ID GSTM1_RAT STANDARD; PRT; 217 AA. AC P04905; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 16-MAY-2006, entry version 75. DE Glutathione S-transferase Mu 1 (EC 2.5.1.18) (GSTM1-1) (Glutathione DE S-transferase Yb-1) (GST Yb1) (GST 3-3). GN Name=Gstm1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=86312882; PubMed=2875437; RA Lai H.-C.J., Grove G., Tu C.-P.D.; RT "Cloning and sequence analysis of a cDNA for a rat liver glutathione RT S-transferase Yb subunit."; RL Nucleic Acids Res. 14:6101-6114(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=86033768; PubMed=3840477; RA Ding G.J.-F., Lu A.Y.H., Pickett C.B.; RT "Rat liver glutathione S-transferases. Nucleotide sequence analysis of RT a Yb1 cDNA clone and prediction of the complete amino acid sequence of RT the Yb1 subunit."; RL J. Biol. Chem. 260:13268-13271(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=86224097; PubMed=3011803; RA Ding G.J.-F., Ding V.D.-H., Rodkey J.A., Bennett C.D., Lu A.Y.H., RA Pickett C.B.; RT "Rat liver glutathione S-transferases. DNA sequence analysis of a Yb2 RT cDNA clone and regulation of the Yb1 and Yb2 mRNAs by phenobarbital."; RL J. Biol. Chem. 261:7952-7957(1986). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87308179; PubMed=3040722; RA Chang C., Saltzman A.G., Sorensen N.S., Hiipakka R.A., Liao S.; RT "Identification of glutathione S-transferase Yb1 mRNA as the androgen- RT repressed mRNA by cDNA cloning and sequence analysis."; RL J. Biol. Chem. 262:11901-11903(1987). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP PROTEIN SEQUENCE OF 1-19; 82-95 AND 108-121. RX MEDLINE=93037509; PubMed=1416995; RA Katusz R.M., Bono B., Colman R.F.; RT "Identification of Tyr115 labeled by RT S-(4-bromo-2,3-dioxobutyl)glutathione in the hydrophobic substrate RT binding site of glutathione S-transferase, isoenzyme 3-3."; RL Arch. Biochem. Biophys. 298:667-677(1992). RN [7] RP PROTEIN SEQUENCE OF 1-20 AND 211-217. RX MEDLINE=89350924; PubMed=2669745; RA Hsieh J.C., Liu L.F., Chen W.L., Tam M.F.; RT "Expression of Yb1 glutathione S-transferase using a baculovirus RT expression system."; RL Biochem. Biophys. Res. Commun. 162:1147-1154(1989). RN [8] RP PROTEIN SEQUENCE OF 1-25. RX MEDLINE=91031411; PubMed=2226415; RA Chang L.H., Hsieh J.C., Chen W.L., Tam M.F.; RT "Identification of rat liver glutathione S-transferase Yb subunits by RT partial N-terminal sequencing after electroblotting of proteins onto a RT polyvinylidene difluoride membrane from an analytical isoelectric RT focusing gel."; RL Electrophoresis 11:589-593(1990). RN [9] RP PROTEIN SEQUENCE OF 1-23. RC STRAIN=Wistar; TISSUE=Olfactory epithelium; RX MEDLINE=93277499; PubMed=8503873; RA Ben-Arie N., Khen M., Lancet D.; RT "Glutathione S-transferases in rat olfactory epithelium: purification, RT molecular properties and odorant biotransformation."; RL Biochem. J. 292:379-384(1993). RN [10] RP PROTEIN SEQUENCE OF 1-19. RX MEDLINE=86042634; PubMed=3864155; RA Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., RA Warholm M., Joernvall H.; RT "Identification of three classes of cytosolic glutathione transferase RT common to several mammalian species: correlation between structural RT data and enzymatic properties."; RL Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985). RN [11] RP MUTAGENESIS OF CYS-86. RX MEDLINE=91354218; PubMed=1883338; RA Hsieh J.-C., Huang S.-C., Chen W.-L., Lai Y.-C., Tam M.F.; RT "Cysteine-86 is not needed for the enzymic activity of glutathione RT S-transferase 3-3."; RL Biochem. J. 278:293-297(1991). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=93041702; PubMed=1420139; RA Ji X., Zhang P., Armstrong R.N., Gilliland G.L.; RT "The three-dimensional structure of a glutathione S-transferase from RT the mu gene class. Structural analysis of the binary complex of RT isoenzyme 3-3 and glutathione at 2.2-A resolution."; RL Biochemistry 31:10169-10184(1992). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=15299462; DOI=10.1107/S0907444993009370; RA Fu J.-H., Rose J., Tam M.F., Wang B.-C.; RT "New crystal forms of a mu-class glutathione S-transferase from rat RT liver."; RL Acta Crystallogr. D 50:219-224(1994). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=94153886; PubMed=8110735; RA Ji X., Johnson W.W., Sesay M.A., Dickert L., Prasad S.M., Ammon H.L., RA Armstrong R.N., Gilliland G.L.; RT "Structure and function of the xenobiotic substrate binding site of a RT glutathione S-transferase as revealed by X-ray crystallographic RT analysis of product complexes with the diastereomers of RT 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene."; RL Biochemistry 33:1043-1052(1994). CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of CC exogenous and endogenous hydrophobic electrophiles. The olfactory CC GST may be crucial for the acuity of the olfactory process. CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- SUBUNIT: Homodimer or heterodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Yb subclass selectively binds steroid hormones. CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X04229; CAA27811.1; -; mRNA. DR EMBL; M11719; AAA41287.1; -; mRNA. DR EMBL; J02810; AAA41293.1; -; mRNA. DR EMBL; BC063172; AAH63172.1; -; mRNA. DR PIR; A29794; A29794. DR UniGene; Rn.625; -. DR PDB; 1GSB; X-ray; A/B/C/D=1-217. DR PDB; 1GSC; X-ray; A/B/C/D=1-217. DR PDB; 1MTC; X-ray; A/B=1-217. DR PDB; 2GST; X-ray; A/B=1-217. DR PDB; 3FYG; X-ray; A/B=1-217. DR PDB; 3GST; X-ray; A/B=1-217. DR PDB; 4GST; X-ray; A/B=1-217. DR PDB; 5FWG; X-ray; A/B=1-217. DR PDB; 5GST; X-ray; A/B=1-217. DR PDB; 6GST; X-ray; A/B=1-217. DR PDB; 6GSU; X-ray; A/B=1-217. DR PDB; 6GSV; X-ray; A/B=1-217. DR PDB; 6GSW; X-ray; A/B=1-217. DR PDB; 6GSX; X-ray; A/B=1-217. DR PDB; 6GSY; X-ray; A/B=1-217. DR Ensembl; ENSRNOG00000029726; Rattus norvegicus. DR RGD; 2755; Gstm1. DR LinkHub; P04905; -. DR GO; GO:0005576; C:extracellular region; IDA. DR GO; GO:0004364; F:glutathione transferase activity; IDA. DR GO; GO:0005496; F:steroid binding; IPI. DR InterPro; IPR004046; GST_C. DR InterPro; IPR010987; GST_C_like. DR InterPro; IPR003081; GST_mu. DR InterPro; IPR004045; GST_N. DR InterPro; IPR012336; Thiordxn-like_fd. DR InterPro; IPR012335; Thioredoxin_fold. DR PANTHER; PTHR11571:SF6; GST_mu; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR PRINTS; PR01267; GSTRNSFRASEM. KW 3D-structure; Direct protein sequencing; Olfaction; KW Sensory transduction; Transferase. FT INIT_MET 0 0 FT CHAIN 1 217 Glutathione S-transferase Mu 1. FT /FTId=PRO_0000185831. FT MUTAGEN 86 86 C->S: No change in activity. FT CONFLICT 168 168 I -> N (in Ref. 3). FT CONFLICT 198 199 KS -> NC (in Ref. 2). FT STRAND 2 9 FT TURN 11 13 FT HELIX 14 22 FT TURN 23 24 FT STRAND 27 32 FT TURN 37 40 FT HELIX 43 46 FT TURN 47 50 FT STRAND 51 52 FT STRAND 55 56 FT STRAND 59 64 FT TURN 65 66 FT STRAND 67 71 FT HELIX 72 82 FT TURN 83 84 FT STRAND 86 86 FT STRAND 88 89 FT HELIX 90 114 FT TURN 115 115 FT TURN 117 118 FT HELIX 119 141 FT TURN 142 143 FT STRAND 145 151 FT HELIX 154 169 FT STRAND 170 170 FT TURN 171 174 FT STRAND 175 176 FT HELIX 178 188 FT TURN 189 189 FT STRAND 190 190 FT HELIX 191 197 FT TURN 198 198 FT STRAND 199 199 FT TURN 200 201 FT STRAND 208 208 FT TURN 210 211 FT STRAND 212 215 SQ SEQUENCE 217 AA; 25783 MW; 2ACE8D49DA785118 CRC64; PMILGYWNVR GLTHPIRLLL EYTDSSYEEK RYAMGDAPDY DRSQWLNEKF KLGLDFPNLP YLIDGSRKIT QSNAIMRYLA RKHHLCGETE EERIRADIVE NQVMDNRMQL IMLCYNPDFE KQKPEFLKTI PEKMKLYSEF LGKRPWFAGD KVTYVDFLAY DILDQYHIFE PKCLDAFPNL KDFLARFEGL KKISAYMKSS RYLSTPIFSK LAQWSNK //