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 27-MAR-2024, entry version 159. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q9FIJ0; -. DR PeroxiBase; 3286; AtRboh04. DR iPTMnet; Q9FIJ0; -. DR PaxDb; 3702-AT5G47910-1; -. 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; AT5G47910; RBOHD. DR eggNOG; KOG0039; Eukaryota. DR HOGENOM; CLU_005646_6_0_1; -. DR InParanoid; Q9FIJ0; -. DR OMA; ARCSAYI; -. DR OrthoDB; 367877at2759; -. DR PhylomeDB; Q9FIJ0; -. DR BioCyc; ARA:AT5G47910-MONOMER; -. DR BRENDA; 1.6.3.1; 399. DR PRO; PR:Q9FIJ0; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9FIJ0; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR. 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: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 CDD; cd06186; NOX_Duox_like_FAD_NADP; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 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 PANTHER; PTHR11972; NADPH OXIDASE; 1. DR PANTHER; PTHR11972:SF152; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN D; 1. 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 SFLD; SFLDS00052; Ferric_Reductase_Domain; 1. DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1. DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; 2. DR PROSITE; PS51384; FAD_FR; 1. DR Genevisible; Q9FIJ0; AT. 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 //