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Protein

Protein toll

Gene

Tl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).7 Publications

GO - Molecular functioni

  • cytokine binding Source: FlyBase
  • TIR domain binding Source: FlyBase
  • transmembrane signaling receptor activity Source: FlyBase

GO - Biological processi

  • antifungal humoral response Source: FlyBase
  • antimicrobial humoral response Source: FlyBase
  • cell adhesion Source: UniProtKB-KW
  • defense response Source: FlyBase
  • defense response to fungus Source: FlyBase
  • defense response to Gram-positive bacterium Source: FlyBase
  • defense response to oomycetes Source: FlyBase
  • dorsal/ventral axis specification Source: UniProtKB
  • embryonic pattern specification Source: FlyBase
  • heart development Source: FlyBase
  • hemocyte proliferation Source: FlyBase
  • hemopoiesis Source: FlyBase
  • immune response Source: FlyBase
  • innate immune response Source: FlyBase
  • larval somatic muscle development Source: FlyBase
  • mitotic cytokinesis Source: FlyBase
  • positive regulation of antibacterial peptide biosynthetic process Source: FlyBase
  • positive regulation of antifungal peptide biosynthetic process Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • regulation of embryonic pattern specification Source: UniProtKB
  • regulation of hemocyte differentiation Source: FlyBase
  • regulation of melanization defense response Source: FlyBase
  • response to bacterium Source: FlyBase
  • response to fungus Source: FlyBase
  • synapse assembly Source: FlyBase
  • synaptic target inhibition Source: FlyBase
  • Toll signaling pathway Source: FlyBase
  • zygotic specification of dorsal/ventral axis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Cell adhesion, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-DME-109704. PI3K Cascade.
R-DME-1679131. Trafficking and processing of endosomal TLR.
R-DME-168138. Toll Like Receptor 9 (TLR9) Cascade.
R-DME-168181. Toll Like Receptor 7/8 (TLR7/8) Cascade.
R-DME-5686938. Regulation of TLR by endogenous ligand.
R-DME-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-DME-975138. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
R-DME-975155. MyD88 dependent cascade initiated on endosome.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein toll
Gene namesi
Name:TlImported
ORF Names:CG5490Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0262473. Tl.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 807ExtracellularSequence analysisAdd BLAST780
Transmembranei808 – 828HelicalSequence analysisAdd BLAST21
Topological domaini829 – 1097CytoplasmicSequence analysisAdd BLAST269

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: FlyBase
  • early endosome Source: FlyBase
  • external side of plasma membrane Source: FlyBase
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
  • protein complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi154R → A: No change in signaling capacity. 1 Publication1
Mutagenesisi208K → E: 25% decrease in signaling capacity. 1 Publication1
Mutagenesisi432R → A: 33% decrease in signaling capacity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000003474028 – 1097Protein tollAdd BLAST1070

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi34 ↔ 45Combined sources
Disulfide bondi43 ↔ 56Combined sources
Disulfide bondi79 ↔ 107Combined sources
Glycosylationi80N-linked (GlcNAc...)Combined sources1
Glycosylationi140N-linked (GlcNAc...)Combined sources1
Glycosylationi175N-linked (GlcNAc...)Combined sources1
Glycosylationi235N-linked (GlcNAc...)Combined sources1
Glycosylationi270N-linked (GlcNAc...)Combined sources1
Glycosylationi275N-linked (GlcNAc...)Sequence analysis1
Glycosylationi346N-linked (GlcNAc...)Combined sources1
Glycosylationi391N-linked (GlcNAc...)Combined sources1
Glycosylationi482N-linked (GlcNAc...)Combined sources1
Glycosylationi508N-linked (GlcNAc...)Combined sources1
Glycosylationi528N-linked (GlcNAc...)Combined sources1
Disulfide bondi565 ↔ 597Combined sources
Disulfide bondi567 ↔ 618Combined sources
Disulfide bondi631 ↔ 637Combined sources
Disulfide bondi635 ↔ 650Combined sources
Glycosylationi654N-linked (GlcNAc...)Combined sources1
Glycosylationi677N-linked (GlcNAc...)Sequence analysis1
Glycosylationi703N-linked (GlcNAc...)Combined sources1
Glycosylationi715N-linked (GlcNAc...)Combined sources1
Glycosylationi730N-linked (GlcNAc...)Sequence analysis1
Glycosylationi738N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi755 ↔ 781Combined sources
Disulfide bondi757 ↔ 799Combined sources

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08953.
PRIDEiP08953.

Expressioni

Tissue specificityi

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).2 Publications

Developmental stagei

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).5 Publications

Inductioni

Up-regulated during vesicular stomatitis virus (VSV) infection.1 Publication

Gene expression databases

BgeeiFBgn0262473.
ExpressionAtlasiP08953. baseline.
GenevisibleiP08953. DM.

Interactioni

Subunit structurei

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).1 Publication3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-143610,EBI-143610
Myd88Q7K1053EBI-143610,EBI-129988

GO - Molecular functioni

  • cytokine binding Source: FlyBase
  • TIR domain binding Source: FlyBase

Protein-protein interaction databases

BioGridi68116. 10 interactors.
DIPiDIP-34358N.
IntActiP08953. 3 interactors.
STRINGi7227.FBpp0303187.

Structurei

Secondary structure

11097
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 36Combined sources6
Turni37 – 40Combined sources4
Beta strandi42 – 48Combined sources7
Beta strandi51 – 57Combined sources7
Beta strandi64 – 70Combined sources7
Beta strandi72 – 79Combined sources8
Helixi84 – 89Combined sources6
Beta strandi97 – 106Combined sources10
Beta strandi111 – 113Combined sources3
Helixi115 – 121Combined sources7
Beta strandi124 – 126Combined sources3
Beta strandi128 – 133Combined sources6
Helixi143 – 146Combined sources4
Beta strandi153 – 158Combined sources6
Turni167 – 172Combined sources6
Beta strandi177 – 183Combined sources7
Helixi190 – 193Combined sources4
Beta strandi201 – 203Combined sources3
Helixi217 – 219Combined sources3
Beta strandi225 – 227Combined sources3
Helixi238 – 241Combined sources4
Beta strandi249 – 251Combined sources3
Turni262 – 267Combined sources6
Beta strandi273 – 275Combined sources3
Turni286 – 291Combined sources6
Beta strandi297 – 300Combined sources4
Turni312 – 315Combined sources4
Beta strandi323 – 326Combined sources4
Turni335 – 340Combined sources6
Beta strandi346 – 348Combined sources3
Turni359 – 364Combined sources6
Beta strandi370 – 372Combined sources3
Turni383 – 386Combined sources4
Beta strandi394 – 396Combined sources3
Turni409 – 412Combined sources4
Beta strandi418 – 420Combined sources3
Turni431 – 434Combined sources4
Beta strandi442 – 444Combined sources3
Helixi456 – 460Combined sources5
Helixi468 – 471Combined sources4
Beta strandi477 – 479Combined sources3
Helixi490 – 494Combined sources5
Beta strandi501 – 503Combined sources3
Beta strandi511 – 513Combined sources3
Helixi514 – 517Combined sources4
Beta strandi526 – 528Combined sources3
Beta strandi536 – 538Combined sources3
Beta strandi554 – 557Combined sources4
Helixi567 – 569Combined sources3
Helixi570 – 576Combined sources7
Beta strandi577 – 579Combined sources3
Helixi584 – 586Combined sources3
Beta strandi588 – 591Combined sources4
Beta strandi596 – 600Combined sources5
Turni601 – 605Combined sources5
Helixi608 – 610Combined sources3
Helixi613 – 615Combined sources3
Beta strandi617 – 619Combined sources3
Beta strandi636 – 640Combined sources5
Turni641 – 644Combined sources4
Beta strandi645 – 649Combined sources5
Beta strandi670 – 674Combined sources5
Helixi691 – 693Combined sources3
Beta strandi695 – 698Combined sources4
Helixi709 – 711Combined sources3
Beta strandi718 – 720Combined sources3
Beta strandi723 – 725Combined sources3
Helixi731 – 737Combined sources7
Beta strandi745 – 747Combined sources3
Helixi757 – 759Combined sources3
Helixi760 – 767Combined sources8
Turni770 – 772Combined sources3
Helixi776 – 778Combined sources3
Helixi790 – 792Combined sources3
Helixi795 – 798Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ARNX-ray2.41A/B/C/D28-228[»]
4ARRX-ray3.00A/B28-228[»]
4BV4X-ray2.35R28-397[»]
4LXRX-ray2.20A28-802[»]
4LXSX-ray3.30A28-802[»]
ProteinModelPortaliP08953.
SMRiP08953.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati175 – 195LRR 1Add BLAST21
Repeati198 – 219LRR 2Add BLAST22
Repeati222 – 243LRR 3Add BLAST22
Repeati246 – 267LRR 4Add BLAST22
Repeati270 – 291LRR 5Add BLAST22
Repeati294 – 314LRR 6Add BLAST21
Repeati320 – 340LRR 7Add BLAST21
Repeati343 – 364LRR 8Add BLAST22
Repeati367 – 388LRR 9Add BLAST22
Repeati391 – 412LRR 10Add BLAST22
Repeati415 – 436LRR 11Add BLAST22
Repeati439 – 460LRR 12Add BLAST22
Repeati474 – 495LRR 13Add BLAST22
Repeati498 – 521LRR 14Add BLAST24
Repeati523 – 544LRR 15Add BLAST22
Domaini561 – 620LRRCT 1Add BLAST60
Domaini622 – 663LRRNTAdd BLAST42
Repeati669 – 690LRR 16Add BLAST22
Repeati693 – 713LRR 17Add BLAST21
Repeati715 – 738LRR 18Add BLAST24
Domaini751 – 801LRRCT 2Add BLAST51
Domaini857 – 996TIRPROSITE-ProRule annotationAdd BLAST140

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated
Contains 18 LRR (leucine-rich) repeats.Curated
Contains 2 LRRCT domains.Curated
Contains 1 LRRNT domain.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
InParanoidiP08953.
KOiK18809.
OrthoDBiEOG091G00ZN.
PhylomeDBiP08953.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 5 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR026906. LRR_5.
IPR000372. LRRNT.
IPR000157. TIR_dom.
IPR027202. Toll.
[Graphical view]
PANTHERiPTHR24365:SF325. PTHR24365:SF325. 3 hits.
PfamiPF00560. LRR_1. 1 hit.
PF13306. LRR_5. 1 hit.
PF13855. LRR_8. 1 hit.
PF01462. LRRNT. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 11 hits.
SM00082. LRRCT. 2 hits.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 3 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 13 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08953-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRLKAASEL ALLVIILQLL QWPGSEASFG RDACSEMSID GLCQCAPIMS
60 70 80 90 100
EYEIICPANA ENPTFRLTIQ PKDYVQIMCN LTDTTDYQQL PKKLRIGEVD
110 120 130 140 150
RVQMRRCMLP GHTPIASILD YLGIVSPTTL IFESDNLGMN ITRQHLDRLH
160 170 180 190 200
GLKRFRFTTR RLTHIPANLL TDMRNLSHLE LRANIEEMPS HLFDDLENLE
210 220 230 240 250
SIEFGSNKLR QMPRGIFGKM PKLKQLNLWS NQLHNLTKHD FEGATSVLGI
260 270 280 290 300
DIHDNGIEQL PHDVFAHLTN VTDINLSANL FRSLPQGLFD HNKHLNEVRL
310 320 330 340 350
MNNRVPLATL PSRLFANQPE LQILRLRAEL QSLPGDLFEH STQITNISLG
360 370 380 390 400
DNLLKTLPAT LLEHQVNLLS LDLSNNRLTH LPDSLFAHTT NLTDLRLEDN
410 420 430 440 450
LLTGISGDIF SNLGNLVTLV MSRNRLRTID SRAFVSTNGL RHLHLDHNDI
460 470 480 490 500
DLQQPLLDIM LQTQINSPFG YMHGLLTLNL RNNSIIFVYN DWKNTMLQLR
510 520 530 540 550
ELDLSYNNIS SLGYEDLAFL SQNRLHVNMT HNKIRRIALP EDVHLGEGYN
560 570 580 590 600
NNLVHVDLND NPLVCDCTIL WFIQLVRGVH KPQYSRQFKL RTDRLVCSQP
610 620 630 640 650
NVLEGTPVRQ IEPQTLICPL DFSDDPRERK CPRGCNCHVR TYDKALVINC
660 670 680 690 700
HSGNLTHVPR LPNLHKNMQL MELHLENNTL LRLPSANTPG YESVTSLHLA
710 720 730 740 750
GNNLTSIDVD QLPTNLTHLD ISWNHLQMLN ATVLGFLNRT MKWRSVKLSG
760 770 780 790 800
NPWMCDCTAK PLLLFTQDNF ERIGDRNEMM CVNAEMPTRM VELSTNDICP
810 820 830 840 850
AEKGVFIALA VVIALTGLLA GFTAALYYKF QTEIKIWLYA HNLLLWFVTE
860 870 880 890 900
EDLDKDKKFD AFISYSHKDQ SFIEDYLVPQ LEHGPQKFQL CVHERDWLVG
910 920 930 940 950
GHIPENIMRS VADSRRTIIV LSQNFIKSEW ARLEFRAAHR SALNEGRSRI
960 970 980 990 1000
IVIIYSDIGD VEKLDEELKA YLKMNTYLKW GDPWFWDKLR FALPHRRPVG
1010 1020 1030 1040 1050
NIGNGALIKT ALKGSTDDKL ELIKPSPVTP PLTTPPAEAT KNPLVAQLNG
1060 1070 1080 1090
VTPHQAIMIA NGKNGLTNLY TPNGKSHGNG HINGAFIINT NAKQSDV
Length:1,097
Mass (Da):124,656
Last modified:November 1, 1988 - v1
Checksum:iD1BFC42245E3EABE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti355K → S in AAQ64932 (PubMed:12930753).Curated1
Sequence conflicti355K → S in AAQ64933 (PubMed:12930753).Curated1
Sequence conflicti355K → S in AAQ64934 (PubMed:12930753).Curated1
Sequence conflicti355K → S in AAQ64935 (PubMed:12930753).Curated1
Sequence conflicti355K → S in AAQ64936 (PubMed:12930753).Curated1
Sequence conflicti355K → S in AAQ64937 (PubMed:12930753).Curated1
Sequence conflicti355K → S in AAQ64938 (PubMed:12930753).Curated1
Sequence conflicti602V → A in AAQ64933 (PubMed:12930753).Curated1
Sequence conflicti602V → A in AAQ64934 (PubMed:12930753).Curated1
Sequence conflicti602V → A in AAQ64937 (PubMed:12930753).Curated1
Sequence conflicti602V → A in AAQ64938 (PubMed:12930753).Curated1
Sequence conflicti786M → I in ABX00775 (Ref. 4) Curated1
Sequence conflicti825A → T in ABX00775 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti98E → G in strain: MelZim6. 1
Natural varianti218G → S in strain: MelZim7. 1
Natural varianti245T → S in strain: MelZim3. 1
Natural varianti390T → I in strain: MelZim3 and MelZim7. 1
Natural varianti414G → A in strain: MelZim3. 1
Natural varianti435V → L in strain: MelZim8. 1
Natural varianti460M → T in strain: MelZim6. 1
Natural varianti471Y → D in strain: MelZim1, MelZim4, MelZim5 and MelZim6. 1
Natural varianti486I → R in strain: MelZim6. 1
Natural varianti513G → R in strain: MelZim1, MelZim5 and MelZim6. 1
Natural varianti538A → E in strain: MelZim1, MelZim5 and MelZim6. 1
Natural varianti544H → Y in strain: MelZim1, MelZim5 and MelZim6. 1
Natural varianti568T → M in strain: MelZim1, MelZim5 and MelZim6. 1
Natural varianti592T → A in strain: MelZim6. 1
Natural varianti603L → M in strain: MelZim1, MelZim5 and MelZim6. 1
Natural varianti681L → V in strain: MelZim1, MelZim3, MelZim4, MelZim5, MelZim6 and MelZim7. 1
Natural varianti714T → I in strain: MelZim5 and MelZim8. 1
Natural varianti732T → S in strain: MelZim8. 1
Natural varianti741M → I in strain: MelZim1. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19969 mRNA. Translation: AAA28941.1.
AE014297 Genomic DNA. Translation: AAF56624.1.
AE014297 Genomic DNA. Translation: AAN14086.1.
BT031153 mRNA. Translation: ABX00775.1.
AY349649 Genomic DNA. Translation: AAQ64932.1.
AY349650 Genomic DNA. Translation: AAQ64933.1.
AY349651 Genomic DNA. Translation: AAQ64934.1.
AY349652 Genomic DNA. Translation: AAQ64935.1.
AY349653 Genomic DNA. Translation: AAQ64936.1.
AY349654 Genomic DNA. Translation: AAQ64937.1.
AY349655 Genomic DNA. Translation: AAQ64938.1.
AY121616 mRNA. Translation: AAM51943.1.
PIRiA29943.
RefSeqiNP_524518.1. NM_079794.3.
NP_733166.1. NM_170287.3.
UniGeneiDm.2347.

Genome annotation databases

EnsemblMetazoaiFBtr0085059; FBpp0084431; FBgn0262473.
FBtr0330155; FBpp0303188; FBgn0262473.
GeneIDi43222.
KEGGidme:Dmel_CG5490.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19969 mRNA. Translation: AAA28941.1.
AE014297 Genomic DNA. Translation: AAF56624.1.
AE014297 Genomic DNA. Translation: AAN14086.1.
BT031153 mRNA. Translation: ABX00775.1.
AY349649 Genomic DNA. Translation: AAQ64932.1.
AY349650 Genomic DNA. Translation: AAQ64933.1.
AY349651 Genomic DNA. Translation: AAQ64934.1.
AY349652 Genomic DNA. Translation: AAQ64935.1.
AY349653 Genomic DNA. Translation: AAQ64936.1.
AY349654 Genomic DNA. Translation: AAQ64937.1.
AY349655 Genomic DNA. Translation: AAQ64938.1.
AY121616 mRNA. Translation: AAM51943.1.
PIRiA29943.
RefSeqiNP_524518.1. NM_079794.3.
NP_733166.1. NM_170287.3.
UniGeneiDm.2347.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ARNX-ray2.41A/B/C/D28-228[»]
4ARRX-ray3.00A/B28-228[»]
4BV4X-ray2.35R28-397[»]
4LXRX-ray2.20A28-802[»]
4LXSX-ray3.30A28-802[»]
ProteinModelPortaliP08953.
SMRiP08953.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68116. 10 interactors.
DIPiDIP-34358N.
IntActiP08953. 3 interactors.
STRINGi7227.FBpp0303187.

Proteomic databases

PaxDbiP08953.
PRIDEiP08953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085059; FBpp0084431; FBgn0262473.
FBtr0330155; FBpp0303188; FBgn0262473.
GeneIDi43222.
KEGGidme:Dmel_CG5490.

Organism-specific databases

CTDi109651.
FlyBaseiFBgn0262473. Tl.

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
InParanoidiP08953.
KOiK18809.
OrthoDBiEOG091G00ZN.
PhylomeDBiP08953.

Enzyme and pathway databases

ReactomeiR-DME-109704. PI3K Cascade.
R-DME-1679131. Trafficking and processing of endosomal TLR.
R-DME-168138. Toll Like Receptor 9 (TLR9) Cascade.
R-DME-168181. Toll Like Receptor 7/8 (TLR7/8) Cascade.
R-DME-5686938. Regulation of TLR by endogenous ligand.
R-DME-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-DME-975138. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
R-DME-975155. MyD88 dependent cascade initiated on endosome.

Miscellaneous databases

ChiTaRSiTl. fly.
GenomeRNAii43222.
PROiP08953.

Gene expression databases

BgeeiFBgn0262473.
ExpressionAtlasiP08953. baseline.
GenevisibleiP08953. DM.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 5 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR026906. LRR_5.
IPR000372. LRRNT.
IPR000157. TIR_dom.
IPR027202. Toll.
[Graphical view]
PANTHERiPTHR24365:SF325. PTHR24365:SF325. 3 hits.
PfamiPF00560. LRR_1. 1 hit.
PF13306. LRR_5. 1 hit.
PF13855. LRR_8. 1 hit.
PF01462. LRRNT. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 11 hits.
SM00082. LRRCT. 2 hits.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 3 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 13 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTOLL_DROME
AccessioniPrimary (citable) accession number: P08953
Secondary accession number(s): A4V3G7
, A8WHK7, Q8MRF3, Q9VBB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 30, 2016
This is version 183 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.