TOLL_DROME
ID TOLL_DROME Reviewed; 1097 AA.
AC P08953; A4V3G7; A8WHK7; Q8MRF3; Q9VBB8;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Protein toll;
DE Flags: Precursor;
GN Name=Tl {ECO:0000312|FlyBase:FBgn0262473};
GN ORFNames=CG5490 {ECO:0000312|FlyBase:FBgn0262473};
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 [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=2449285; DOI=10.1016/0092-8674(88)90516-8;
RA Hashimoto C., Hudson K.L., Anderson K.V.;
RT "The Toll gene of Drosophila, required for dorsal-ventral embryonic
RT polarity, appears to encode a transmembrane protein.";
RL Cell 52:269-279(1988).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-1097, AND VARIANTS.
RC STRAIN=MelZim1, MelZim3, MelZim4, MelZim5, MelZim6, MelZim7, and MelZim8;
RX PubMed=12930753; DOI=10.1093/genetics/164.4.1471;
RA Schlenke T.A., Begun D.J.;
RT "Natural selection drives Drosophila immune system evolution.";
RL Genetics 164:1471-1480(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-1097.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP FUNCTION.
RX PubMed=3931919; DOI=10.1016/0092-8674(85)90275-2;
RA Anderson K.V., Bokla L., Nusslein-Volhard C.;
RT "Establishment of dorsal-ventral polarity in the Drosophila embryo: the
RT induction of polarity by the Toll gene product.";
RL Cell 42:791-798(1985).
RN [8]
RP FUNCTION.
RX PubMed=2124970; DOI=10.1002/j.1460-2075.1990.tb07878.x;
RA Keith F.J., Gay N.J.;
RT "The Drosophila membrane receptor Toll can function to promote cellular
RT adhesion.";
RL EMBO J. 9:4299-4306(1990).
RN [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=1879347; DOI=10.1242/dev.111.4.1021;
RA Hashimoto C., Gerttula S., Anderson K.V.;
RT "Plasma membrane localization of the Toll protein in the syncytial
RT Drosophila embryo: importance of transmembrane signaling for dorsal-ventral
RT pattern formation.";
RL Development 111:1021-1028(1991).
RN [10]
RP FUNCTION.
RX PubMed=8808632; DOI=10.1016/s0092-8674(00)80172-5;
RA Lemaitre B., Nicolas E., Michaut L., Reichhart J.-M., Hoffmann J.A.;
RT "The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the
RT potent antifungal response in Drosophila adults.";
RL Cell 86:973-983(1996).
RN [11]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10973475; DOI=10.1073/pnas.180130797;
RA Tauszig S., Jouanguy E., Hoffmann J.A., Imler J.L.;
RT "Toll-related receptors and the control of antimicrobial peptide expression
RT in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10520-10525(2000).
RN [12]
RP DEVELOPMENTAL STAGE.
RX PubMed=12617819; DOI=10.1016/s1567-133x(02)00020-0;
RA Kambris Z., Hoffmann J.A., Imler J.L., Capovilla M.;
RT "Tissue and stage-specific expression of the Tolls in Drosophila embryos.";
RL Gene Expr. Patterns 2:311-317(2002).
RN [13]
RP FUNCTION.
RX PubMed=12872120; DOI=10.1038/ni955;
RA Weber A.N., Tauszig-Delamasure S., Hoffmann J.A., Lelievre E., Gascan H.,
RA Ray K.P., Morse M.A., Imler J.L., Gay N.J.;
RT "Binding of the Drosophila cytokine Spatzle to Toll is direct and
RT establishes signaling.";
RL Nat. Immunol. 4:794-800(2003).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=15373972; DOI=10.1179/096805104225004897;
RA Bettencourt R., Tanji T., Yagi Y., Ip Y.T.;
RT "Toll and Toll-9 in Drosophila innate immune response.";
RL J. Endotoxin Res. 10:261-268(2004).
RN [15]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=19018662; DOI=10.1371/journal.pbio.0060284;
RA Zhu B., Pennack J.A., McQuilton P., Forero M.G., Mizuguchi K.,
RA Sutcliffe B., Gu C.-J., Fenton J.C., Hidalgo A.;
RT "Drosophila neurotrophins reveal a common mechanism for nervous system
RT formation.";
RL PLoS Biol. 6:E284-E284(2008).
RN [16]
RP INDUCTION BY VIRAL INFECTION.
RX PubMed=22464169; DOI=10.1016/j.immuni.2012.03.003;
RA Nakamoto M., Moy R.H., Xu J., Bambina S., Yasunaga A., Shelly S.S.,
RA Gold B., Cherry S.;
RT "Virus recognition by Toll-7 activates antiviral autophagy in Drosophila.";
RL Immunity 36:658-667(2012).
RN [17]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20504957; DOI=10.1242/dev.046672;
RA Inaki M., Shinza-Kameda M., Ismat A., Frasch M., Nose A.;
RT "Drosophila Tey represses transcription of the repulsive cue Toll and
RT generates neuromuscular target specificity.";
RL Development 137:2139-2146(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 28-228, AND GLYCOSYLATION AT
RP ASN-80 AND ASN-140.
RX PubMed=23596340; DOI=10.1107/s0021889812051606;
RA Gangloff M., Moreno A., Gay N.J.;
RT "Liesegang-like patterns of Toll crystals grown in gel.";
RL J. Appl. Crystallogr. 46:337-345(2013).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 28-397 IN COMPLEX WITH SPZ,
RP SUBUNIT, AND GLYCOSYLATION AT ASN-80; ASN-140; ASN-270; ASN-346 AND
RP ASN-391.
RX PubMed=24282309; DOI=10.1073/pnas.1317002110;
RA Lewis M., Arnot C.J., Beeston H., McCoy A., Ashcroft A.E., Gay N.J.,
RA Gangloff M.;
RT "Cytokine Spatzle binds to the Drosophila immunoreceptor Toll with a
RT neurotrophin-like specificity and couples receptor activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20461-20466(2013).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 28-228, MUTAGENESIS OF ARG-154;
RP LYS-208 AND ARG-432, AND GLYCOSYLATION AT ASN-80; ASN-140 AND ASN-175.
RX PubMed=23245851; DOI=10.1016/j.str.2012.11.003;
RA Gangloff M., Arnot C.J., Lewis M., Gay N.J.;
RT "Functional insights from the crystal structure of the N-terminal domain of
RT the prototypical toll receptor.";
RL Structure 21:143-153(2013).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 28-802 IN COMPLEX WITH SPZ,
RP SUBUNIT, AND GLYCOSYLATION AT ASN-80; ASN-140; ASN-175; ASN-235; ASN-270;
RP ASN-346; ASN-391; ASN-482; ASN-508; ASN-528; ASN-654; ASN-703 AND ASN-715.
RX PubMed=24733933; DOI=10.1073/pnas.1320678111;
RA Parthier C., Stelter M., Ursel C., Fandrich U., Lilie H., Breithaupt C.,
RA Stubbs M.T.;
RT "Structure of the Toll-Spatzle complex, a molecular hub in Drosophila
RT development and innate immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6281-6286(2014).
CC -!- FUNCTION: Receptor for the cleaved activated form of spz, spaetzle C-
CC 106 (PubMed:12872120). Binding to spaetzle C-106 activates the Toll
CC signaling pathway and induces expression of the antifungal peptide
CC drosomycin (PubMed:12872120, PubMed:8808632, PubMed:10973475).
CC Component of the extracellular signaling pathway that establishes
CC dorsal-ventral polarity in the embryo (PubMed:3931919). Promotes
CC heterophilic cellular adhesion (PubMed:2124970). Involved in synaptic
CC targeting of motoneurons RP5 and V to muscle 12 (M12); functions as a
CC repulsive cue inhibiting motoneuron synapse formation on muscle 13
CC (M13) to guide RP5 and V to the neighboring M12, where its expression
CC is repressed by tey (PubMed:20504957). May also function in embryonic
CC neuronal survival and the synaptic targeting of SNa motoneurons
CC (PubMed:19018662). {ECO:0000269|PubMed:10973475,
CC ECO:0000269|PubMed:12872120, ECO:0000269|PubMed:19018662,
CC ECO:0000269|PubMed:20504957, ECO:0000269|PubMed:2124970,
CC ECO:0000269|PubMed:3931919, ECO:0000269|PubMed:8808632}.
CC -!- SUBUNIT: In the absence of ligand, forms a low-affinity disulfide-
CC linked homodimer (PubMed:24733933). In the presence of ligand, crystal
CC structures show one Tl molecule bound to a spaetzle C-106 homodimer
CC (PubMed:24282309, PubMed:24733933). However, the active complex
CC probably consists of two Tl molecules bound to a spaetzle C-106
CC homodimer (PubMed:24282309, PubMed:24733933). This is supported by in
CC vitro experiments which also show binding of the spaetzle C-106 dimer
CC to 2 Tl receptors (PubMed:12872120). Ligand binding induces
CC conformational changes in the extracellular domain of Tl
CC (PubMed:24282309). This may enable a secondary homodimerization
CC interface at the C-terminus of the Tl extracellular domain
CC (PubMed:24282309). {ECO:0000269|PubMed:12872120,
CC ECO:0000269|PubMed:24282309, ECO:0000269|PubMed:24733933,
CC ECO:0000303|PubMed:24282309}.
CC -!- INTERACTION:
CC P08953; Q7K105: Myd88; NbExp=3; IntAct=EBI-143610, EBI-129988;
CC P08953; P08953: Tl; NbExp=2; IntAct=EBI-143610, EBI-143610;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15373972,
CC ECO:0000269|PubMed:1879347}; Single-pass type I membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15373972}. Note=In the fat
CC body, detected in puntate structures along the cell periphery. Becomes
CC evenly distributed in the cytoplasm 1 hour after bacterial infection.
CC {ECO:0000269|PubMed:15373972}.
CC -!- TISSUE SPECIFICITY: In early embryos, concentrated in the
CC pseudocleavage furrows that form transiently between nuclei before
CC cellularization and in the cleavage furrows during cellularization (at
CC protein level) (PubMed:1879347). Later, found on cells in the
CC mesectoderm, stomodeum, proctodeum, anterior and posterior midguts,
CC splanchnopleura, salivary gland placode and adjacent to the segmentally
CC repeated tracheal placodes (at protein level) (PubMed:1879347). During
CC and after germ band shortening, localized in a number of cell types,
CC including the salivary gland, foregut, hindgut, Malpighian tubules and
CC epidermis (at protein level) (PubMed:1879347). In embryos, high
CC expression in M13 with comparatively low expression in M12
CC (PubMed:20504957). {ECO:0000269|PubMed:1879347,
CC ECO:0000269|PubMed:20504957}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC (PubMed:2449285, PubMed:1879347, PubMed:12617819). Maternal Tl
CC increases in syncytial embryos, reaching a peak at the syncytial
CC blastoderm stage and then decreases and is almost undetectable by the
CC time of ventral furrow formation at gastrulation (at protein level)
CC (PubMed:1879347). Expressed throughout development, with highest levels
CC of expression in the embryo (PubMed:10973475). Expressed in all
CC embryonic central nervous system axons (PubMed:19018662). In larvae,
CC detected in the blood cells and fat body (PubMed:12617819).
CC {ECO:0000269|PubMed:10973475, ECO:0000269|PubMed:12617819,
CC ECO:0000269|PubMed:1879347, ECO:0000269|PubMed:19018662,
CC ECO:0000269|PubMed:2449285}.
CC -!- INDUCTION: Up-regulated during vesicular stomatitis virus (VSV)
CC infection. {ECO:0000269|PubMed:22464169}.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
CC -!- CAUTION: In some plant proteins and in human SARM1, the TIR domain has
CC NAD(+) hydrolase (NADase) activity (By similarity). However, despite
CC the presence of the catalytic Asp residue, the isolated TIR domain of
CC human TLR4 lacks NADase activity (By similarity). Based on this, it is
CC unlikely that Toll-like receptors have NADase activity.
CC {ECO:0000250|UniProtKB:O00206, ECO:0000305}.
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DR EMBL; M19969; AAA28941.1; -; mRNA.
DR EMBL; AE014297; AAF56624.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14086.1; -; Genomic_DNA.
DR EMBL; BT031153; ABX00775.1; -; mRNA.
DR EMBL; AY349649; AAQ64932.1; -; Genomic_DNA.
DR EMBL; AY349650; AAQ64933.1; -; Genomic_DNA.
DR EMBL; AY349651; AAQ64934.1; -; Genomic_DNA.
DR EMBL; AY349652; AAQ64935.1; -; Genomic_DNA.
DR EMBL; AY349653; AAQ64936.1; -; Genomic_DNA.
DR EMBL; AY349654; AAQ64937.1; -; Genomic_DNA.
DR EMBL; AY349655; AAQ64938.1; -; Genomic_DNA.
DR EMBL; AY121616; AAM51943.1; -; mRNA.
DR PIR; A29943; A29943.
DR RefSeq; NP_524518.1; NM_079794.3.
DR RefSeq; NP_733166.1; NM_170287.3.
DR PDB; 4ARN; X-ray; 2.41 A; A/B/C/D=28-228.
DR PDB; 4ARR; X-ray; 3.00 A; A/B=28-228.
DR PDB; 4BV4; X-ray; 2.35 A; R=28-397.
DR PDB; 4LXR; X-ray; 2.20 A; A=28-802.
DR PDB; 4LXS; X-ray; 3.30 A; A=28-802.
DR PDBsum; 4ARN; -.
DR PDBsum; 4ARR; -.
DR PDBsum; 4BV4; -.
DR PDBsum; 4LXR; -.
DR PDBsum; 4LXS; -.
DR AlphaFoldDB; P08953; -.
DR SMR; P08953; -.
DR BioGRID; 68116; 34.
DR DIP; DIP-34358N; -.
DR IntAct; P08953; 4.
DR MINT; P08953; -.
DR STRING; 7227.FBpp0084431; -.
DR GlyGen; P08953; 17 sites.
DR iPTMnet; P08953; -.
DR PaxDb; P08953; -.
DR EnsemblMetazoa; FBtr0085059; FBpp0084431; FBgn0262473.
DR EnsemblMetazoa; FBtr0330155; FBpp0303188; FBgn0262473.
DR GeneID; 43222; -.
DR KEGG; dme:Dmel_CG5490; -.
DR CTD; 109651; -.
DR FlyBase; FBgn0262473; Tl.
DR VEuPathDB; VectorBase:FBgn0262473; -.
DR eggNOG; KOG4641; Eukaryota.
DR HOGENOM; CLU_009970_0_0_1; -.
DR InParanoid; P08953; -.
DR OMA; EYELNCP; -.
DR OrthoDB; 303561at2759; -.
DR PhylomeDB; P08953; -.
DR Reactome; R-DME-168142; Toll Like Receptor 10 (TLR10) Cascade.
DR Reactome; R-DME-209442; Formation of the trans-membrane 'signalling complex'.
DR Reactome; R-DME-214842; DL and DIF homodimers bind to TUB and phosphorylated PLL in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214844; DL and DIF homodimers complexed with CACT are all phosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214862; Activated PLL kinase is autophosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214863; Adaptor protein complex binds to TL receptor at the plasma membrane.
DR Reactome; R-DME-214869; Phosphorylated CACT, DL and DIF homodimers dissociate from the TL receptor 'signalling complex'.
DR Reactome; R-DME-214874; PLL kinase binds to TUB in the TL receptor 'signalling complex'.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; P08953; -.
DR BioGRID-ORCS; 43222; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Tl; fly.
DR GenomeRNAi; 43222; -.
DR PRO; PR:P08953; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0262473; Expressed in cleaving embryo and 30 other tissues.
DR ExpressionAtlas; P08953; baseline and differential.
DR Genevisible; P08953; DM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:FlyBase.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019955; F:cytokine binding; IPI:FlyBase.
DR GO; GO:0004896; F:cytokine receptor activity; IMP:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0070976; F:TIR domain binding; IPI:FlyBase.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:FlyBase.
DR GO; GO:0046790; F:virion binding; IDA:FlyBase.
DR GO; GO:0061760; P:antifungal innate immune response; IDA:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:FlyBase.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:FlyBase.
DR GO; GO:0009597; P:detection of virus; IDA:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IDA:FlyBase.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:FlyBase.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0002804; P:positive regulation of antifungal peptide production; IDA:FlyBase.
DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IMP:FlyBase.
DR GO; GO:0035208; P:positive regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:1902875; P:regulation of embryonic pattern specification; IMP:UniProtKB.
DR GO; GO:0002347; P:response to tumor cell; IMP:FlyBase.
DR GO; GO:0009611; P:response to wounding; IDA:FlyBase.
DR GO; GO:0007416; P:synapse assembly; IMP:FlyBase.
DR GO; GO:0016201; P:synaptic target inhibition; IMP:FlyBase.
DR GO; GO:0008063; P:Toll signaling pathway; IDA:FlyBase.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:InterPro.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01462; LRRNT; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00082; LRRCT; 2.
DR SMART; SM00013; LRRNT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 13.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Cytoplasm;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Leucine-rich repeat; Membrane; NAD; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1097
FT /note="Protein toll"
FT /id="PRO_0000034740"
FT TOPO_DOM 28..807
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 808..828
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 829..1097
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 175..195
FT /note="LRR 1"
FT REPEAT 198..219
FT /note="LRR 2"
FT REPEAT 222..243
FT /note="LRR 3"
FT REPEAT 246..267
FT /note="LRR 4"
FT REPEAT 270..291
FT /note="LRR 5"
FT REPEAT 294..314
FT /note="LRR 6"
FT REPEAT 320..340
FT /note="LRR 7"
FT REPEAT 343..364
FT /note="LRR 8"
FT REPEAT 367..388
FT /note="LRR 9"
FT REPEAT 391..412
FT /note="LRR 10"
FT REPEAT 415..436
FT /note="LRR 11"
FT REPEAT 439..460
FT /note="LRR 12"
FT REPEAT 474..495
FT /note="LRR 13"
FT REPEAT 498..521
FT /note="LRR 14"
FT REPEAT 523..544
FT /note="LRR 15"
FT DOMAIN 561..620
FT /note="LRRCT 1"
FT DOMAIN 622..663
FT /note="LRRNT"
FT REPEAT 669..690
FT /note="LRR 16"
FT REPEAT 693..713
FT /note="LRR 17"
FT REPEAT 715..738
FT /note="LRR 18"
FT DOMAIN 751..801
FT /note="LRRCT 2"
FT DOMAIN 857..993
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23245851,
FT ECO:0000269|PubMed:23596340, ECO:0000269|PubMed:24282309,
FT ECO:0000269|PubMed:24733933, ECO:0007744|PDB:4ARN,
FT ECO:0007744|PDB:4ARR, ECO:0007744|PDB:4BV4,
FT ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23245851,
FT ECO:0000269|PubMed:23596340, ECO:0000269|PubMed:24282309,
FT ECO:0000269|PubMed:24733933, ECO:0007744|PDB:4ARN,
FT ECO:0007744|PDB:4ARR, ECO:0007744|PDB:4BV4,
FT ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23245851,
FT ECO:0000269|PubMed:24733933, ECO:0007744|PDB:4ARN,
FT ECO:0007744|PDB:4LXS"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24733933,
FT ECO:0007744|PDB:4LXS"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24282309,
FT ECO:0000269|PubMed:24733933, ECO:0007744|PDB:4BV4,
FT ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24282309,
FT ECO:0000269|PubMed:24733933, ECO:0007744|PDB:4BV4,
FT ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24282309,
FT ECO:0000269|PubMed:24733933, ECO:0007744|PDB:4BV4,
FT ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24733933,
FT ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24733933,
FT ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24733933,
FT ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24733933,
FT ECO:0007744|PDB:4LXS"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24733933,
FT ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24733933,
FT ECO:0007744|PDB:4LXR"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..45
FT /evidence="ECO:0007744|PDB:4ARN, ECO:0007744|PDB:4ARR,
FT ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT DISULFID 43..56
FT /evidence="ECO:0007744|PDB:4ARN, ECO:0007744|PDB:4ARR,
FT ECO:0007744|PDB:4BV4, ECO:0007744|PDB:4LXR,
FT ECO:0007744|PDB:4LXS"
FT DISULFID 79..107
FT /evidence="ECO:0007744|PDB:4ARN, ECO:0007744|PDB:4ARR,
FT ECO:0007744|PDB:4BV4, ECO:0007744|PDB:4LXR,
FT ECO:0007744|PDB:4LXS"
FT DISULFID 565..597
FT /evidence="ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT DISULFID 567..618
FT /evidence="ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT DISULFID 631..637
FT /evidence="ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT DISULFID 635..650
FT /evidence="ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT DISULFID 755..781
FT /evidence="ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT DISULFID 757..799
FT /evidence="ECO:0007744|PDB:4LXR, ECO:0007744|PDB:4LXS"
FT VARIANT 98
FT /note="E -> G (in strain: MelZim6)"
FT VARIANT 218
FT /note="G -> S (in strain: MelZim7)"
FT VARIANT 245
FT /note="T -> S (in strain: MelZim3)"
FT VARIANT 390
FT /note="T -> I (in strain: MelZim3 and MelZim7)"
FT VARIANT 414
FT /note="G -> A (in strain: MelZim3)"
FT VARIANT 435
FT /note="V -> L (in strain: MelZim8)"
FT VARIANT 460
FT /note="M -> T (in strain: MelZim6)"
FT VARIANT 471
FT /note="Y -> D (in strain: MelZim1, MelZim4, MelZim5 and
FT MelZim6)"
FT VARIANT 486
FT /note="I -> R (in strain: MelZim6)"
FT VARIANT 513
FT /note="G -> R (in strain: MelZim1, MelZim5 and MelZim6)"
FT VARIANT 538
FT /note="A -> E (in strain: MelZim1, MelZim5 and MelZim6)"
FT VARIANT 544
FT /note="H -> Y (in strain: MelZim1, MelZim5 and MelZim6)"
FT VARIANT 568
FT /note="T -> M (in strain: MelZim1, MelZim5 and MelZim6)"
FT VARIANT 592
FT /note="T -> A (in strain: MelZim6)"
FT VARIANT 603
FT /note="L -> M (in strain: MelZim1, MelZim5 and MelZim6)"
FT VARIANT 681
FT /note="L -> V (in strain: MelZim1, MelZim3, MelZim4,
FT MelZim5, MelZim6 and MelZim7)"
FT VARIANT 714
FT /note="T -> I (in strain: MelZim5 and MelZim8)"
FT VARIANT 732
FT /note="T -> S (in strain: MelZim8)"
FT VARIANT 741
FT /note="M -> I (in strain: MelZim1)"
FT MUTAGEN 154
FT /note="R->A: No change in signaling capacity."
FT /evidence="ECO:0000269|PubMed:23245851"
FT MUTAGEN 208
FT /note="K->E: 25% decrease in signaling capacity."
FT /evidence="ECO:0000269|PubMed:23245851"
FT MUTAGEN 432
FT /note="R->A: 33% decrease in signaling capacity."
FT /evidence="ECO:0000269|PubMed:23245851"
FT CONFLICT 355
FT /note="K -> S (in Ref. 5; AAQ64932/AAQ64933/AAQ64934/
FT AAQ64935/AAQ64936/AAQ64937/AAQ64938)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="V -> A (in Ref. 5; AAQ64933/AAQ64934/AAQ64937/
FT AAQ64938)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="M -> I (in Ref. 4; ABX00775)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="A -> T (in Ref. 4; ABX00775)"
FT /evidence="ECO:0000305"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4ARN"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4ARR"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 167..172
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 262..267
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 286..291
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 335..340
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 359..364
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 383..386
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 431..434
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 456..460
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 468..471
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 490..494
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:4LXS"
FT HELIX 514..517
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:4LXS"
FT STRAND 554..557
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 570..576
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 596..600
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 601..605
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 608..610
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 636..640
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 641..644
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 691..693
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 718..720
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:4LXS"
FT HELIX 731..737
FT /evidence="ECO:0007829|PDB:4LXR"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 757..759
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 760..767
FT /evidence="ECO:0007829|PDB:4LXR"
FT TURN 770..772
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 790..792
FT /evidence="ECO:0007829|PDB:4LXR"
FT HELIX 795..798
FT /evidence="ECO:0007829|PDB:4LXR"
SQ SEQUENCE 1097 AA; 124656 MW; D1BFC42245E3EABE CRC64;
MSRLKAASEL ALLVIILQLL QWPGSEASFG RDACSEMSID GLCQCAPIMS EYEIICPANA
ENPTFRLTIQ PKDYVQIMCN LTDTTDYQQL PKKLRIGEVD RVQMRRCMLP GHTPIASILD
YLGIVSPTTL IFESDNLGMN ITRQHLDRLH GLKRFRFTTR RLTHIPANLL TDMRNLSHLE
LRANIEEMPS HLFDDLENLE SIEFGSNKLR QMPRGIFGKM PKLKQLNLWS NQLHNLTKHD
FEGATSVLGI DIHDNGIEQL PHDVFAHLTN VTDINLSANL FRSLPQGLFD HNKHLNEVRL
MNNRVPLATL PSRLFANQPE LQILRLRAEL QSLPGDLFEH STQITNISLG DNLLKTLPAT
LLEHQVNLLS LDLSNNRLTH LPDSLFAHTT NLTDLRLEDN LLTGISGDIF SNLGNLVTLV
MSRNRLRTID SRAFVSTNGL RHLHLDHNDI DLQQPLLDIM LQTQINSPFG YMHGLLTLNL
RNNSIIFVYN DWKNTMLQLR ELDLSYNNIS SLGYEDLAFL SQNRLHVNMT HNKIRRIALP
EDVHLGEGYN NNLVHVDLND NPLVCDCTIL WFIQLVRGVH KPQYSRQFKL RTDRLVCSQP
NVLEGTPVRQ IEPQTLICPL DFSDDPRERK CPRGCNCHVR TYDKALVINC HSGNLTHVPR
LPNLHKNMQL MELHLENNTL LRLPSANTPG YESVTSLHLA GNNLTSIDVD QLPTNLTHLD
ISWNHLQMLN ATVLGFLNRT MKWRSVKLSG NPWMCDCTAK PLLLFTQDNF ERIGDRNEMM
CVNAEMPTRM VELSTNDICP AEKGVFIALA VVIALTGLLA GFTAALYYKF QTEIKIWLYA
HNLLLWFVTE EDLDKDKKFD AFISYSHKDQ SFIEDYLVPQ LEHGPQKFQL CVHERDWLVG
GHIPENIMRS VADSRRTIIV LSQNFIKSEW ARLEFRAAHR SALNEGRSRI IVIIYSDIGD
VEKLDEELKA YLKMNTYLKW GDPWFWDKLR FALPHRRPVG NIGNGALIKT ALKGSTDDKL
ELIKPSPVTP PLTTPPAEAT KNPLVAQLNG VTPHQAIMIA NGKNGLTNLY TPNGKSHGNG
HINGAFIINT NAKQSDV
