KMO_YEAST
ID KMO_YEAST Reviewed; 460 AA.
AC P38169; D6VPQ7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Kynurenine 3-monooxygenase {ECO:0000255|HAMAP-Rule:MF_03018};
DE EC=1.14.13.9 {ECO:0000255|HAMAP-Rule:MF_03018};
DE AltName: Full=Biosynthesis of nicotinic acid protein 4 {ECO:0000255|HAMAP-Rule:MF_03018};
DE AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_03018};
GN Name=BNA4 {ECO:0000255|HAMAP-Rule:MF_03018}; OrderedLocusNames=YBL098W;
GN ORFNames=YBL0828;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, AND PATHWAY.
RX PubMed=12062417; DOI=10.1016/s0014-5793(02)02585-1;
RA Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M.,
RA Rytka J., Herbert C.J.;
RT "Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae.";
RL FEBS Lett. 517:97-102(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP FUNCTION.
RX PubMed=15806102; DOI=10.1038/ng1542;
RA Giorgini F., Guidetti P., Nguyen Q., Bennett S.C., Muchowski P.J.;
RT "A genomic screen in yeast implicates kynurenine 3-monooxygenase as a
RT therapeutic target for Huntington disease.";
RL Nat. Genet. 37:526-531(2005).
RN [11] {ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31, ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34, ECO:0007744|PDB:4J36}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 1-396 IN COMPLEX WITH FAD AND
RP INHIBITOR, FUNCTION, AND MUTAGENESIS OF ARG-83.
RX PubMed=23575632; DOI=10.1038/nature12039;
RA Amaral M., Levy C., Heyes D.J., Lafite P., Outeiro T.F., Giorgini F.,
RA Leys D., Scrutton N.S.;
RT "Structural basis of kynurenine 3-monooxygenase inhibition.";
RL Nature 496:382-385(2013).
RN [12] {ECO:0007744|PDB:5X6R}
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 1-394 IN COMPLEX WITH FAD AND
RP INHIBITOR, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND MUTAGENESIS OF
RP 322-PHE-TYR-323.
RX PubMed=29429898; DOI=10.1016/j.chembiol.2018.01.008;
RA Kim H.T., Na B.K., Chung J., Kim S., Kwon S.K., Cha H., Son J., Cho J.M.,
RA Hwang K.Y.;
RT "Structural Basis for Inhibitor-Induced Hydrogen Peroxide Production by
RT Kynurenine 3-Monooxygenase.";
RL Cell Chem. Biol. 0:0-0(2018).
CC -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form
CC 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic
CC acid. {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:12062417,
CC ECO:0000269|PubMed:15806102, ECO:0000269|PubMed:23575632}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine +
CC H2O + NADP(+); Xref=Rhea:RHEA:20545, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57959, ChEBI:CHEBI:58125, ChEBI:CHEBI:58349;
CC EC=1.14.13.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03018,
CC ECO:0000269|PubMed:29429898};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:29429898};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018,
CC ECO:0000269|PubMed:12062417, ECO:0000269|PubMed:29429898}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_03018, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16407407}.
CC -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Deletion of BNA4 suppresses the toxicity of a mutant
CC HD/HTT fragment.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03018}.
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DR EMBL; X79489; CAA56002.1; -; Genomic_DNA.
DR EMBL; Z35859; CAA84920.1; -; Genomic_DNA.
DR EMBL; AY692951; AAT92970.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07027.1; -; Genomic_DNA.
DR PIR; S45402; S45402.
DR RefSeq; NP_009454.1; NM_001178338.1.
DR PDB; 4J2W; X-ray; 2.60 A; A/B=1-396.
DR PDB; 4J31; X-ray; 2.40 A; A/B=1-396.
DR PDB; 4J33; X-ray; 1.82 A; A/B=1-394.
DR PDB; 4J34; X-ray; 2.03 A; A/B=1-394.
DR PDB; 4J36; X-ray; 2.13 A; A/B=1-394.
DR PDB; 5X6R; X-ray; 1.91 A; A/B=1-394.
DR PDBsum; 4J2W; -.
DR PDBsum; 4J31; -.
DR PDBsum; 4J33; -.
DR PDBsum; 4J34; -.
DR PDBsum; 4J36; -.
DR PDBsum; 5X6R; -.
DR AlphaFoldDB; P38169; -.
DR SMR; P38169; -.
DR BioGRID; 32607; 96.
DR DIP; DIP-5165N; -.
DR IntAct; P38169; 2.
DR STRING; 4932.YBL098W; -.
DR BindingDB; P38169; -.
DR ChEMBL; CHEMBL3627588; -.
DR iPTMnet; P38169; -.
DR MaxQB; P38169; -.
DR PaxDb; P38169; -.
DR PRIDE; P38169; -.
DR EnsemblFungi; YBL098W_mRNA; YBL098W; YBL098W.
DR GeneID; 852179; -.
DR KEGG; sce:YBL098W; -.
DR SGD; S000000194; BNA4.
DR VEuPathDB; FungiDB:YBL098W; -.
DR eggNOG; KOG2614; Eukaryota.
DR GeneTree; ENSGT00390000000747; -.
DR HOGENOM; CLU_023210_0_1_1; -.
DR InParanoid; P38169; -.
DR OMA; REFMFIA; -.
DR BioCyc; MetaCyc:YBL098W-MON; -.
DR BioCyc; YEAST:YBL098W-MON; -.
DR BRENDA; 1.14.13.9; 984.
DR Reactome; R-SCE-71240; Tryptophan catabolism.
DR UniPathway; UPA00253; UER00328.
DR PRO; PR:P38169; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38169; protein.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0004502; F:kynurenine 3-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IDA:UniProtKB.
DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IGI:SGD.
DR GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0070189; P:kynurenine metabolic process; IDA:UniProtKB.
DR GO; GO:0019674; P:NAD metabolic process; IDA:UniProtKB.
DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_01971; Kynurenine_monooxygenase; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027545; Kynurenine_monooxygenase.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Monooxygenase; NADP; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..460
FT /note="Kynurenine 3-monooxygenase"
FT /id="PRO_0000020823"
FT BINDING 13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT ECO:0007744|PDB:4J36"
FT BINDING 32..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT ECO:0007744|PDB:4J36"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT ECO:0007744|PDB:4J36"
FT BINDING 83
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT BINDING 97
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT BINDING 109
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT ECO:0007744|PDB:4J36"
FT BINDING 133
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT ECO:0007744|PDB:4J36"
FT BINDING 195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4J33"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT ECO:0007744|PDB:4J36"
FT BINDING 325..328
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT ECO:0007744|PDB:4J36"
FT BINDING 373
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT BINDING 408
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT MUTAGEN 83
FT /note="R->A: Strongly decreases enzymatic activity."
FT /evidence="ECO:0000269|PubMed:23575632"
FT MUTAGEN 83
FT /note="R->M: Abolsihes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:23575632"
FT MUTAGEN 322..323
FT /note="FY->AA: Abolishes NADPH oxidase activity."
FT /evidence="ECO:0000269|PubMed:29429898"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:4J33"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4J34"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:4J33"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:4J33"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:4J33"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4J33"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:5X6R"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:4J33"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:4J33"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 326..343
FT /evidence="ECO:0007829|PDB:4J33"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:4J33"
FT HELIX 348..377
FT /evidence="ECO:0007829|PDB:4J33"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:4J33"
SQ SEQUENCE 460 AA; 52429 MW; 5340CC6C9D901D17 CRC64;
MSESVAIIGA GLVGCLAALA FSKEGYNVTL YDFRQDPRLD TTKNKNLKSI NLAISARGID
ALKSIDPDAC EHILQDMIPM KGRMIHDLKG RQESQLYGLH GEAINSINRS VLNNSLLDEL
EKSTTELKFG HKLVKIEWTD DKQICHFAIG EDLKTPHTEK YDFVIGCDGA YSATRSQMQR
KVEMDFSQEY MNLRYIELYI PPTEEFKPNY GGNFAIAPDH LHIWPRHKFM LIALANSDGS
FTSTFFGSKD QISDLITSKS RVREFLIENF PDIINIMDLD DAVKRFITYP KESLVCVNCK
PYDVPGGKAI LLGDAAHAMV PFYGQGMNCG FEDVRILMAL LKKHSGDRSR AFTEYTQTRH
KDLVSITELA KRNYKEMSHD VTSKRFLLRK KLDALFSIIM KDKWIPLYTM ISFRSDISYS
RALERAGKQT RILKFLESLT LGMLSIGGYK LFKFLTRERS
