DUOX_DROME
ID DUOX_DROME Reviewed; 1537 AA.
AC Q9VQH2; Q6AWK1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Dual oxidase;
DE EC=1.11.1.-;
DE EC=1.6.3.1;
GN Name=Duox; ORFNames=CG3131;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=16272120; DOI=10.1126/science.1117311;
RA Ha E.-M., Oh C.-T., Bae Y.S., Lee W.-J.;
RT "A direct role for dual oxidase in Drosophila gut immunity.";
RL Science 310:847-850(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25639794; DOI=10.1016/j.chom.2014.12.012;
RA Lee K.A., Kim B., Bhin J., Kim D.H., You H., Kim E.K., Kim S.H., Ryu J.H.,
RA Hwang D., Lee W.J.;
RT "Bacterial uracil modulates Drosophila DUOX-dependent gut immunity via
RT Hedgehog-induced signaling endosomes.";
RL Cell Host Microbe 17:191-204(2015).
CC -!- FUNCTION: Plays a role in innate immunity limiting microbial
CC proliferation in the gut (PubMed:16272120, PubMed:25639794). Acts
CC downstream of a hh-signaling pathway to induce the production of
CC reactive oxygen species (ROS) in response to intestinal bacterial
CC infection (PubMed:25639794). May generate antimicrobial oxidative burst
CC through its peroxidase-like domain (PubMed:16272120).
CC {ECO:0000269|PubMed:16272120, ECO:0000269|PubMed:25639794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1;
CC Evidence={ECO:0000269|PubMed:16272120};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC Evidence={ECO:0000269|PubMed:16272120};
CC -!- ACTIVITY REGULATION: Peroxidase activity is inhibited by aminotriazole
CC and azide. {ECO:0000269|PubMed:16272120}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown severely reduces adult
CC survival following the ingestion of E.carotovora.
CC {ECO:0000269|PubMed:25639794}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT94476.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT94476.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF51201.2; -; Genomic_DNA.
DR EMBL; BT015247; AAT94476.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001259968.1; NM_001273039.1.
DR RefSeq; NP_608715.2; NM_134871.3.
DR AlphaFoldDB; Q9VQH2; -.
DR SMR; Q9VQH2; -.
DR BioGRID; 59700; 9.
DR STRING; 7227.FBpp0289611; -.
DR GlyGen; Q9VQH2; 4 sites.
DR PaxDb; Q9VQH2; -.
DR PRIDE; Q9VQH2; -.
DR EnsemblMetazoa; FBtr0300382; FBpp0289611; FBgn0283531.
DR EnsemblMetazoa; FBtr0335133; FBpp0307132; FBgn0283531.
DR GeneID; 33477; -.
DR KEGG; dme:Dmel_CG3131; -.
DR CTD; 565097; -.
DR FlyBase; FBgn0283531; Duox.
DR VEuPathDB; VectorBase:FBgn0283531; -.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000163963; -.
DR HOGENOM; CLU_004482_1_0_1; -.
DR InParanoid; Q9VQH2; -.
DR OMA; KDVFMWR; -.
DR OrthoDB; 27424at2759; -.
DR PhylomeDB; Q9VQH2; -.
DR Reactome; R-DME-209968; Thyroxine biosynthesis.
DR BioGRID-ORCS; 33477; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33477; -.
DR PRO; PR:Q9VQH2; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0283531; Expressed in capitellum (Drosophila) and 17 other tissues.
DR ExpressionAtlas; Q9VQH2; baseline and differential.
DR Genevisible; Q9VQH2; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0043020; C:NADPH oxidase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0106293; F:NADH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0106294; F:NADPH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0004601; F:peroxidase activity; IDA:FlyBase.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR GO; GO:0106292; F:superoxide-generating NADPH oxidase activity; IMP:FlyBase.
DR GO; GO:0008365; P:adult chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0048085; P:adult chitin-containing cuticle pigmentation; IMP:FlyBase.
DR GO; GO:0042335; P:cuticle development; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:FlyBase.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0002385; P:mucosal immune response; IMP:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:FlyBase.
DR GO; GO:0051591; P:response to cAMP; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0009611; P:response to wounding; IMP:FlyBase.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR CDD; cd09820; dual_peroxidase_like; 1.
DR CDD; cd00051; EFh; 3.
DR Gene3D; 1.10.640.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR029595; DUOX1/Duox.
DR InterPro; IPR034821; DUOX_peroxidase.
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; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF175; PTHR11972:SF175; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Calcium; FAD; Flavoprotein; Glycoprotein; Hydrogen peroxide; Membrane;
KW Metal-binding; NADP; Oxidoreductase; Peroxidase; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1537
FT /note="Dual oxidase"
FT /id="PRO_0000223352"
FT TOPO_DOM 1..626
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..1029
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1030..1050
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1051..1065
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1066..1086
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1087..1116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1117..1137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1138..1171
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1172..1192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1193..1202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1203..1223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1224..1230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1231..1251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1252..1537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 855..890
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 891..926
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 936..971
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1078..1218
FT /note="Ferric oxidoreductase"
FT DOMAIN 1253..1358
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..628
FT /note="Peroxidase-like; mediates peroxidase activity"
FT /evidence="ECO:0000250"
FT BINDING 868
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 870
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 872
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 874
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 879
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 904
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 906
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 908
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 915
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 1105
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1537 AA; 177690 MW; E26329E7BFBAB34C CRC64;
MSVPSAPHQR AESKNRVPRP GQKNRKLPKL RLHWPGATYG GALLLLLISY GLELGSVHCY
EKMYSQTEKQ RYDGWYNNLA HPDWGSVDSH LVRKAPPSYS DGVYAMAGAN RPSTRRLSRL
FMRGKDGLGS KFNRTALLAF FGQLVANEIV MASESGCPIE MHRIEIEKCD EMYDRECRGD
KYIPFHRAAY DRDTGQSPNA PREQINQMTA WIDGSFIYST SEAWLNAMRS FHNGTLLTEK
DGKLPVRNTM RVPLFNNPVP SVMKMLSPER LFLLGDPRTN QNPAILSFAI LFLRWHNTLA
QRIKRVHPDW SDEDIYQRAR HTVIASLQNV IVYEYLPAFL GTSLPPYEGY KQDIHPGIGH
IFQAAAFRFG HTMIPPGIYR RDGQCNFKET PMGYPAVRLC STWWDSSGFF ADTSVEEVLM
GLASQISERE DPVLCSDVRD KLFGPMEFTR RDLGALNIMR GRDNGLPDYN TARESYGLKR
HKTWTDINPP LFETQPELLD MLKEAYDNKL DDVDVYVGGM LESYGQPGEF FTAVIKEQFQ
RLRDADRFWF ENERNGIFTP EEIAELRKIT LWDIIVNSTD VKEEEIQKDV FMWRTGDPCP
QPMQLNATEL EPCTYLEGYD YFSGSELMFI YVCVFLGFVP ILCAGAGYCV VKLQNSKRRR
LKIRQEALRA PQHKGSVDKM LAREWLHANH KRLVTVKFGP EAAIYTVDRK GEKLRTFSLK
HIDVVSVEES ATNHIKKKPY ILLRVPSDHD LVLELESYGA RRKFVKKLED FLLLHKKEMT
LMEVNRDIML ARAETRERRQ KRLEYFFREA YALTFGLRPG ERRRRSDASS DGEVMTVMRT
SLSKAEFAAA LGMKPNDMFV RKMFNIVDKD QDGRISFQEF LETVVLFSRG KTDDKLRIIF
DMCDNDRNGV IDKGELSEMM RSLVEIARTT SLGDDQVTEL IDGMFQDVGL EHKNHLTYQD
FKLMMKEYKG DFVAIGLDCK GAKQNFLDTS TNVARMTSFN IEPMQDKPRH WLLAKWDAYI
TFLEENRQNI FYLFLFYVVT IVLFVERFIH YSFMAEHTDL RHIMGVGIAI TRGSAASLSF
CYSLLLLTMS RNLITKLKEF PIQQYIPLDS HIQFHKIAAC TALFFSVLHT VGHIVNFYHV
STQSHENLRC LTREVHFASD YKPDITFWLF QTVTGTTGVM LFIIMCIIFV FAHPTIRKKA
YNFFWNMHTL YIGLYLLSLI HGLARLTGPP RFWMFFLGPG IVYTLDKIVS LRTKYMALDV
IDTDLLPSDV IKIKFYRPPN LKYLSGQWVR LSCTAFRPHE MHSFTLTSAP HENFLSCHIK
AQGPWTWKLR NYFDPCNYNP EDQPKIRIEG PFGGGNQDWY KFEVAVMVGG GIGVTPYASI
LNDLVFGTST NRYSGVACKK VYFLWICPSH KHFEWFIDVL RDVEKKDVTN VLEIHIFITQ
FFHKFDLRTT MLYICENHFQ RLSKTSIFTG LKAVNHFGRP DMSSFLKFVQ KKHSYVSKIG
VFSCGPRPLT KSVMSACDEV NKTRKLPYFI HHFENFG
