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Protein toll

 TOLL_DROME              Reviewed;        1097 AA.
P08953; A4V3G7; A8WHK7; Q8MRF3; Q9VBB8;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
12-SEP-2018, entry version 200.
RecName: Full=Protein toll;
Flags: Precursor;
Name=Tl {ECO:0000312|FlyBase:FBgn0262473};
ORFNames=CG5490 {ECO:0000312|FlyBase:FBgn0262473};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=2449285; DOI=10.1016/0092-8674(88)90516-8;
Hashimoto C., Hudson K.L., Anderson K.V.;
"The Toll gene of Drosophila, required for dorsal-ventral embryonic
polarity, appears to encode a transmembrane protein.";
Cell 52:269-279(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H.,
Yu C., Celniker S.E.;
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-1097, AND VARIANTS.
STRAIN=MelZim1, MelZim3, MelZim4, MelZim5, MelZim6, MelZim7, and
MelZim8;
PubMed=12930753;
Schlenke T.A., Begun D.J.;
"Natural selection drives Drosophila immune system evolution.";
Genetics 164:1471-1480(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-1097.
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
FUNCTION.
PubMed=3931919; DOI=10.1016/0092-8674(85)90275-2;
Anderson K.V., Bokla L., Nusslein-Volhard C.;
"Establishment of dorsal-ventral polarity in the Drosophila embryo:
the induction of polarity by the Toll gene product.";
Cell 42:791-798(1985).
[8]
FUNCTION.
PubMed=2124970;
Keith F.J., Gay N.J.;
"The Drosophila membrane receptor Toll can function to promote
cellular adhesion.";
EMBO J. 9:4299-4306(1990).
[9]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=1879347;
Hashimoto C., Gerttula S., Anderson K.V.;
"Plasma membrane localization of the Toll protein in the syncytial
Drosophila embryo: importance of transmembrane signaling for dorsal-
ventral pattern formation.";
Development 111:1021-1028(1991).
[10]
FUNCTION.
PubMed=8808632; DOI=10.1016/S0092-8674(00)80172-5;
Lemaitre B., Nicolas E., Michaut L., Reichhart J.-M., Hoffmann J.A.;
"The dorsoventral regulatory gene cassette spatzle/Toll/cactus
controls the potent antifungal response in Drosophila adults.";
Cell 86:973-983(1996).
[11]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=10973475; DOI=10.1073/pnas.180130797;
Tauszig S., Jouanguy E., Hoffmann J.A., Imler J.L.;
"Toll-related receptors and the control of antimicrobial peptide
expression in Drosophila.";
Proc. Natl. Acad. Sci. U.S.A. 97:10520-10525(2000).
[12]
DEVELOPMENTAL STAGE.
PubMed=12617819; DOI=10.1016/S1567-133X(02)00020-0;
Kambris Z., Hoffmann J.A., Imler J.L., Capovilla M.;
"Tissue and stage-specific expression of the Tolls in Drosophila
embryos.";
Gene Expr. Patterns 2:311-317(2002).
[13]
FUNCTION.
PubMed=12872120; DOI=10.1038/ni955;
Weber A.N., Tauszig-Delamasure S., Hoffmann J.A., Lelievre E.,
Gascan H., Ray K.P., Morse M.A., Imler J.L., Gay N.J.;
"Binding of the Drosophila cytokine Spatzle to Toll is direct and
establishes signaling.";
Nat. Immunol. 4:794-800(2003).
[14]
SUBCELLULAR LOCATION.
PubMed=15373972; DOI=10.1179/096805104225004897;
Bettencourt R., Tanji T., Yagi Y., Ip Y.T.;
"Toll and Toll-9 in Drosophila innate immune response.";
J. Endotoxin Res. 10:261-268(2004).
[15]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=19018662; DOI=10.1371/journal.pbio.0060284;
Zhu B., Pennack J.A., McQuilton P., Forero M.G., Mizuguchi K.,
Sutcliffe B., Gu C.-J., Fenton J.C., Hidalgo A.;
"Drosophila neurotrophins reveal a common mechanism for nervous system
formation.";
PLoS Biol. 6:E284-E284(2008).
[16]
INDUCTION BY VIRAL INFECTION.
PubMed=22464169; DOI=10.1016/j.immuni.2012.03.003;
Nakamoto M., Moy R.H., Xu J., Bambina S., Yasunaga A., Shelly S.S.,
Gold B., Cherry S.;
"Virus recognition by Toll-7 activates antiviral autophagy in
Drosophila.";
Immunity 36:658-667(2012).
[17]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=20504957; DOI=10.1242/dev.046672;
Inaki M., Shinza-Kameda M., Ismat A., Frasch M., Nose A.;
"Drosophila Tey represses transcription of the repulsive cue Toll and
generates neuromuscular target specificity.";
Development 137:2139-2146(2010).
[18]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 28-228, AND GLYCOSYLATION AT
ASN-80 AND ASN-140.
PubMed=23596340; DOI=10.1107/S0021889812051606;
Gangloff M., Moreno A., Gay N.J.;
"Liesegang-like patterns of Toll crystals grown in gel.";
J. Appl. Crystallogr. 46:337-345(2013).
[19]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 28-397 IN COMPLEX WITH SPZ,
SUBUNIT, AND GLYCOSYLATION AT ASN-80; ASN-140; ASN-270; ASN-346 AND
ASN-391.
PubMed=24282309; DOI=10.1073/pnas.1317002110;
Lewis M., Arnot C.J., Beeston H., McCoy A., Ashcroft A.E., Gay N.J.,
Gangloff M.;
"Cytokine Spatzle binds to the Drosophila immunoreceptor Toll with a
neurotrophin-like specificity and couples receptor activation.";
Proc. Natl. Acad. Sci. U.S.A. 110:20461-20466(2013).
[20]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 28-228, MUTAGENESIS OF
ARG-154; LYS-208 AND ARG-432, AND GLYCOSYLATION AT ASN-80; ASN-140 AND
ASN-175.
PubMed=23245851; DOI=10.1016/j.str.2012.11.003;
Gangloff M., Arnot C.J., Lewis M., Gay N.J.;
"Functional insights from the crystal structure of the N-terminal
domain of the prototypical toll receptor.";
Structure 21:143-153(2013).
[21]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 28-802 IN COMPLEX WITH SPZ,
SUBUNIT, AND GLYCOSYLATION AT ASN-80; ASN-140; ASN-175; ASN-235;
ASN-270; ASN-346; ASN-391; ASN-482; ASN-508; ASN-528; ASN-654; ASN-703
AND ASN-715.
PubMed=24733933; DOI=10.1073/pnas.1320678111;
Parthier C., Stelter M., Ursel C., Fandrich U., Lilie H.,
Breithaupt C., Stubbs M.T.;
"Structure of the Toll-Spatzle complex, a molecular hub in Drosophila
development and innate immunity.";
Proc. Natl. Acad. Sci. U.S.A. 111:6281-6286(2014).
-!- FUNCTION: Receptor for the cleaved activated form of spz, spaetzle
C-106 (PubMed:12872120). Binding to spaetzle C-106 activates the
Toll signaling pathway and induces expression of the antifungal
peptide drosomycin (PubMed:12872120, PubMed:8808632,
PubMed:10973475). Component of the extracellular signaling pathway
that establishes dorsal-ventral polarity in the embryo
(PubMed:3931919). Promotes heterophilic cellular adhesion
(PubMed:2124970). Involved in synaptic targeting of motoneurons
RP5 and V to muscle 12 (M12); functions as a repulsive cue
inhibiting motoneuron synapse formation on muscle 13 (M13) to
guide RP5 and V to the neighboring M12, where its expression is
repressed by tey (PubMed:20504957). May also function in embryonic
neuronal survival and the synaptic targeting of SNa motoneurons
(PubMed:19018662). {ECO:0000269|PubMed:10973475,
ECO:0000269|PubMed:12872120, ECO:0000269|PubMed:19018662,
ECO:0000269|PubMed:20504957, ECO:0000269|PubMed:2124970,
ECO:0000269|PubMed:3931919, ECO:0000269|PubMed:8808632}.
-!- SUBUNIT: In the absence of ligand, forms a low-affinity disulfide-
linked homodimer (PubMed:24733933). In the presence of ligand,
crystal structures show one Tl molecule bound to a spaetzle C-106
homodimer (PubMed:24282309, PubMed:24733933). However, the active
complex probably consists of two Tl molecules bound to a spaetzle
C-106 homodimer (PubMed:24282309, PubMed:24733933). This is
supported by in vitro experiments which also show binding of the
spaetzle C-106 dimer to 2 Tl receptors (PubMed:12872120). Ligand
binding induces conformational changes in the extracellular domain
of Tl (PubMed:24282309). This may enable a secondary
homodimerization interface at the C-terminus of the Tl
extracellular domain (PubMed:24282309).
{ECO:0000269|PubMed:12872120, ECO:0000269|PubMed:24282309,
ECO:0000269|PubMed:24733933, ECO:0000303|PubMed:24282309}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-143610, EBI-143610;
Q7K105:Myd88; NbExp=3; IntAct=EBI-143610, EBI-129988;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15373972,
ECO:0000269|PubMed:1879347}; Single-pass type I membrane protein
{ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15373972}. Note=In
the fat body, detected in puntate structures along the cell
periphery. Becomes evenly distributed in the cytoplasm 1 hour
after bacterial infection. {ECO:0000269|PubMed:15373972}.
-!- TISSUE SPECIFICITY: In early embryos, concentrated in the
pseudocleavage furrows that form transiently between nuclei before
cellularization and in the cleavage furrows during cellularization
(at protein level) (PubMed:1879347). Later, found on cells in the
mesectoderm, stomodeum, proctodeum, anterior and posterior
midguts, splanchnopleura, salivary gland placode and adjacent to
the segmentally repeated tracheal placodes (at protein level)
(PubMed:1879347). During and after germ band shortening, localized
in a number of cell types, including the salivary gland, foregut,
hindgut, Malpighian tubules and epidermis (at protein level)
(PubMed:1879347). In embryos, high expression in M13 with
comparatively low expression in M12 (PubMed:20504957).
{ECO:0000269|PubMed:1879347, ECO:0000269|PubMed:20504957}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
(PubMed:2449285, PubMed:1879347, PubMed:12617819). Maternal Tl
increases in syncytial embryos, reaching a peak at the syncytial
blastoderm stage and then decreases and is almost undetectable by
the time of ventral furrow formation at gastrulation (at protein
level) (PubMed:1879347). Expressed throughout development, with
highest levels of expression in the embryo (PubMed:10973475).
Expressed in all embryonic central nervous system axons
(PubMed:19018662). In larvae, detected in the blood cells and fat
body (PubMed:12617819). {ECO:0000269|PubMed:10973475,
ECO:0000269|PubMed:12617819, ECO:0000269|PubMed:1879347,
ECO:0000269|PubMed:19018662, ECO:0000269|PubMed:2449285}.
-!- INDUCTION: Up-regulated during vesicular stomatitis virus (VSV)
infection. {ECO:0000269|PubMed:22464169}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
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EMBL; M19969; AAA28941.1; -; mRNA.
EMBL; AE014297; AAF56624.1; -; Genomic_DNA.
EMBL; AE014297; AAN14086.1; -; Genomic_DNA.
EMBL; BT031153; ABX00775.1; -; mRNA.
EMBL; AY349649; AAQ64932.1; -; Genomic_DNA.
EMBL; AY349650; AAQ64933.1; -; Genomic_DNA.
EMBL; AY349651; AAQ64934.1; -; Genomic_DNA.
EMBL; AY349652; AAQ64935.1; -; Genomic_DNA.
EMBL; AY349653; AAQ64936.1; -; Genomic_DNA.
EMBL; AY349654; AAQ64937.1; -; Genomic_DNA.
EMBL; AY349655; AAQ64938.1; -; Genomic_DNA.
EMBL; AY121616; AAM51943.1; -; mRNA.
PIR; A29943; A29943.
RefSeq; NP_524518.1; NM_079794.3.
RefSeq; NP_733166.1; NM_170287.3.
UniGene; Dm.2347; -.
PDB; 4ARN; X-ray; 2.41 A; A/B/C/D=28-228.
PDB; 4ARR; X-ray; 3.00 A; A/B=28-228.
PDB; 4BV4; X-ray; 2.35 A; R=28-397.
PDB; 4LXR; X-ray; 2.20 A; A=28-802.
PDB; 4LXS; X-ray; 3.30 A; A=28-802.
PDBsum; 4ARN; -.
PDBsum; 4ARR; -.
PDBsum; 4BV4; -.
PDBsum; 4LXR; -.
PDBsum; 4LXS; -.
ProteinModelPortal; P08953; -.
SMR; P08953; -.
BioGrid; 68116; 22.
DIP; DIP-34358N; -.
IntAct; P08953; 4.
MINT; P08953; -.
STRING; 7227.FBpp0303187; -.
PaxDb; P08953; -.
PRIDE; P08953; -.
EnsemblMetazoa; FBtr0085059; FBpp0084431; FBgn0262473.
EnsemblMetazoa; FBtr0330155; FBpp0303188; FBgn0262473.
GeneID; 43222; -.
KEGG; dme:Dmel_CG5490; -.
CTD; 109651; -.
FlyBase; FBgn0262473; Tl.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
InParanoid; P08953; -.
KO; K18809; -.
OMA; PAIMIAN; -.
OrthoDB; EOG091G00ZN; -.
PhylomeDB; P08953; -.
Reactome; R-DME-209442; Formation of the trans-membrane 'signalling complex'.
Reactome; R-DME-214842; DL and DIF homodimers bind to TUB and phosphorylated PLL in the TL receptor 'signalling complex'.
Reactome; R-DME-214844; DL and DIF homodimers complexed with CACT are all phosphorylated in the TL receptor 'signalling complex'.
Reactome; R-DME-214862; Activated PLL kinase is autophosphorylated in the TL receptor 'signalling complex'.
Reactome; R-DME-214863; Adaptor protein complex binds to TL receptor at the plasma membrane.
Reactome; R-DME-214869; Phosphorylated CACT, DL and DIF homodimers dissociate from the TL receptor 'signalling complex'.
Reactome; R-DME-214874; PLL kinase binds to TUB in the TL receptor 'signalling complex'.
ChiTaRS; Tl; fly.
GenomeRNAi; 43222; -.
PRO; PR:P08953; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0262473; Expressed in 34 organ(s), highest expression level in embryo.
ExpressionAtlas; P08953; baseline and differential.
Genevisible; P08953; DM.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005769; C:early endosome; IDA:FlyBase.
GO; GO:0009897; C:external side of plasma membrane; IDA:FlyBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
GO; GO:0019955; F:cytokine binding; TAS:FlyBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070976; F:TIR domain binding; IPI:FlyBase.
GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:FlyBase.
GO; GO:0019732; P:antifungal humoral response; IMP:FlyBase.
GO; GO:0019730; P:antimicrobial humoral response; IGI:FlyBase.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; TAS:FlyBase.
GO; GO:0050832; P:defense response to fungus; TAS:FlyBase.
GO; GO:0050830; P:defense response to Gram-positive bacterium; TAS:FlyBase.
GO; GO:0002229; P:defense response to oomycetes; IMP:FlyBase.
GO; GO:0009950; P:dorsal/ventral axis specification; IMP:UniProtKB.
GO; GO:0009880; P:embryonic pattern specification; TAS:FlyBase.
GO; GO:0007507; P:heart development; IMP:FlyBase.
GO; GO:0035172; P:hemocyte proliferation; IMP:FlyBase.
GO; GO:0030097; P:hemopoiesis; TAS:FlyBase.
GO; GO:0006955; P:immune response; TAS:FlyBase.
GO; GO:0045087; P:innate immune response; IDA:FlyBase.
GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
GO; GO:0006967; P:positive regulation of antifungal peptide biosynthetic process; IMP:FlyBase.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
GO; GO:1902875; P:regulation of embryonic pattern specification; IMP:UniProtKB.
GO; GO:0045610; P:regulation of hemocyte differentiation; IMP:FlyBase.
GO; GO:0035007; P:regulation of melanization defense response; TAS:FlyBase.
GO; GO:0009617; P:response to bacterium; NAS:FlyBase.
GO; GO:0009620; P:response to fungus; TAS:FlyBase.
GO; GO:0007416; P:synapse assembly; IMP:FlyBase.
GO; GO:0016201; P:synaptic target inhibition; IMP:FlyBase.
GO; GO:0008063; P:Toll signaling pathway; TAS:Reactome.
GO; GO:0007352; P:zygotic specification of dorsal/ventral axis; NAS:FlyBase.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR026906; LRR_5.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
Pfam; PF00560; LRR_1; 2.
Pfam; PF13306; LRR_5; 1.
Pfam; PF13855; LRR_8; 1.
Pfam; PF01462; LRRNT; 1.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 11.
SMART; SM00082; LRRCT; 2.
SMART; SM00013; LRRNT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 13.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell membrane; Complete proteome;
Cytoplasm; Developmental protein; Disulfide bond; Glycoprotein;
Immunity; Innate immunity; Leucine-rich repeat; Membrane;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 1097 Protein toll.
/FTId=PRO_0000034740.
TOPO_DOM 28 807 Extracellular. {ECO:0000255}.
TRANSMEM 808 828 Helical. {ECO:0000255}.
TOPO_DOM 829 1097 Cytoplasmic. {ECO:0000255}.
REPEAT 175 195 LRR 1.
REPEAT 198 219 LRR 2.
REPEAT 222 243 LRR 3.
REPEAT 246 267 LRR 4.
REPEAT 270 291 LRR 5.
REPEAT 294 314 LRR 6.
REPEAT 320 340 LRR 7.
REPEAT 343 364 LRR 8.
REPEAT 367 388 LRR 9.
REPEAT 391 412 LRR 10.
REPEAT 415 436 LRR 11.
REPEAT 439 460 LRR 12.
REPEAT 474 495 LRR 13.
REPEAT 498 521 LRR 14.
REPEAT 523 544 LRR 15.
DOMAIN 561 620 LRRCT 1.
DOMAIN 622 663 LRRNT.
REPEAT 669 690 LRR 16.
REPEAT 693 713 LRR 17.
REPEAT 715 738 LRR 18.
DOMAIN 751 801 LRRCT 2.
DOMAIN 857 996 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4ARN,
ECO:0000244|PDB:4ARR,
ECO:0000244|PDB:4BV4,
ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:23245851,
ECO:0000269|PubMed:23596340,
ECO:0000269|PubMed:24282309,
ECO:0000269|PubMed:24733933}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4ARN,
ECO:0000244|PDB:4ARR,
ECO:0000244|PDB:4BV4,
ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:23245851,
ECO:0000269|PubMed:23596340,
ECO:0000269|PubMed:24282309,
ECO:0000269|PubMed:24733933}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4ARN,
ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:23245851,
ECO:0000269|PubMed:24733933}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:24733933}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4BV4,
ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:24282309,
ECO:0000269|PubMed:24733933}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4BV4,
ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:24282309,
ECO:0000269|PubMed:24733933}.
CARBOHYD 391 391 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4BV4,
ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:24282309,
ECO:0000269|PubMed:24733933}.
CARBOHYD 482 482 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:24733933}.
CARBOHYD 508 508 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:24733933}.
CARBOHYD 528 528 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:24733933}.
CARBOHYD 654 654 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:24733933}.
CARBOHYD 677 677 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 703 703 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS,
ECO:0000269|PubMed:24733933}.
CARBOHYD 715 715 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4LXR,
ECO:0000269|PubMed:24733933}.
CARBOHYD 730 730 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 738 738 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 45 {ECO:0000244|PDB:4ARN,
ECO:0000244|PDB:4ARR,
ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS}.
DISULFID 43 56 {ECO:0000244|PDB:4ARN,
ECO:0000244|PDB:4ARR,
ECO:0000244|PDB:4BV4,
ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS}.
DISULFID 79 107 {ECO:0000244|PDB:4ARN,
ECO:0000244|PDB:4ARR,
ECO:0000244|PDB:4BV4,
ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS}.
DISULFID 565 597 {ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS}.
DISULFID 567 618 {ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS}.
DISULFID 631 637 {ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS}.
DISULFID 635 650 {ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS}.
DISULFID 755 781 {ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS}.
DISULFID 757 799 {ECO:0000244|PDB:4LXR,
ECO:0000244|PDB:4LXS}.
VARIANT 98 98 E -> G (in strain: MelZim6).
VARIANT 218 218 G -> S (in strain: MelZim7).
VARIANT 245 245 T -> S (in strain: MelZim3).
VARIANT 390 390 T -> I (in strain: MelZim3 and MelZim7).
VARIANT 414 414 G -> A (in strain: MelZim3).
VARIANT 435 435 V -> L (in strain: MelZim8).
VARIANT 460 460 M -> T (in strain: MelZim6).
VARIANT 471 471 Y -> D (in strain: MelZim1, MelZim4,
MelZim5 and MelZim6).
VARIANT 486 486 I -> R (in strain: MelZim6).
VARIANT 513 513 G -> R (in strain: MelZim1, MelZim5 and
MelZim6).
VARIANT 538 538 A -> E (in strain: MelZim1, MelZim5 and
MelZim6).
VARIANT 544 544 H -> Y (in strain: MelZim1, MelZim5 and
MelZim6).
VARIANT 568 568 T -> M (in strain: MelZim1, MelZim5 and
MelZim6).
VARIANT 592 592 T -> A (in strain: MelZim6).
VARIANT 603 603 L -> M (in strain: MelZim1, MelZim5 and
MelZim6).
VARIANT 681 681 L -> V (in strain: MelZim1, MelZim3,
MelZim4, MelZim5, MelZim6 and MelZim7).
VARIANT 714 714 T -> I (in strain: MelZim5 and MelZim8).
VARIANT 732 732 T -> S (in strain: MelZim8).
VARIANT 741 741 M -> I (in strain: MelZim1).
MUTAGEN 154 154 R->A: No change in signaling capacity.
{ECO:0000269|PubMed:23245851}.
MUTAGEN 208 208 K->E: 25% decrease in signaling capacity.
{ECO:0000269|PubMed:23245851}.
MUTAGEN 432 432 R->A: 33% decrease in signaling capacity.
{ECO:0000269|PubMed:23245851}.
CONFLICT 355 355 K -> S (in Ref. 5; AAQ64932/AAQ64933/
AAQ64934/AAQ64935/AAQ64936/AAQ64937/
AAQ64938). {ECO:0000305}.
CONFLICT 602 602 V -> A (in Ref. 5; AAQ64933/AAQ64934/
AAQ64937/AAQ64938). {ECO:0000305}.
CONFLICT 786 786 M -> I (in Ref. 4; ABX00775).
{ECO:0000305}.
CONFLICT 825 825 A -> T (in Ref. 4; ABX00775).
{ECO:0000305}.
HELIX 31 36 {ECO:0000244|PDB:4LXR}.
TURN 37 40 {ECO:0000244|PDB:4LXR}.
STRAND 42 48 {ECO:0000244|PDB:4LXR}.
STRAND 51 57 {ECO:0000244|PDB:4LXR}.
STRAND 64 70 {ECO:0000244|PDB:4LXR}.
STRAND 72 79 {ECO:0000244|PDB:4LXR}.
HELIX 84 89 {ECO:0000244|PDB:4LXR}.
STRAND 97 106 {ECO:0000244|PDB:4LXR}.
STRAND 111 113 {ECO:0000244|PDB:4ARN}.
HELIX 115 121 {ECO:0000244|PDB:4LXR}.
STRAND 124 126 {ECO:0000244|PDB:4ARR}.
STRAND 128 133 {ECO:0000244|PDB:4LXR}.
HELIX 143 146 {ECO:0000244|PDB:4LXR}.
STRAND 153 158 {ECO:0000244|PDB:4LXR}.
TURN 167 172 {ECO:0000244|PDB:4LXR}.
STRAND 177 183 {ECO:0000244|PDB:4LXR}.
HELIX 190 193 {ECO:0000244|PDB:4LXR}.
STRAND 201 203 {ECO:0000244|PDB:4LXR}.
HELIX 217 219 {ECO:0000244|PDB:4LXR}.
STRAND 225 227 {ECO:0000244|PDB:4LXR}.
HELIX 238 241 {ECO:0000244|PDB:4LXR}.
STRAND 249 251 {ECO:0000244|PDB:4LXR}.
TURN 262 267 {ECO:0000244|PDB:4LXR}.
STRAND 273 275 {ECO:0000244|PDB:4LXR}.
TURN 286 291 {ECO:0000244|PDB:4LXR}.
STRAND 297 300 {ECO:0000244|PDB:4LXR}.
TURN 312 315 {ECO:0000244|PDB:4LXR}.
STRAND 323 326 {ECO:0000244|PDB:4LXR}.
TURN 335 340 {ECO:0000244|PDB:4LXR}.
STRAND 346 348 {ECO:0000244|PDB:4LXR}.
TURN 359 364 {ECO:0000244|PDB:4LXR}.
STRAND 370 372 {ECO:0000244|PDB:4LXR}.
TURN 383 386 {ECO:0000244|PDB:4LXR}.
STRAND 394 396 {ECO:0000244|PDB:4LXR}.
TURN 409 412 {ECO:0000244|PDB:4LXR}.
STRAND 418 420 {ECO:0000244|PDB:4LXR}.
TURN 431 434 {ECO:0000244|PDB:4LXR}.
STRAND 442 444 {ECO:0000244|PDB:4LXR}.
HELIX 456 460 {ECO:0000244|PDB:4LXR}.
HELIX 468 471 {ECO:0000244|PDB:4LXR}.
STRAND 477 479 {ECO:0000244|PDB:4LXR}.
HELIX 490 494 {ECO:0000244|PDB:4LXR}.
STRAND 501 503 {ECO:0000244|PDB:4LXR}.
STRAND 511 513 {ECO:0000244|PDB:4LXS}.
HELIX 514 517 {ECO:0000244|PDB:4LXR}.
STRAND 526 528 {ECO:0000244|PDB:4LXR}.
STRAND 536 538 {ECO:0000244|PDB:4LXS}.
STRAND 554 557 {ECO:0000244|PDB:4LXR}.
HELIX 567 569 {ECO:0000244|PDB:4LXR}.
HELIX 570 576 {ECO:0000244|PDB:4LXR}.
STRAND 577 579 {ECO:0000244|PDB:4LXR}.
HELIX 584 586 {ECO:0000244|PDB:4LXR}.
STRAND 588 591 {ECO:0000244|PDB:4LXR}.
STRAND 596 600 {ECO:0000244|PDB:4LXR}.
TURN 601 605 {ECO:0000244|PDB:4LXR}.
HELIX 608 610 {ECO:0000244|PDB:4LXR}.
HELIX 613 615 {ECO:0000244|PDB:4LXR}.
STRAND 617 619 {ECO:0000244|PDB:4LXR}.
STRAND 636 640 {ECO:0000244|PDB:4LXR}.
TURN 641 644 {ECO:0000244|PDB:4LXR}.
STRAND 645 649 {ECO:0000244|PDB:4LXR}.
STRAND 670 674 {ECO:0000244|PDB:4LXR}.
HELIX 691 693 {ECO:0000244|PDB:4LXR}.
STRAND 695 698 {ECO:0000244|PDB:4LXR}.
HELIX 709 711 {ECO:0000244|PDB:4LXR}.
STRAND 718 720 {ECO:0000244|PDB:4LXR}.
STRAND 723 725 {ECO:0000244|PDB:4LXS}.
HELIX 731 737 {ECO:0000244|PDB:4LXR}.
STRAND 745 747 {ECO:0000244|PDB:4LXR}.
HELIX 757 759 {ECO:0000244|PDB:4LXR}.
HELIX 760 767 {ECO:0000244|PDB:4LXR}.
TURN 770 772 {ECO:0000244|PDB:4LXR}.
HELIX 776 778 {ECO:0000244|PDB:4LXR}.
HELIX 790 792 {ECO:0000244|PDB:4LXR}.
HELIX 795 798 {ECO:0000244|PDB:4LXR}.
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


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