evidence="ECO:0000269|PubMed:10903867" FT MUTAGEN 108 FT /note="R->L: Reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:10903867" FT MUTAGEN 210 FT /note="W->F: Reduced affinity for glutathione." FT /evidence="ECO:0000269|PubMed:10903867" FT MUTAGEN 210 FT /note="W->H,I,P: Reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:10903867" FT STRAND 3..11 FT /evidence="ECO:0007829|PDB:1GSU" FT HELIX 12..14 FT /evidence="ECO:0007829|PDB:1GSU" FT HELIX 15..23 FT /evidence="ECO:0007829|PDB:1GSU" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:1GSU" FT TURN 38..40 FT /evidence="ECO:0007829|PDB:1C72" FT HELIX 44..47 FT /evidence="ECO:0007829|PDB:1GSU" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:1GSU" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:1GSU" FT STRAND 68..72 FT /evidence="ECO:0007829|PDB:1GSU" FT HELIX 73..82 FT /evidence="ECO:0007829|PDB:1GSU" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:1GSU" FT HELIX 91..116 FT /evidence="ECO:0007829|PDB:1GSU" FT HELIX 120..142 FT /evidence="ECO:0007829|PDB:1GSU" FT STRAND 146..152 FT /evidence="ECO:0007829|PDB:1GSU" FT HELIX 155..170 FT /evidence="ECO:0007829|PDB:1GSU" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:1GSU" FT HELIX 180..189 FT /evidence="ECO:0007829|PDB:1GSU" FT HELIX 192..198 FT /evidence="ECO:0007829|PDB:1GSU" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:1GSU" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:1GSU" SQ SEQUENCE 220 AA; 25893 MW; A7A7D843CE54E6F9 CRC64; MVVTLGYWDI RGLAHAIRLL LEYTETPYQE RRYKAGPAPD FDPSDWTNEK EKLGLDFPNL PYLIDGDVKL TQSNAILRYI ARKHNMCGET EVEKQRVDVL ENHLMDLRMA FARLCYSPDF EKLKPAYLEQ LPGKLRQLSR FLGSRSWFVG DKLTFVDFLA YDVLDQQRMF VPDCPELQGN LSQFLQRFEA LEKISAYMRS GRFMKAPIFW YTALWNNKKE //