GSTM2_CHICK
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 03-AUG-2022, entry version 139.
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}.
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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 Ensembl; ENSGALT00000077418; ENSGALP00000048878; ENSGALG00000032922.
DR GeneID; 395976; -.
DR KEGG; gga:395976; -.
DR CTD; 2946; -.
DR VEuPathDB; HostDB:geneid_395976; -.
DR GeneTree; ENSGT00940000154679; -.
DR InParanoid; P20136; -.
DR OMA; ADFIMYE; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P20136; -.
DR EvolutionaryTrace; P20136; -.
DR PRO; PR:P20136; -.
DR Proteomes; UP000000539; Chromosome 26.
DR Bgee; ENSGALG00000032922; Expressed in kidney and 13 other tissues.
DR ExpressionAtlas; P20136; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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 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
