GSTM1_RAT
ID GSTM1_RAT Reviewed; 218 AA.
AC P04905;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Glutathione S-transferase Mu 1 {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P09488};
DE AltName: Full=GST 3-3;
DE AltName: Full=GSTM1-1;
DE AltName: Full=Glutathione S-transferase Yb-1;
DE Short=GST Yb1;
GN Name=Gstm1 {ECO:0000312|RGD:2755};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2875437; DOI=10.1093/nar/14.15.6101;
RA Lai H.-C.J., Grove G., Tu C.-P.D.;
RT "Cloning and sequence analysis of a cDNA for a rat liver glutathione S-
RT transferase Yb subunit.";
RL Nucleic Acids Res. 14:6101-6114(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3840477; DOI=10.1016/s0021-9258(17)38864-6;
RA Ding G.J.-F., Lu A.Y.H., Pickett C.B.;
RT "Rat liver glutathione S-transferases. Nucleotide sequence analysis of a
RT Yb1 cDNA clone and prediction of the complete amino acid sequence of the
RT Yb1 subunit.";
RL J. Biol. Chem. 260:13268-13271(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-24, AND SUBUNIT.
RX PubMed=3011803; DOI=10.1016/s0021-9258(19)57495-6;
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 cDNA
RT 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 PubMed=3040722; DOI=10.1016/s0021-9258(18)45291-x;
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;
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 [6]
RP PROTEIN SEQUENCE OF 2-20; 83-96 AND 109-122.
RX PubMed=1416995; DOI=10.1016/0003-9861(92)90464-8;
RA Katusz R.M., Bono B., Colman R.F.;
RT "Identification of Tyr115 labeled by S-(4-bromo-2,3-dioxobutyl)glutathione
RT in the hydrophobic substrate binding site of glutathione S-transferase,
RT isoenzyme 3-3.";
RL Arch. Biochem. Biophys. 298:667-677(1992).
RN [7]
RP PROTEIN SEQUENCE OF 2-21 AND 212-218.
RX PubMed=2669745; DOI=10.1016/0006-291x(89)90793-6;
RA Hsieh J.C., Liu L.F., Chen W.L., Tam M.F.;
RT "Expression of Yb1 glutathione S-transferase using a baculovirus expression
RT system.";
RL Biochem. Biophys. Res. Commun. 162:1147-1154(1989).
RN [8]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=2226415; DOI=10.1002/elps.1150110710;
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 focusing
RT gel.";
RL Electrophoresis 11:589-593(1990).
RN [9]
RP PROTEIN SEQUENCE OF 2-24.
RC STRAIN=Wistar; TISSUE=Olfactory epithelium;
RX PubMed=8503873; DOI=10.1042/bj2920379;
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 2-20.
RX PubMed=3864155; DOI=10.1073/pnas.82.21.7202;
RA Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M.,
RA Joernvall H.;
RT "Identification of three classes of cytosolic glutathione transferase
RT common to several mammalian species: correlation between structural data
RT and enzymatic properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985).
RN [11]
RP PROTEIN SEQUENCE OF 19-32; 33-50; 53-68; 70-78; 97-108; 137-144; 174-187
RP AND 203-218, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [12]
RP MUTAGENESIS OF CYS-87.
RX PubMed=1883338; DOI=10.1042/bj2780293;
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 S-
RT transferase 3-3.";
RL Biochem. J. 278:293-297(1991).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-205 AND SER-210, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RX PubMed=1420139; DOI=10.1021/bi00157a004;
RA Ji X., Zhang P., Armstrong R.N., Gilliland G.L.;
RT "The three-dimensional structure of a glutathione S-transferase from the mu
RT gene class. Structural analysis of the binary complex of isoenzyme 3-3 and
RT glutathione at 2.2-A resolution.";
RL Biochemistry 31:10169-10184(1992).
RN [15]
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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE
RP ANALOGS, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-116.
RX PubMed=8110735; DOI=10.1021/bi00171a002;
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 analysis of
RT product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-
RT 9,10-dihydrophenanthrene.";
RL Biochemistry 33:1043-1052(1994).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT PHE-7 IN COMPLEXES WITH
RP GLUTATHIONE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-7.
RX PubMed=8664265; DOI=10.1021/bi960189k;
RA Xiao G., Liu S., Ji X., Johnson W.W., Chen J., Parsons J.F., Stevens W.J.,
RA Gilliland G.L., Armstrong R.N.;
RT "First-sphere and second-sphere electrostatic effects in the active site of
RT a class mu gluthathione transferase.";
RL Biochemistry 35:4753-4765(1996).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. The olfactory GST
CC may be crucial for the acuity of the olfactory process (PubMed:8110735,
CC PubMed:8664265). Participates in the formation of novel hepoxilin
CC regioisomers (By similarity). {ECO:0000250|UniProtKB:P09488,
CC ECO:0000269|PubMed:8110735, ECO:0000269|PubMed:8664265}.
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; Evidence={ECO:0000269|PubMed:8110735,
CC ECO:0000269|PubMed:8664265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000305|PubMed:8110735, ECO:0000305|PubMed:8664265};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133768;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133771;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133772;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133769;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801;
CC Evidence={ECO:0000250|UniProtKB:P09488};
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:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- SUBUNIT: Homodimer or heterodimer. {ECO:0000269|PubMed:1420139,
CC ECO:0000269|PubMed:3011803, ECO:0000269|PubMed:8110735}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Yb subclass selectively binds steroid hormones.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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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 RefSeq; NP_058710.1; NM_017014.1.
DR PDB; 1GSB; X-ray; 2.50 A; A/B/C/D=2-218.
DR PDB; 1GSC; X-ray; 2.50 A; A/B/C/D=2-218.
DR PDB; 1MTC; X-ray; 2.20 A; A/B=2-218.
DR PDB; 2GST; X-ray; 1.80 A; A/B=2-218.
DR PDB; 3FYG; X-ray; 2.20 A; A/B=2-218.
DR PDB; 3GST; X-ray; 1.90 A; A/B=2-218.
DR PDB; 4GST; X-ray; 1.90 A; A/B=2-218.
DR PDB; 5FWG; X-ray; 2.00 A; A/B=2-218.
DR PDB; 5GST; X-ray; 2.00 A; A/B=2-218.
DR PDB; 6GST; X-ray; 2.20 A; A/B=2-218.
DR PDB; 6GSU; X-ray; 1.85 A; A/B=2-218.
DR PDB; 6GSV; X-ray; 1.75 A; A/B=2-218.
DR PDB; 6GSW; X-ray; 1.85 A; A/B=2-218.
DR PDB; 6GSX; X-ray; 1.91 A; A/B=2-218.
DR PDB; 6GSY; X-ray; 2.20 A; A/B=2-218.
DR PDBsum; 1GSB; -.
DR PDBsum; 1GSC; -.
DR PDBsum; 1MTC; -.
DR PDBsum; 2GST; -.
DR PDBsum; 3FYG; -.
DR PDBsum; 3GST; -.
DR PDBsum; 4GST; -.
DR PDBsum; 5FWG; -.
DR PDBsum; 5GST; -.
DR PDBsum; 6GST; -.
DR PDBsum; 6GSU; -.
DR PDBsum; 6GSV; -.
DR PDBsum; 6GSW; -.
DR PDBsum; 6GSX; -.
DR PDBsum; 6GSY; -.
DR AlphaFoldDB; P04905; -.
DR SMR; P04905; -.
DR BioGRID; 246588; 3.
DR IntAct; P04905; 1.
DR STRING; 10116.ENSRNOP00000039050; -.
DR ChEMBL; CHEMBL2209; -.
DR iPTMnet; P04905; -.
DR PhosphoSitePlus; P04905; -.
DR SwissPalm; P04905; -.
DR jPOST; P04905; -.
DR PaxDb; P04905; -.
DR PRIDE; P04905; -.
DR GeneID; 24423; -.
DR KEGG; rno:24423; -.
DR UCSC; RGD:2755; rat.
DR CTD; 2944; -.
DR RGD; 2755; Gstm1.
DR eggNOG; KOG1695; Eukaryota.
DR InParanoid; P04905; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P04905; -.
DR BRENDA; 2.5.1.18; 5301.
DR Reactome; R-RNO-156590; Glutathione conjugation.
DR EvolutionaryTrace; P04905; -.
DR PRO; PR:P04905; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0043295; F:glutathione binding; IDA:CAFA.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0016151; F:nickel cation binding; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0005496; F:steroid binding; IPI:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0018916; P:nitrobenzene metabolic process; ISO:RGD.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0010226; P:response to lithium ion; IEP:RGD.
DR GO; GO:0010038; P:response to metal ion; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:CAFA.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
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; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
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 Olfaction; Phosphoprotein; Reference proteome; Sensory transduction;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1416995,
FT ECO:0000269|PubMed:2226415, ECO:0000269|PubMed:2669745,
FT ECO:0000269|PubMed:3011803, ECO:0000269|PubMed:3864155,
FT ECO:0000269|PubMed:8503873"
FT CHAIN 2..218
FT /note="Glutathione S-transferase Mu 1"
FT /id="PRO_0000185831"
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:0000269|PubMed:8664265,
FT ECO:0000305|PubMed:8110735"
FT BINDING 43..46
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:8664265,
FT ECO:0000305|PubMed:8110735"
FT BINDING 50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:8664265,
FT ECO:0000305|PubMed:8110735"
FT BINDING 59..60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:8664265,
FT ECO:0000305|PubMed:8110735"
FT BINDING 72..73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:8664265,
FT ECO:0000305|PubMed:8110735"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 7
FT /note="Y->F,L: Reduces catalytic activity about 100-fold."
FT /evidence="ECO:0000269|PubMed:8664265"
FT MUTAGEN 87
FT /note="C->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:1883338"
FT MUTAGEN 116
FT /note="Y->F: Reduces enzyme activity about 100-fold."
FT /evidence="ECO:0000269|PubMed:8110735"
FT CONFLICT 199..200
FT /note="KS -> NC (in Ref. 2; AAA41287)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:6GSV"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:6GSV"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:6GSV"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:6GSV"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:6GSV"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:6GSV"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:6GSV"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:6GSV"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:6GSV"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:6GSV"
FT HELIX 91..115
FT /evidence="ECO:0007829|PDB:6GSV"
FT HELIX 120..142
FT /evidence="ECO:0007829|PDB:6GSV"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:6GSV"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:6GSV"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:6GSV"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:6GSV"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:6GSV"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6GSX"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:6GSV"
SQ SEQUENCE 218 AA; 25914 MW; 1A8E80D09A5CACA8 CRC64;
MPMILGYWNV RGLTHPIRLL LEYTDSSYEE KRYAMGDAPD YDRSQWLNEK FKLGLDFPNL
PYLIDGSRKI TQSNAIMRYL ARKHHLCGET EEERIRADIV ENQVMDNRMQ LIMLCYNPDF
EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYHIF EPKCLDAFPN
LKDFLARFEG LKKISAYMKS SRYLSTPIFS KLAQWSNK
