C83B1_ARATH
ID C83B1_ARATH Reviewed; 499 AA.
AC O65782;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cytochrome P450 83B1 {ECO:0000303|PubMed:11114200, ECO:0000303|PubMed:9808718};
DE EC=1.14.14.45 {ECO:0000269|PubMed:12970475};
DE AltName: Full=Protein ALTERED TRYPTOPHAN REGULATION 4;
DE AltName: Full=Protein RED ELONGATED 1 {ECO:0000303|PubMed:14963708};
DE AltName: Full=Protein SUPERROOT 2 {ECO:0000303|PubMed:11114200, ECO:0000303|PubMed:9675903};
GN Name=CYP83B1 {ECO:0000303|PubMed:11114200, ECO:0000303|PubMed:9808718};
GN Synonyms=ATR4, RED1 {ECO:0000303|PubMed:14963708}, RNT1, RUNT1,
GN SUR2 {ECO:0000303|PubMed:11114200, ECO:0000303|PubMed:9675903};
GN OrderedLocusNames=At4g31500 {ECO:0000312|Araport:AT4G31500};
GN ORFNames=F3L17.70 {ECO:0000312|EMBL:CAB45909.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=9620263; DOI=10.1023/a:1005921406884;
RA Mizutani M., Ward E., Ohta D.;
RT "Cytochrome P450 superfamily in Arabidopsis thaliana: isolation of cDNAs,
RT differential expression, and RFLP mapping of multiple cytochromes P450.";
RL Plant Mol. Biol. 37:39-52(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=9675903; DOI=10.1046/j.1365-313x.1998.00163.x;
RA Delarue M., Prinsen E., Onckelen H.V., Caboche M., Bellini C.;
RT "Sur2 mutations of Arabidopsis thaliana define a new locus involved in the
RT control of auxin homeostasis.";
RL Plant J. 14:603-611(1998).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=9808718; DOI=10.1104/pp.118.3.743;
RA Winkler R.G., Frank M.R., Galbraith D.W., Feyereisen R., Feldmann K.A.;
RT "Systematic reverse genetics of transfer-DNA-tagged lines of Arabidopsis.
RT Isolation of mutations in the cytochrome p450 gene superfamily.";
RL Plant Physiol. 118:743-750(1998).
RN [8]
RP FUNCTION, AND INDUCTION BY AUXIN.
RX PubMed=11114200; DOI=10.1073/pnas.260502697;
RA Barlier I., Kowalczyk M., Marchant A., Ljung K., Bhalerao R., Bennett M.,
RA Sandberg G., Bellini C.;
RT "The SUR2 gene of Arabidopsis thaliana encodes the cytochrome P450 CYP83B1,
RT a modulator of auxin homeostasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14819-14824(2000).
RN [9]
RP FUNCTION.
RX PubMed=11333274; DOI=10.1074/jbc.m102637200;
RA Hansen C.H., Du L., Naur P., Olsen C.E., Axelsen K.B., Hick A.J.,
RA Pickett J.A., Halkier B.A.;
RT "CYP83b1 is the oxime-metabolizing enzyme in the glucosinolate pathway in
RT Arabidopsis.";
RL J. Biol. Chem. 276:24790-24796(2001).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=11158532; DOI=10.2307/3871156;
RA Bak S., Tax F.E., Feldmann K.A., Galbraith D.W., Feyereisen R.;
RT "CYP83B1, a cytochrome P450 at the metabolic branch point in auxin and
RT indole glucosinolate biosynthesis in Arabidopsis.";
RL Plant Cell 13:101-111(2001).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=11553739; DOI=10.1104/pp.127.1.108;
RA Bak S., Feyereisen R.;
RT "The involvement of two p450 enzymes, CYP83B1 and CYP83A1, in auxin
RT homeostasis and glucosinolate biosynthesis.";
RL Plant Physiol. 127:108-118(2001).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11805067; DOI=10.1093/genetics/160.1.323;
RA Smolen G., Bender J.;
RT "Arabidopsis cytochrome P450 cyp83B1 mutations activate the tryptophan
RT biosynthetic pathway.";
RL Genetics 160:323-332(2002).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12970475; DOI=10.1104/pp.102.019240;
RA Naur P., Petersen B.L., Mikkelsen M.D., Bak S., Rasmussen H., Olsen C.E.,
RA Halkier B.A.;
RT "CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing
RT oximes in the biosynthesis of glucosinolates in Arabidopsis.";
RL Plant Physiol. 133:63-72(2003).
RN [14]
RP INDUCTION BY CONTINUOUS RED LIGHT, AND DISRUPTION PHENOTYPE.
RX PubMed=14963708; DOI=10.1007/s00425-004-1211-z;
RA Hoecker U., Toledo-Ortiz G., Bender J., Quail P.H.;
RT "The photomorphogenesis-related mutant red1 is defective in CYP83B1, a red
RT light-induced gene encoding a cytochrome P450 required for normal auxin
RT homeostasis.";
RL Planta 219:195-200(2004).
RN [15]
RP INDUCTION BY SPODOPTERA LITTORALIS AND DOF1.1.
RX PubMed=16740150; DOI=10.1111/j.1365-313x.2006.02767.x;
RA Skirycz A., Reichelt M., Burow M., Birkemeyer C., Rolcik J., Kopka J.,
RA Zanor M.I., Gershenzon J., Strnad M., Szopa J., Mueller-Roeber B., Witt I.;
RT "DOF transcription factor AtDof1.1 (OBP2) is part of a regulatory network
RT controlling glucosinolate biosynthesis in Arabidopsis.";
RL Plant J. 47:10-24(2006).
RN [16]
RP FUNCTION.
RX PubMed=26361733; DOI=10.1111/tpj.13023;
RA Clausen M., Kannangara R.M., Olsen C.E., Blomstedt C.K., Gleadow R.M.,
RA Joergensen K., Bak S., Motawie M.S., Moeller B.L.;
RT "The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic
RT pathways.";
RL Plant J. 84:558-573(2015).
CC -!- FUNCTION: Involved in the metabolism of aromatic oximes. Catalyzes the
CC oxime metabolizing step in indole glucosinolate biosynthesis by
CC converting indole-3-acetaldoxime into indole-3-S-alkyl-thiohydroximate.
CC Probably required for glucosinolate activation in response to
CC pathogens. Functions in auxin homeostasis because indole-3-acetaldoxime
CC also serves as a precursor for auxin biosynthesis. Specifically
CC metabolizes (E)-p-hydroxyphenylacetaldoxime into an S-alkyl-
CC thiohydroximate (PubMed:26361733). {ECO:0000269|PubMed:11114200,
CC ECO:0000269|PubMed:11158532, ECO:0000269|PubMed:11333274,
CC ECO:0000269|PubMed:11553739, ECO:0000269|PubMed:11805067,
CC ECO:0000269|PubMed:12970475, ECO:0000269|PubMed:26361733}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-(indol-3-yl)acetaldehyde oxime + glutathione + O2 +
CC reduced [NADPH--hemoprotein reductase] = (E)-1-(glutathione-S-yl)-2-
CC (1H-indol-3-yl)acetohydroximate + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:52180, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17545, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58210, ChEBI:CHEBI:136444;
CC EC=1.14.14.45; Evidence={ECO:0000269|PubMed:12970475};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-phenylacetaldehyde oxime + glutathione + O2 + reduced
CC [NADPH--hemoprotein reductase] = (Z)-1-(glutathione-S-yl)-2-
CC phenylacetohydroximate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:52192, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:47793, ChEBI:CHEBI:57618, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:136447; EC=1.14.14.45;
CC Evidence={ECO:0000269|PubMed:12970475};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 uM for indole-3-acetaldoxime {ECO:0000269|PubMed:11158532,
CC ECO:0000269|PubMed:11553739, ECO:0000269|PubMed:12970475};
CC KM=65 uM for p-hydroxyphenylacetaldoxime
CC {ECO:0000269|PubMed:12970475};
CC KM=188 uM for phenylacetaldoxime {ECO:0000269|PubMed:12970475};
CC Note=kcat is 52 min(-1) with indole-3-acetaldoxime as substrate. kcat
CC is 14 min(-1) with p-hydroxyphenylacetaldoxime as substrate. kcat is
CC 47 min(-1) with phenylacetaldoxime as substrate.
CC {ECO:0000269|PubMed:12970475};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By auxin and continuous red light. Stimulated by DOF1.1 and,
CC transiently, by the generalist herbivore S.littoralis
CC (PubMed:16740150). {ECO:0000269|PubMed:11114200,
CC ECO:0000269|PubMed:14963708, ECO:0000269|PubMed:16740150}.
CC -!- DISRUPTION PHENOTYPE: Runt phenotype (small plants with hooked leaves).
CC Epinastic leaves and defect in root development. High levels of
CC endogenous free auxin. Altered tryptophan genes regulation.
CC {ECO:0000269|PubMed:11158532, ECO:0000269|PubMed:11553739,
CC ECO:0000269|PubMed:11805067, ECO:0000269|PubMed:14963708,
CC ECO:0000269|PubMed:9675903, ECO:0000269|PubMed:9808718}.
CC -!- MISCELLANEOUS: The sur2 mutant phenotype can be complemented by
CC exogenous auxin or low pH medium. Plants overexpresseing SUR2 show
CC decreased apical dominance.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; D78598; BAA28531.1; -; mRNA.
DR EMBL; AL080283; CAB45909.1; -; Genomic_DNA.
DR EMBL; AL161579; CAB79868.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85921.1; -; Genomic_DNA.
DR EMBL; BT002333; AAN86166.1; -; mRNA.
DR EMBL; AY085195; AAM61746.1; -; mRNA.
DR PIR; T10680; T10680.
DR RefSeq; NP_194878.1; NM_119299.3.
DR AlphaFoldDB; O65782; -.
DR SMR; O65782; -.
DR BioGRID; 14563; 3.
DR STRING; 3702.AT4G31500.1; -.
DR PaxDb; O65782; -.
DR PRIDE; O65782; -.
DR ProteomicsDB; 240237; -.
DR EnsemblPlants; AT4G31500.1; AT4G31500.1; AT4G31500.
DR GeneID; 829277; -.
DR Gramene; AT4G31500.1; AT4G31500.1; AT4G31500.
DR KEGG; ath:AT4G31500; -.
DR Araport; AT4G31500; -.
DR TAIR; locus:2125264; AT4G31500.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_1_1; -.
DR InParanoid; O65782; -.
DR OMA; MHLGIAM; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; O65782; -.
DR BioCyc; ARA:AT4G31500-MON; -.
DR BioCyc; MetaCyc:AT4G31500-MON; -.
DR BRENDA; 1.14.14.43; 399.
DR BRENDA; 1.14.14.45; 399.
DR SABIO-RK; O65782; -.
DR PRO; PR:O65782; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65782; baseline and differential.
DR Genevisible; O65782; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:TAIR.
DR GO; GO:0048830; P:adventitious root development; TAS:TAIR.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0009759; P:indole glucosinolate biosynthetic process; IDA:TAIR.
DR GO; GO:0009684; P:indoleacetic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009682; P:induced systemic resistance; IEP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009625; P:response to insect; IEP:UniProtKB.
DR GO; GO:0010114; P:response to red light; IMP:TAIR.
DR GO; GO:0009641; P:shade avoidance; IMP:TAIR.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP:TAIR.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Growth regulation; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..499
FT /note="Cytochrome P450 83B1"
FT /id="PRO_0000052167"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 441
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q96242"
SQ SEQUENCE 499 AA; 56846 MW; CCA2D733E7D00D7B CRC64;
MDLLLIIAGL VAAAAFFFLR STTKKSLRLP PGPKGLPIIG NLHQMEKFNP QHFLFRLSKL
YGPIFTMKIG GRRLAVISSA ELAKELLKTQ DLNFTARPLL KGQQTMSYQG RELGFGQYTA
YYREMRKMCM VNLFSPNRVA SFRPVREEEC QRMMDKIYKA ADQSGTVDLS ELLLSFTNCV
VCRQAFGKRY NEYGTEMKRF IDILYETQAL LGTLFFSDLF PYFGFLDNLT GLSARLKKAF
KELDTYLQEL LDETLDPNRP KQETESFIDL LMQIYKDQPF SIKFTHENVK AMILDIVVPG
TDTAAAVVVW AMTYLIKYPE AMKKAQDEVR SVIGDKGYVS EEDIPNLPYL KAVIKESLRL
EPVIPILLHR ETIADAKIGG YDIPAKTIIQ VNAWAVSRDT AAWGDNPNEF IPERFMNEHK
GVDFKGQDFE LLPFGSGRRM CPAMHLGIAM VEIPFANLLY KFDWSLPKGI KPEDIKMDVM
TGLAMHKKEH LVLAPTKHI
