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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). Component of the extracellular signaling pathway that establishes dorsal-ventral polarity in the embryo (PubMed:3931919). Promotes heterophilic cellular adhesion (PubMed:2124970).4 Publications

GO - Molecular functioni

  1. cytokine binding Source: FlyBase
  2. identical protein binding Source: IntAct
  3. TIR domain binding Source: FlyBase
  4. transmembrane signaling receptor activity Source: FlyBase

GO - Biological processi

  1. antifungal humoral response Source: FlyBase
  2. antimicrobial humoral response Source: FlyBase
  3. cell adhesion Source: UniProtKB-KW
  4. defense response Source: FlyBase
  5. defense response to fungus Source: FlyBase
  6. defense response to Gram-positive bacterium Source: FlyBase
  7. dorsal/ventral axis specification Source: FlyBase
  8. embryonic pattern specification Source: FlyBase
  9. heart development Source: FlyBase
  10. hemocyte proliferation Source: FlyBase
  11. hemopoiesis Source: FlyBase
  12. immune response Source: FlyBase
  13. innate immune response Source: FlyBase
  14. mitotic cytokinesis Source: FlyBase
  15. positive regulation of antibacterial peptide biosynthetic process Source: FlyBase
  16. positive regulation of antifungal peptide biosynthetic process Source: FlyBase
  17. regulation of hemocyte differentiation Source: FlyBase
  18. regulation of melanization defense response Source: FlyBase
  19. response to bacterium Source: FlyBase
  20. response to fungus Source: FlyBase
  21. synapse assembly Source: FlyBase
  22. synaptic target inhibition Source: FlyBase
  23. Toll signaling pathway Source: FlyBase
  24. 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

Names & Taxonomyi

Protein namesi
Recommended name:
Protein toll
Gene namesi
Name:Tl
ORF Names:CG5490
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0262473. Tl.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein Sequence Analysis

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 807780ExtracellularSequence AnalysisAdd
BLAST
Transmembranei808 – 82821HelicalSequence AnalysisAdd
BLAST
Topological domaini829 – 1097269CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. early endosome Source: FlyBase
  3. external side of plasma membrane Source: FlyBase
  4. integral component of membrane Source: UniProtKB-KW
  5. plasma membrane Source: FlyBase
  6. protein complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi154 – 1541R → A: No change in signaling capacity. 1 Publication
Mutagenesisi208 – 2081K → E: 25% decrease in signaling capacity. 1 Publication
Mutagenesisi432 – 4321R → A: 33% decrease in signaling capacity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 10971070Protein tollPRO_0000034740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 45Combined sources
Disulfide bondi43 ↔ 56Combined sources
Disulfide bondi79 ↔ 107Combined sources
Glycosylationi80 – 801N-linked (GlcNAc...)Combined sources
Glycosylationi140 – 1401N-linked (GlcNAc...)Combined sources
Glycosylationi175 – 1751N-linked (GlcNAc...)Combined sources
Glycosylationi235 – 2351N-linked (GlcNAc...)Combined sources
Glycosylationi270 – 2701N-linked (GlcNAc...)Combined sources
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi346 – 3461N-linked (GlcNAc...)Combined sources
Glycosylationi391 – 3911N-linked (GlcNAc...)Combined sources
Glycosylationi482 – 4821N-linked (GlcNAc...)Combined sources
Glycosylationi508 – 5081N-linked (GlcNAc...)Combined sources
Glycosylationi528 – 5281N-linked (GlcNAc...)Combined sources
Disulfide bondi565 ↔ 597Combined sources
Disulfide bondi567 ↔ 618Combined sources
Disulfide bondi631 ↔ 637Combined sources
Disulfide bondi635 ↔ 650Combined sources
Glycosylationi654 – 6541N-linked (GlcNAc...)Combined sources
Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi703 – 7031N-linked (GlcNAc...)Combined sources
Glycosylationi715 – 7151N-linked (GlcNAc...)Combined sources
Glycosylationi730 – 7301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi738 – 7381N-linked (GlcNAc...)Sequence Analysis
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. 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. 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).1 Publication

Developmental stagei

Expressed both maternally and zygotically (PubMed:2449285, PubMed:1879347). 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).2 Publications

Gene expression databases

BgeeiP08953.
ExpressionAtlasiP08953. differential.

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).3 Publications1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi68116. 10 interactions.
DIPiDIP-34358N.
IntActiP08953. 3 interactions.
STRINGi7227.FBpp0084431.

Structurei

Secondary structure

1
1097
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 366Combined sources
Turni37 – 404Combined sources
Beta strandi42 – 487Combined sources
Beta strandi51 – 577Combined sources
Beta strandi64 – 707Combined sources
Beta strandi72 – 798Combined sources
Helixi84 – 896Combined sources
Beta strandi97 – 10610Combined sources
Beta strandi111 – 1133Combined sources
Helixi115 – 1217Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1336Combined sources
Helixi143 – 1464Combined sources
Beta strandi153 – 1586Combined sources
Turni167 – 1726Combined sources
Beta strandi177 – 1837Combined sources
Helixi190 – 1934Combined sources
Beta strandi201 – 2033Combined sources
Helixi217 – 2193Combined sources
Beta strandi225 – 2273Combined sources
Helixi238 – 2414Combined sources
Beta strandi249 – 2513Combined sources
Turni262 – 2676Combined sources
Beta strandi273 – 2753Combined sources
Turni286 – 2916Combined sources
Beta strandi297 – 3004Combined sources
Turni312 – 3154Combined sources
Beta strandi323 – 3264Combined sources
Turni335 – 3406Combined sources
Beta strandi346 – 3483Combined sources
Turni359 – 3646Combined sources
Beta strandi370 – 3723Combined sources
Turni383 – 3864Combined sources
Beta strandi394 – 3963Combined sources
Turni409 – 4124Combined sources
Beta strandi418 – 4203Combined sources
Turni431 – 4344Combined sources
Beta strandi442 – 4443Combined sources
Helixi456 – 4605Combined sources
Helixi468 – 4714Combined sources
Beta strandi477 – 4793Combined sources
Helixi490 – 4945Combined sources
Beta strandi501 – 5033Combined sources
Beta strandi511 – 5133Combined sources
Helixi514 – 5174Combined sources
Beta strandi526 – 5283Combined sources
Beta strandi536 – 5383Combined sources
Beta strandi554 – 5574Combined sources
Helixi567 – 5693Combined sources
Helixi570 – 5767Combined sources
Beta strandi577 – 5793Combined sources
Helixi584 – 5863Combined sources
Beta strandi588 – 5914Combined sources
Beta strandi596 – 6005Combined sources
Turni601 – 6055Combined sources
Helixi608 – 6103Combined sources
Helixi613 – 6153Combined sources
Beta strandi617 – 6193Combined sources
Beta strandi636 – 6405Combined sources
Turni641 – 6444Combined sources
Beta strandi645 – 6495Combined sources
Beta strandi670 – 6745Combined sources
Helixi691 – 6933Combined sources
Beta strandi695 – 6984Combined sources
Helixi709 – 7113Combined sources
Beta strandi718 – 7203Combined sources
Beta strandi723 – 7253Combined sources
Helixi731 – 7377Combined sources
Beta strandi745 – 7473Combined sources
Helixi757 – 7593Combined sources
Helixi760 – 7678Combined sources
Turni770 – 7723Combined sources
Helixi776 – 7783Combined sources
Helixi790 – 7923Combined sources
Helixi795 – 7984Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 28-993.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati175 – 19521LRR 1Add
BLAST
Repeati198 – 21922LRR 2Add
BLAST
Repeati222 – 24322LRR 3Add
BLAST
Repeati246 – 26722LRR 4Add
BLAST
Repeati270 – 29122LRR 5Add
BLAST
Repeati294 – 31421LRR 6Add
BLAST
Repeati320 – 34021LRR 7Add
BLAST
Repeati343 – 36422LRR 8Add
BLAST
Repeati367 – 38822LRR 9Add
BLAST
Repeati391 – 41222LRR 10Add
BLAST
Repeati415 – 43622LRR 11Add
BLAST
Repeati439 – 46022LRR 12Add
BLAST
Repeati474 – 49522LRR 13Add
BLAST
Repeati498 – 52124LRR 14Add
BLAST
Repeati523 – 54422LRR 15Add
BLAST
Domaini561 – 62060LRRCT 1Add
BLAST
Domaini622 – 66342LRRNTAdd
BLAST
Repeati669 – 69022LRR 16Add
BLAST
Repeati693 – 71321LRR 17Add
BLAST
Repeati715 – 73824LRR 18Add
BLAST
Domaini751 – 80151LRRCT 2Add
BLAST
Domaini857 – 996140TIRPROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG4886.
GeneTreeiENSGT00760000119006.
InParanoidiP08953.
OrthoDBiEOG761BT1.
PhylomeDBiP08953.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR000157. TIR_dom.
[Graphical view]
PfamiPF00560. LRR_1. 2 hits.
PF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 2 hits.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52200. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti355 – 3551K → S in AAQ64932. (PubMed:12930753)Curated
Sequence conflicti355 – 3551K → S in AAQ64933. (PubMed:12930753)Curated
Sequence conflicti355 – 3551K → S in AAQ64934. (PubMed:12930753)Curated
Sequence conflicti355 – 3551K → S in AAQ64935. (PubMed:12930753)Curated
Sequence conflicti355 – 3551K → S in AAQ64936. (PubMed:12930753)Curated
Sequence conflicti355 – 3551K → S in AAQ64937. (PubMed:12930753)Curated
Sequence conflicti355 – 3551K → S in AAQ64938. (PubMed:12930753)Curated
Sequence conflicti602 – 6021V → A in AAQ64933. (PubMed:12930753)Curated
Sequence conflicti602 – 6021V → A in AAQ64934. (PubMed:12930753)Curated
Sequence conflicti602 – 6021V → A in AAQ64937. (PubMed:12930753)Curated
Sequence conflicti602 – 6021V → A in AAQ64938. (PubMed:12930753)Curated
Sequence conflicti786 – 7861M → I in ABX00775. 1 PublicationCurated
Sequence conflicti825 – 8251A → T in ABX00775. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981E → G in strain: MelZim6.
Natural varianti218 – 2181G → S in strain: MelZim7.
Natural varianti245 – 2451T → S in strain: MelZim3.
Natural varianti390 – 3901T → I in strain: MelZim3 and MelZim7.
Natural varianti414 – 4141G → A in strain: MelZim3.
Natural varianti435 – 4351V → L in strain: MelZim8.
Natural varianti460 – 4601M → T in strain: MelZim6.
Natural varianti471 – 4711Y → D in strain: MelZim1, MelZim4, MelZim5 and MelZim6.
Natural varianti486 – 4861I → R in strain: MelZim6.
Natural varianti513 – 5131G → R in strain: MelZim1, MelZim5 and MelZim6.
Natural varianti538 – 5381A → E in strain: MelZim1, MelZim5 and MelZim6.
Natural varianti544 – 5441H → Y in strain: MelZim1, MelZim5 and MelZim6.
Natural varianti568 – 5681T → M in strain: MelZim1, MelZim5 and MelZim6.
Natural varianti592 – 5921T → A in strain: MelZim6.
Natural varianti603 – 6031L → M in strain: MelZim1, MelZim5 and MelZim6.
Natural varianti681 – 6811L → V in strain: MelZim1, MelZim3, MelZim4, MelZim5, MelZim6 and MelZim7.
Natural varianti714 – 7141T → I in strain: MelZim5 and MelZim8.
Natural varianti732 – 7321T → S in strain: MelZim8.
Natural varianti741 – 7411M → I in strain: MelZim1.

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
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. Positions 28-993.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68116. 10 interactions.
DIPiDIP-34358N.
IntActiP08953. 3 interactions.
STRINGi7227.FBpp0084431.

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

eggNOGiCOG4886.
GeneTreeiENSGT00760000119006.
InParanoidiP08953.
OrthoDBiEOG761BT1.
PhylomeDBiP08953.

Miscellaneous databases

ChiTaRSiTl. fly.
GenomeRNAii43222.
NextBioi832799.
PROiP08953.

Gene expression databases

BgeeiP08953.
ExpressionAtlasiP08953. differential.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR000157. TIR_dom.
[Graphical view]
PfamiPF00560. LRR_1. 2 hits.
PF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 2 hits.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 13 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein."
    Hashimoto C., Hudson K.L., Anderson K.V.
    Cell 52:269-279(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
  2. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Natural selection drives Drosophila immune system evolution."
    Schlenke T.A., Begun D.J.
    Genetics 164:1471-1480(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-1097, VARIANTS.
    Strain: MelZim1, MelZim3, MelZim4, MelZim5, MelZim6, MelZim7 and MelZim8.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-1097.
    Strain: Berkeley.
    Tissue: Head.
  7. "Establishment of dorsal-ventral polarity in the Drosophila embryo: the induction of polarity by the Toll gene product."
    Anderson K.V., Bokla L., Nusslein-Volhard C.
    Cell 42:791-798(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The Drosophila membrane receptor Toll can function to promote cellular adhesion."
    Keith F.J., Gay N.J.
    EMBO J. 9:4299-4306(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Plasma membrane localization of the Toll protein in the syncytial Drosophila embryo: importance of transmembrane signaling for dorsal-ventral pattern formation."
    Hashimoto C., Gerttula S., Anderson K.V.
    Development 111:1021-1028(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  10. "The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults."
    Lemaitre B., Nicolas E., Michaut L., Reichhart J.-M., Hoffmann J.A.
    Cell 86:973-983(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Binding of the Drosophila cytokine Spatzle to Toll is direct and establishes signaling."
    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.
    Nat. Immunol. 4:794-800(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Liesegang-like patterns of Toll crystals grown in gel."
    Gangloff M., Moreno A., Gay N.J.
    J. Appl. Crystallogr. 46:337-345(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 28-228.
  13. "Cytokine Spatzle binds to the Drosophila immunoreceptor Toll with a neurotrophin-like specificity and couples receptor activation."
    Lewis M., Arnot C.J., Beeston H., McCoy A., Ashcroft A.E., Gay N.J., Gangloff M.
    Proc. Natl. Acad. Sci. U.S.A. 110:20461-20466(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 28-397 IN COMPLEX WITH SPZ, SUBUNIT.
  14. "Functional insights from the crystal structure of the N-terminal domain of the prototypical toll receptor."
    Gangloff M., Arnot C.J., Lewis M., Gay N.J.
    Structure 21:143-153(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 28-228, MUTAGENESIS OF ARG-154; LYS-208 AND ARG-432.
  15. "Structure of the Toll-Spatzle complex, a molecular hub in Drosophila development and innate immunity."
    Parthier C., Stelter M., Ursel C., Fandrich U., Lilie H., Breithaupt C., Stubbs M.T.
    Proc. Natl. Acad. Sci. U.S.A. 111:6281-6286(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 28-802 IN COMPLEX WITH SPZ, SUBUNIT.

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: January 7, 2015
This is version 166 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

External Data

Dasty 3

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 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.