TOLL8_DROME
ID TOLL8_DROME Reviewed; 1346 AA.
AC Q9V477; Q2XXW0;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Toll-like receptor Tollo {ECO:0000305};
DE AltName: Full=Toll-like receptor 8 {ECO:0000305};
DE Flags: Precursor;
GN Name=Tollo {ECO:0000312|FlyBase:FBgn0029114};
GN Synonyms=Tl-8 {ECO:0000312|FlyBase:FBgn0029114},
GN Toll-8 {ECO:0000312|FlyBase:FBgn0029114};
GN ORFNames=CG6890 {ECO:0000312|FlyBase:FBgn0029114};
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 {ECO:0000312|EMBL:AAF18983.1};
RN [1] {ECO:0000312|EMBL:AAF18983.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000312|EMBL:AAF18983.1};
RA Seppo A., Matani P., Tiemeyer M.;
RT "Tollo regulates neural expression of the HRP-epitope in Drosophila.";
RL Glycobiology 9:1138-1138(1999).
RN [2] {ECO:0000312|EMBL:AAF86224.1}
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [3] {ECO:0000312|EMBL:ABA86508.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ral1 {ECO:0000312|EMBL:ABA86508.1};
RX PubMed=16120803; DOI=10.1093/molbev/msi246;
RA Comeron J.M., Guthrie T.B.;
RT "Intragenic Hill-Robertson interference influences selection intensity on
RT synonymous mutations in Drosophila.";
RL Mol. Biol. Evol. 22:2519-2530(2005).
RN [4] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [5] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [6] {ECO:0000312|EMBL:AAM49920.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM49920.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000312|EMBL:AAF49650.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA Svirskas R., Rubin G.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000305}
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 [9] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=12588858; DOI=10.1242/dev.00347;
RA Seppo A., Matani P., Sharrow M., Tiemeyer M.;
RT "Induction of neuron-specific glycosylation by Tollo/Toll-8, a Drosophila
RT Toll-like receptor expressed in non-neural cells.";
RL Development 130:1439-1448(2003).
RN [10] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17078066; DOI=10.1002/dvg.20245;
RA Kim S., Chung S., Yoon J., Choi K.W., Yim J.;
RT "Ectopic expression of Tollo/Toll-8 antagonizes Dpp signaling and induces
RT cell sorting in the Drosophila wing.";
RL Genesis 44:541-549(2006).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=17264077; DOI=10.1074/jbc.m606711200;
RA Aoki K., Perlman M., Lim J.M., Cantu R., Wells L., Tiemeyer M.;
RT "Dynamic developmental elaboration of N-linked glycan complexity in the
RT Drosophila melanogaster embryo.";
RL J. Biol. Chem. 282:9127-9142(2007).
RN [12] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18000549; DOI=10.1371/journal.pone.0001178;
RA Ayyar S., Pistillo D., Calleja M., Brookfield A., Gittins K., Goldstone C.,
RA Simpson P.;
RT "NF-kappaB/Rel-mediated regulation of the neural fate in Drosophila.";
RL PLoS ONE 2:E1178-E1178(2007).
RN [13] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21158756; DOI=10.1111/j.1440-169x.2010.01213.x;
RA Yagi Y., Nishida Y., Ip Y.T.;
RT "Functional analysis of Toll-related genes in Drosophila.";
RL Dev. Growth Differ. 52:771-783(2010).
RN [14] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION BY BACTERIA,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22022271; DOI=10.1371/journal.ppat.1002319;
RA Akhouayri I., Turc C., Royet J., Charroux B.;
RT "Toll-8/Tollo negatively regulates antimicrobial response in the Drosophila
RT respiratory epithelium.";
RL PLoS Pathog. 7:E1002319-E1002319(2011).
RN [15]
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 [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24662564; DOI=10.1083/jcb.201308115;
RA Ballard S.L., Miller D.L., Ganetzky B.;
RT "Retrograde neurotrophin signaling through Tollo regulates synaptic growth
RT in Drosophila.";
RL J. Cell Biol. 204:1157-1172(2014).
RN [17]
RP FUNCTION, INTERACTION WITH 18W, AND DEVELOPMENTAL STAGE.
RX PubMed=25363762; DOI=10.1038/nature13953;
RA Pare A.C., Vichas A., Fincher C.T., Mirman Z., Farrell D.L., Mainieri A.,
RA Zallen J.A.;
RT "A positional Toll receptor code directs convergent extension in
RT Drosophila.";
RL Nature 515:523-527(2014).
RN [18]
RP FUNCTION.
RX PubMed=25477468; DOI=10.1126/science.1258236;
RA Meyer S.N., Amoyel M., Bergantinos C., de la Cova C., Schertel C.,
RA Basler K., Johnston L.A.;
RT "An ancient defense system eliminates unfit cells from developing tissues
RT during cell competition.";
RL Science 346:1258236-1258236(2014).
CC -!- FUNCTION: Toll-related receptor (PubMed:10973475). Probably specific to
CC larval innate immunity (PubMed:22022271). Involved in the tracheal
CC immune response of larvae to Gram-negative and perhaps Gram-positive
CC bacteria; upon infection it negatively regulates the immune deficiency
CC (Imd) signaling cascade specifically in the respiratory epithelium to
CC prevent the overexpression of antimicrobial peptides (AMP)
CC (PubMed:22022271). Involved in the NF-kappa-B-dependent apoptosis of
CC unfit cells during cell competition (PubMed:25477468). Involved in
CC neuron-specific glycosylation (PubMed:12588858, PubMed:17264077).
CC Positively controls the neuromuscular junction (NMJ) growth in
CC presynaptic motorneurons, probably via the JNK pathway
CC (PubMed:24662564). During development of the peripheral nervous system,
CC may function in the NF-kappa-B (rel) regulatory cascade to repress
CC expression of the neuron-specific genes sc and ase in non-neuronal
CC cells (PubMed:18000549). Promotes heterophilic cell adhesion with 18w
CC in vitro (PubMed:25363762). May have a minor role in leg development
CC (PubMed:21158756). May be involved in determining the proximal cell
CC fate in the wing, possibly by negatively regulating the Dpp signaling
CC pathway.(PubMed:17078066). May also be involved in the Dpp signaling
CC pathway in the eye (PubMed:17078066). Possibly functions with 18w and
CC Toll-6 during convergent extension, to help direct proper planar cell
CC polarity, cell intercalation and axis elongation (PubMed:25363762).
CC {ECO:0000269|PubMed:10973475, ECO:0000269|PubMed:17078066,
CC ECO:0000269|PubMed:17264077, ECO:0000269|PubMed:18000549,
CC ECO:0000269|PubMed:21158756, ECO:0000269|PubMed:22022271,
CC ECO:0000269|PubMed:24662564, ECO:0000269|PubMed:25363762,
CC ECO:0000269|PubMed:25477468}.
CC -!- SUBUNIT: May interact (via the extracellular domain) with 18w (via the
CC extracellular domain). {ECO:0000269|PubMed:25363762}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22022271};
CC Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane
CC {ECO:0000269|PubMed:22022271}. Note=In larvae, localizes to the apical
CC cell membrane in trachea epithelial cells.
CC {ECO:0000269|PubMed:22022271}.
CC -!- DEVELOPMENTAL STAGE: At the cellular blastoderm stage, expressed in 8
CC segmentally repeated stripes, and 14 stripes at germ band extension (at
CC protein level) (PubMed:12617819). Expressed in the neurogenic region
CC during the blastoderm and germ band extension stages (at protein level)
CC (PubMed:12617819). Expressed zygotically (PubMed:12617819). Expressed
CC throughout development, with two peaks of expression at mid-
CC embryogenesis (6-12 hours old embryos) and in early larvae stages
CC (PubMed:10973475). First detected in the cellular blastoderm as two
CC distinct anterior and posterior bands (PubMed:12588858). By germband
CC retraction (late stage 12), segmentally repeated stripes span the width
CC of the germband (PubMed:25363762, PubMed:12588858). In embryos (stages
CC 12-15), detected in ectodermal cells that surround differentiating
CC neurons of the ventral nerve cord and peripheral nervous system
CC (PubMed:12588858). In third instar larvae, expressed at high levels in
CC the tracheal epithelium, and at relatively lower levels in the gut and
CC fat body (PubMed:22022271). In the wing imaginal disks, expressed in
CC the proximal region around the wing pouch and noctum, and in the hinge
CC regions (PubMed:17078066, PubMed:21158756). Also expressed in the
CC anterior compartment of the leg imaginal disks (PubMed:21158756). In
CC larvae, detected in the blood cells, lymph glands and fat body
CC (PubMed:12617819). In third instar larvae to the pre-pupae stage, high
CC levels of expression across the lateral noctum except where
CC dorsocentral and scutellar bristles form (PubMed:18000549). In late
CC stage third instar larvae, expressed throughout the lateral noctum
CC epithelium, except for the SOPs (anterior postalar, supraalar and
CC sensilla trichoidea) in which expression decreases as SOPs develop
CC (PubMed:18000549). {ECO:0000269|PubMed:10973475,
CC ECO:0000269|PubMed:12588858, ECO:0000269|PubMed:12617819,
CC ECO:0000269|PubMed:17078066, ECO:0000269|PubMed:18000549,
CC ECO:0000269|PubMed:21158756, ECO:0000269|PubMed:22022271,
CC ECO:0000269|PubMed:25363762}.
CC -!- INDUCTION: By Gram-negative bacteria, in the respiratory epithelium
CC (PubMed:22022271). Up-regulated during vesicular stomatitis virus (VSV)
CC infection (PubMed:22464169). {ECO:0000269|PubMed:22022271,
CC ECO:0000269|PubMed:22464169}.
CC -!- DISRUPTION PHENOTYPE: Viable (PubMed:18000549, PubMed:22022271). The
CC legs of some adults have the correct number of segments but are bent
CC between the tibia and tarsus, causing the leg to twist in the wrong
CC direction (PubMed:21158756). Formation of ectopic bristles on the
CC heminota (PubMed:18000549). Slight decrease in the branch length of
CC NMJ3 and a reduced number of boutons at NMJ3 and NMJ4
CC (PubMed:24662564). In larvae, tracheal cell morphology is normal and
CC basal expression levels of the AMP gene Drs are unaffected
CC (PubMed:22022271). However after infection with Gram-negative bacteria,
CC the respiratory epithelium displays an over-active immune response with
CC a greater increase in expression of AMPs (Drs, Dro and AttC) compared
CC to wild-type larvae (PubMed:22022271). In adults, no effect on the
CC immune response to septic injury using a mixture of Gram-positive and
CC Gram-negative bacteria; adults are able induce expression of
CC antibacterial peptide genes (Drs, AttA, DptA and Mtk) and mount a
CC proper innate immune response (PubMed:21158756). No visible effect on
CC the development of the embryo central nervous system (PubMed:21158756).
CC {ECO:0000269|PubMed:18000549, ECO:0000269|PubMed:21158756,
CC ECO:0000269|PubMed:22022271, ECO:0000269|PubMed:24662564}.
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; AF204158; AAF18983.1; -; Genomic_DNA.
DR EMBL; AF247764; AAF86224.1; -; mRNA.
DR EMBL; DQ138902; ABA86508.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49650.1; -; Genomic_DNA.
DR EMBL; AY118551; AAM49920.1; -; mRNA.
DR RefSeq; NP_524757.1; NM_080018.2.
DR AlphaFoldDB; Q9V477; -.
DR SMR; Q9V477; -.
DR IntAct; Q9V477; 5.
DR STRING; 7227.FBpp0075360; -.
DR GlyGen; Q9V477; 14 sites.
DR PaxDb; Q9V477; -.
DR PRIDE; Q9V477; -.
DR DNASU; 44497; -.
DR EnsemblMetazoa; FBtr0075607; FBpp0075360; FBgn0029114.
DR GeneID; 44497; -.
DR KEGG; dme:Dmel_CG6890; -.
DR UCSC; CG6890-RA; d. melanogaster.
DR CTD; 44497; -.
DR FlyBase; FBgn0029114; Tollo.
DR VEuPathDB; VectorBase:FBgn0029114; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000170875; -.
DR HOGENOM; CLU_004280_0_0_1; -.
DR InParanoid; Q9V477; -.
DR OMA; WSTMSLE; -.
DR OrthoDB; 282372at2759; -.
DR PhylomeDB; Q9V477; -.
DR BioGRID-ORCS; 44497; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 44497; -.
DR PRO; PR:Q9V477; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0029114; Expressed in wing disc and 36 other tissues.
DR ExpressionAtlas; Q9V477; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0003401; P:axis elongation; IGI:FlyBase.
DR GO; GO:0060026; P:convergent extension; IGI:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048935; P:peripheral nervous system neuron development; IMP:FlyBase.
DR GO; GO:0060049; P:regulation of protein glycosylation; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IMP:FlyBase.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 8.
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; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF13855; LRR_8; 6.
DR Pfam; PF13676; TIR_2; 1.
DR SMART; SM00369; LRR_TYP; 25.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 23.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW Leucine-rich repeat; Membrane; NAD; Neurogenesis; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1346
FT /note="Toll-like receptor Tollo"
FT /id="PRO_5007216111"
FT TOPO_DOM 22..1021
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1022..1042
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1043..1346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 97..120
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 124..146
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 151..174
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 176..198
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 209..232
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 234..256
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 257..280
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 282..304
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 306..330
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 331..354
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 355..378
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 380..402
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 404..426
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 427..450
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 452..473
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 474..497
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 498..521
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 523..544
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 546..568
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 570..591
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 593..614
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 615..637
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 638..661
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 790..813
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 814..837
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 838..861
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 863..885
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT REPEAT 887..909
FT /note="LRR 28"
FT /evidence="ECO:0000255"
FT REPEAT 912..938
FT /note="LRR 29"
FT /evidence="ECO:0000255"
FT DOMAIN 1074..1209
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 1235..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 682..710
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT DISULFID 684..733
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT DISULFID 757..763
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT DISULFID 761..776
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT DISULFID 924..950
FT /evidence="ECO:0000250|UniProtKB:P08953"
FT CONFLICT 1..7
FT /note="Missing (in Ref. 3; ABA86508)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="Q -> P (in Ref. 3; ABA86508)"
FT /evidence="ECO:0000305"
FT CONFLICT 1285..1346
FT /note="QIRGNNNTTQQQQQQQAALLMGGGSVGGPAPQMIPLAGGIQQQSLPLPPNQQ
FT PTPASRNLHM -> SNSRQQQHDAAAAATAGGLADGRRVGGWACSTDDSPGGWHPAAEP
FT TIATEPATDAG (in Ref. 3; ABA86508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1346 AA; 153305 MW; 00C31F239619D4CE CRC64;
MLATTHMLYV LIATCVIPIF GAALSKTVLY QAPDECRWSG GGEHDITLVC HLRTINSELE
NTNFSVIQPQ NTVRLRLECN DALFFQSSLS PDSFRSLVEL RDLTIEYCKL GNLTDGSFRG
LQELRNLTIR THNGDWSTMS LEMASNSFVE FRQLERLDLS LNNIWLIPDG MVCPLKSLQH
LNASYNKIQD ISNFYFSASL SSRKARVCGS TLQSLDLSAN KMVSLPTAML SALGRLTHLN
MAKNSMSFLA DRAFEGLLSL RVVDLSANRL TSLPPELFAE TKQLQEIYLR NNSINVLAPG
IFGELAELLV LDLASNELNS QWINAATFVG LKRLMMLDLS ANKISRLEAH IFRPLASLQI
LKLEDNYIDQ LPGGIFADLT NLHTLILSRN RISVIEQRTL QGLKNLLVLS LDFNRISRMD
QRSLVNCSQL QDLHLNDNKL QAVPEALAHV QLLKTLDVGE NMISQIENTS ITQLESLYGL
RMTENSLTHI RRGVFDRMSS LQILNLSQNK LKSIEAGSLQ RNSQLQAIRL DGNQLKSIAG
LFTELPNLVW LNISGNRLEK FDYSHIPIGL QWLDVRANRI TQLGNYFEIE SELSLSTFDA
SYNLLTEITA SSIPNSVEVL YLNDNQISKI QPYTFFKKPN LTRVDLVRNR LTTLEPNALR
LSPIAEDREI PEFYIGHNAY ECDCNLDWLQ KVNRESRTQP QLMDLDQIHC RLAYARGSSH
VSLIEAKSDD FLCKYASHCF ALCHCCDFQA CDCKMECPDR CSCYHDQSWT SNVVDCSRAS
YEQTLPSHIP MDSTQLYLDG NNFRELQSHA FIGRKRLKVL HLNHSRIEVL HNRTFYGLLE
LEVLQLQSNQ LKALNGNEFQ GLDNLQELYL QHNAIATIDT LTFTHLYHLK ILRLDHNAIT
SFAVWNFLPS YLNELRLASN PWTCSCEFID KLRDYINRHE YVVDKLKMKC DVISGNSTQQ
MVIYPGSGEP ASLPVVQCSQ TLPLGLDNNF NYAEQAGGEN ASNATSTKMI LNQPPKLDYI
PILVAILTAF IFVMICISLV FIFRQEMRVW CHSRFGVRLF YNAQKDVDKN EREKLFDAFV
SYSSKDELFV NEELAPMLEM GEHRYKLCLH QRDFPVGGYL PETIVQAIDS SRRTIMVVSE
NFIKSEWCRF EFKSAHQSVL RDRRRRLIVI VLGEVPQKEL DPDLRLYLKT NTYLQWGDKL
FWQKLRFALP DVSSSQRSNV AGQSCHVPIN HASYHHHHHV HQQAMPLPHS VHHHQQQFML
PPPPQQPGSF RRQPSLHQQQ QQQQQIRGNN NTTQQQQQQQ AALLMGGGSV GGPAPQMIPL
AGGIQQQSLP LPPNQQPTPA SRNLHM
