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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
 
 
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