RBOHD_ARATH
ID RBOHD_ARATH Reviewed; 921 AA.
AC Q9FIJ0; O81212;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Respiratory burst oxidase homolog protein D {ECO:0000303|PubMed:9628030};
DE EC=1.11.1.-;
DE EC=1.6.3.-;
DE AltName: Full=NADPH oxidase RBOHD {ECO:0000303|PubMed:9628030};
DE Short=AtRBOHD {ECO:0000303|PubMed:9628030};
GN Name=RBOHD {ECO:0000303|PubMed:9628030};
GN OrderedLocusNames=At5g47910 {ECO:0000312|Araport:AT5G47910};
GN ORFNames=MCA23.25 {ECO:0000312|EMBL:BAB11338.1};
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9628030; DOI=10.1046/j.1365-313x.1998.00136.x;
RA Torres M.A., Onouchi H., Hamada S., Machida C., Hammond-Kosack K.E.,
RA Jones J.D.G.;
RT "Six Arabidopsis thaliana homologues of the human respiratory burst oxidase
RT (gp91phox).";
RL Plant J. 14:365-370(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 FUNCTION.
RX PubMed=11756663; DOI=10.1073/pnas.012452499;
RA Torres M.A., Dangl J.L., Jones J.D.G.;
RT "Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for
RT accumulation of reactive oxygen intermediates in the plant defense
RT response.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:517-522(2002).
RN [6]
RP FUNCTION, INDUCTION BY ABSCISIC ACID, AND TISSUE SPECIFICITY.
RX PubMed=12773379; DOI=10.1093/emboj/cdg277;
RA Kwak J.M., Mori I.C., Pei Z.-M., Leonhardt N., Torres M.A., Dangl J.L.,
RA Bloom R.E., Bodde S., Jones J.D.G., Schroeder J.I.;
RT "NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA
RT signaling in Arabidopsis.";
RL EMBO J. 22:2623-2633(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15608336; DOI=10.1105/tpc.104.026971;
RA Davletova S., Rizhsky L., Liang H., Shengqiang Z., Oliver D.J., Coutu J.,
RA Shulaev V., Schlauch K., Mittler R.;
RT "Cytosolic ascorbate peroxidase 1 is a central component of the reactive
RT oxygen gene network of Arabidopsis.";
RL Plant Cell 17:268-281(2005).
RN [8]
RP FUNCTION.
RX PubMed=16913867; DOI=10.1111/j.1365-3040.2006.01555.x;
RA Kalbina I., Strid A.;
RT "The role of NADPH oxidase and MAP kinase phosphatase in UV-B-dependent
RT gene expression in Arabidopsis.";
RL Plant Cell Environ. 29:1783-1793(2006).
RN [9]
RP FUNCTION.
RX PubMed=16428598; DOI=10.1104/pp.105.073072;
RA Song C.J., Steinebrunner I., Wang X., Stout S.C., Roux S.J.;
RT "Extracellular ATP induces the accumulation of superoxide via NADPH
RT oxidases in Arabidopsis.";
RL Plant Physiol. 140:1222-1232(2006).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16760484; DOI=10.1104/pp.106.078089;
RA Sagi M., Fluhr R.;
RT "Production of reactive oxygen species by plant NADPH oxidases.";
RL Plant Physiol. 141:336-340(2006).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, AND INDUCTION.
RX PubMed=17601167; DOI=10.1094/mpmi-20-7-0794;
RA Fagard M., Dellagi A., Roux C., Perino C., Rigault M., Boucher V.,
RA Shevchik V.E., Expert D.;
RT "Arabidopsis thaliana expresses multiple lines of defense to counterattack
RT Erwinia chrysanthemi.";
RL Mol. Plant Microbe Interact. 20:794-805(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-343 AND SER-347, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=17651370; DOI=10.1111/j.1365-313x.2007.03192.x;
RA Nuehse T.S., Bottrill A.R., Jones A.M., Peck S.C.;
RT "Quantitative phosphoproteomic analysis of plasma membrane proteins reveals
RT regulatory mechanisms of plant innate immune responses.";
RL Plant J. 51:931-940(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [15]
RP INTERACTION WITH BIK1 AND FLS2, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PHOSPHORYLATION AT SER-39; SER-343 AND SER-347.
RX PubMed=24629339; DOI=10.1016/j.chom.2014.02.009;
RA Li L., Li M., Yu L., Zhou Z., Liang X., Liu Z., Cai G., Gao L., Zhang X.,
RA Wang Y., Chen S., Zhou J.M.;
RT "The FLS2-associated kinase BIK1 directly phosphorylates the NADPH oxidase
RT RbohD to control plant immunity.";
RL Cell Host Microbe 15:329-338(2014).
RN [16]
RP INTERACTION WITH PBL13.
RX PubMed=26432875; DOI=10.1104/pp.15.01391;
RA Lin Z.J., Liebrand T.W., Yadeta K.A., Coaker G.;
RT "PBL13 is a serine/threonine protein kinase that negatively regulates
RT Arabidopsis immune responses.";
RL Plant Physiol. 169:2950-2962(2015).
RN [17]
RP FUNCTION, INTERACTION WITH SIK1, PTM, AND PHOSPHORYLATION AT SER-8; SER-9;
RP SER-339 AND SER-347.
RC STRAIN=cv. Columbia;
RX PubMed=30212650; DOI=10.1016/j.chom.2018.08.007;
RA Zhang M., Chiang Y.-H., Toruno T.Y., Lee D., Ma M., Liang X., Lal N.K.,
RA Lemos M., Lu Y.-J., Ma S., Liu J., Day B., Dinesh-Kumar S.P., Dehesh K.,
RA Dou D., Zhou J.-M., Coaker G.;
RT "The MAP4 Kinase SIK1 Ensures Robust Extracellular ROS Burst and
RT Antibacterial Immunity in Plants.";
RL Cell Host Microbe 24:379.e5-391.e5(2018).
CC -!- FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide.
CC Involved in the generation of reactive oxygen species (ROS) during
CC incompatible interactions with pathogens, in response to pathogen-
CC associated molecular pattern (PAMP)-triggered immunity (PTI) signaling
CC and in UV-B and abscisic acid ROS-dependent signaling and via SIK1
CC mediated activation by phosphorylation (PubMed:30212650). Might be
CC required for ROS signal amplification during light stress.
CC {ECO:0000269|PubMed:11756663, ECO:0000269|PubMed:12773379,
CC ECO:0000269|PubMed:15608336, ECO:0000269|PubMed:16428598,
CC ECO:0000269|PubMed:16913867, ECO:0000269|PubMed:17601167,
CC ECO:0000269|PubMed:30212650}.
CC -!- ACTIVITY REGULATION: Inhibited by diphenylene iodinium (DPI).
CC {ECO:0000269|PubMed:17601167}.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with BIK1 and
CC FLS2 (PubMed:24629339). Interacts with PBL13 (PubMed:26432875). Binds
CC to SIK1 upon flagellin perception and becomes activated by
CC phosphorylation (PubMed:30212650). {ECO:0000250,
CC ECO:0000269|PubMed:24629339, ECO:0000269|PubMed:26432875,
CC ECO:0000269|PubMed:30212650}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: More abundant in roots than in leaves, stems or
CC inflorescences. Expressed in mesophyll and guard cells.
CC {ECO:0000269|PubMed:12773379, ECO:0000269|PubMed:9628030}.
CC -!- INDUCTION: Up-regulated by pathogen infection and by abscisic acid.
CC {ECO:0000269|PubMed:12773379, ECO:0000269|PubMed:17601167}.
CC -!- PTM: Phosphorylated at Ser-39, Ser-343 and Ser-347 by BIK1 upon
CC flagellin (flg22) treatment (PubMed:24629339). Activated by
CC phosphorylation at Ser-347 mediated by SIK1 and at Ser-8, Ser-9 and
CC Ser-339 upon flagellin (e.g. flg22) perception (PubMed:30212650).
CC {ECO:0000269|PubMed:24629339, ECO:0000269|PubMed:30212650}.
CC -!- DISRUPTION PHENOTYPE: Plants do not accumulate reactive oxygen species
CC during disease-resistance reactions, do not up-regulate UV-B-dependent
CC gene expression and are impaired in abscisic acid-induced stomatal
CC closing and in root growth and seed germination inhibitions.
CC {ECO:0000269|PubMed:15608336}.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family. {ECO:0000305}.
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DR EMBL; AF055357; AAC39479.1; -; mRNA.
DR EMBL; AB016886; BAB11338.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95593.1; -; Genomic_DNA.
DR EMBL; AF424625; AAL11618.1; -; mRNA.
DR EMBL; BT002651; AAO11567.1; -; mRNA.
DR PIR; T51804; T51804.
DR RefSeq; NP_199602.1; NM_124165.3.
DR AlphaFoldDB; Q9FIJ0; -.
DR SMR; Q9FIJ0; -.
DR BioGRID; 20090; 38.
DR IntAct; Q9FIJ0; 34.
DR STRING; 3702.AT5G47910.1; -.
DR PeroxiBase; 3286; AtRboh04.
DR iPTMnet; Q9FIJ0; -.
DR PaxDb; Q9FIJ0; -.
DR PRIDE; Q9FIJ0; -.
DR ProteomicsDB; 225974; -.
DR EnsemblPlants; AT5G47910.1; AT5G47910.1; AT5G47910.
DR GeneID; 834842; -.
DR Gramene; AT5G47910.1; AT5G47910.1; AT5G47910.
DR KEGG; ath:AT5G47910; -.
DR Araport; AT5G47910; -.
DR TAIR; locus:2160917; AT5G47910.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; Q9FIJ0; -.
DR OMA; ARCSAYI; -.
DR OrthoDB; 936110at2759; -.
DR PhylomeDB; Q9FIJ0; -.
DR BioCyc; ARA:AT5G47910-MON; -.
DR BRENDA; 1.6.3.1; 399.
DR PRO; PR:Q9FIJ0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIJ0; baseline and differential.
DR Genevisible; Q9FIJ0; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IMP:TAIR.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0033500; P:carbohydrate homeostasis; IMP:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IGI:TAIR.
DR GO; GO:0007231; P:osmosensory signaling pathway; IMP:TAIR.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR013623; NADPH_Ox.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR Pfam; PF08414; NADPH_Ox; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Calcium; FAD; Flavoprotein; Membrane; Metal-binding; NADP; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Plant defense; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..921
FT /note="Respiratory burst oxidase homolog protein D"
FT /id="PRO_0000313756"
FT TOPO_DOM 1..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..461
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 483..516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..559
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..588
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 589..606
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 607..734
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 756..921
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 253..288
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 297..332
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 415..572
FT /note="Ferric oxidoreductase"
FT DOMAIN 611..732
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..203
FT /note="EF-hand-like 1"
FT /evidence="ECO:0000250"
FT REGION 230..241
FT /note="EF-hand-like 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17651370"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24629339,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30212650"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24629339,
FT ECO:0007744|PubMed:17651370"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24629339,
FT ECO:0000269|PubMed:30212650, ECO:0007744|PubMed:17651370"
SQ SEQUENCE 921 AA; 103909 MW; 1A822569A7AB1817 CRC64;
MKMRRGNSSN DHELGILRGA NSDTNSDTES IASDRGAFSG PLGRPKRASK KNARFADDLP
KRSNSVAGGR GDDDEYVEIT LDIRDDSVAV HSVQQAAGGG GHLEDPELAL LTKKTLESSL
NNTTSLSFFR STSSRIKNAS RELRRVFSRR PSPAVRRFDR TSSAAIHALK GLKFIATKTA
AWPAVDQRFD KLSADSNGLL LSAKFWECLG MNKESKDFAD QLFRALARRN NVSGDAITKE
QLRIFWEQIS DESFDAKLQV FFDMVDKDED GRVTEEEVAE IISLSASANK LSNIQKQAKE
YAALIMEELD PDNAGFIMIE NLEMLLLQAP NQSVRMGDSR ILSQMLSQKL RPAKESNPLV
RWSEKIKYFI LDNWQRLWIM MLWLGICGGL FTYKFIQYKN KAAYGVMGYC VCVAKGGAET
LKFNMALILL PVCRNTITWL RNKTKLGTVV PFDDSLNFHK VIASGIVVGV LLHAGAHLTC
DFPRLIAADE DTYEPMEKYF GDQPTSYWWF VKGVEGWTGI VMVVLMAIAF TLATPWFRRN
KLNLPNFLKK LTGFNAFWYT HHLFIIVYAL LIVHGIKLYL TKIWYQKTTW MYLAVPILLY
ASERLLRAFR SSIKPVKMIK VAVYPGNVLS LHMTKPQGFK YKSGQFMLVN CRAVSPFEWH
PFSITSAPGD DYLSVHIRTL GDWTRKLRTV FSEVCKPPTA GKSGLLRADG GDGNLPFPKV
LIDGPYGAPA QDYKKYDVVL LVGLGIGATP MISILKDIIN NMKGPDRDSD IENNNSNNNS
KGFKTRKAYF YWVTREQGSF EWFKGIMDEI SELDEEGIIE LHNYCTSVYE EGDARVALIA
MLQSLQHAKN GVDVVSGTRV KSHFAKPNWR QVYKKIAVQH PGKRIGVFYC GMPGMIKELK
NLALDFSRKT TTKFDFHKEN F
