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P08953

- TOLL_DROME

UniProt

P08953 - TOLL_DROME

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Protein

Protein toll

Gene

Tl

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

Functioni

Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo. Three proteases; ndl, gd and snk process easter to create active easter. Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo. Promotes heterophilic cellular adhesion. Spz C-106 in the hemolymph controls expression of the antifungal peptide Drosomycin (Drs) by acting as a ligand of Tl and inducing an intracellular signaling pathway.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. response to bacterium Source: FlyBase
  19. response to fungus Source: FlyBase
  20. synapse assembly Source: FlyBase
  21. synaptic target inhibition Source: FlyBase
  22. Toll signaling pathway Source: FlyBase
  23. zygotic specification of dorsal/ventral axis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion

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

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

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
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi175 – 1751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi346 – 3461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi528 – 5281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi654 – 6541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi703 – 7031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi715 – 7151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi730 – 7301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi738 – 7381N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08953.
PRIDEiP08953.

Expressioni

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiP08953.
ExpressionAtlasiP08953. differential.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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...

Topological domain

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

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei808 – 82821HelicalSequence AnalysisAdd
BLAST

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A29943.
RefSeqi NP_524518.1. NM_079794.3.
NP_733166.1. NM_170287.3.
UniGenei Dm.2347.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4ARN X-ray 2.41 A/B/C/D 28-228 [» ]
4ARR X-ray 3.00 A/B 28-228 [» ]
4BV4 X-ray 2.35 R 28-397 [» ]
4LXR X-ray 2.20 A 28-802 [» ]
4LXS X-ray 3.30 A 28-802 [» ]
ProteinModelPortali P08953.
SMRi P08953. Positions 28-993.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 68116. 10 interactions.
DIPi DIP-34358N.
IntActi P08953. 3 interactions.
STRINGi 7227.FBpp0084431.

Proteomic databases

PaxDbi P08953.
PRIDEi P08953.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0085059 ; FBpp0084431 ; FBgn0262473 .
FBtr0330155 ; FBpp0303188 ; FBgn0262473 .
GeneIDi 43222.
KEGGi dme:Dmel_CG5490.

Organism-specific databases

CTDi 109651.
FlyBasei FBgn0262473. Tl.

Phylogenomic databases

eggNOGi COG4886.
GeneTreei ENSGT00760000119006.
InParanoidi P08953.
OrthoDBi EOG761BT1.
PhylomeDBi P08953.

Miscellaneous databases

ChiTaRSi Tl. drosophila.
GenomeRNAii 43222.
NextBioi 832799.
PROi P08953.

Gene expression databases

Bgeei P08953.
ExpressionAtlasi P08953. differential.

Family and domain databases

Gene3Di 3.40.50.10140. 1 hit.
InterProi IPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR000157. TIR_dom.
[Graphical view ]
Pfami PF00560. LRR_1. 2 hits.
PF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view ]
SMARTi SM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 2 hits.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view ]
SUPFAMi SSF52200. SSF52200. 1 hit.
PROSITEi PS51450. LRR. 13 hits.
PS50104. TIR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  8. "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.
  9. "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.

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: October 29, 2014
This is version 164 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