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P08953

- TOLL_DROME

UniProt

P08953 - TOLL_DROME

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Protein
Protein toll
Gene
Tl, CG5490
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. TIR domain binding Source: FlyBase
  2. cytokine binding Source: FlyBase
  3. identical protein binding Source: IntAct
  4. protein binding Source: UniProtKB
  5. transmembrane signaling receptor activity Source: FlyBase
Complete GO annotation...

GO - Biological processi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 807780Extracellular Reviewed prediction
Add
BLAST
Transmembranei808 – 82821Helical; Reviewed prediction
Add
BLAST
Topological domaini829 – 1097269Cytoplasmic Reviewed prediction
Add
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727 Reviewed prediction
Add
BLAST
Chaini28 – 10971070Protein toll
PRO_0000034740Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08953.
PRIDEiP08953.

Expressioni

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiP08953.

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

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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 2 LRRCT domains.
Contains 1 LRRNT domain.
Contains 1 TIR domain.

Keywords - Domaini

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

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00710000106753.
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

MSRLKAASEL ALLVIILQLL QWPGSEASFG RDACSEMSID GLCQCAPIMS     50
EYEIICPANA ENPTFRLTIQ PKDYVQIMCN LTDTTDYQQL PKKLRIGEVD 100
RVQMRRCMLP GHTPIASILD YLGIVSPTTL IFESDNLGMN ITRQHLDRLH 150
GLKRFRFTTR RLTHIPANLL TDMRNLSHLE LRANIEEMPS HLFDDLENLE 200
SIEFGSNKLR QMPRGIFGKM PKLKQLNLWS NQLHNLTKHD FEGATSVLGI 250
DIHDNGIEQL PHDVFAHLTN VTDINLSANL FRSLPQGLFD HNKHLNEVRL 300
MNNRVPLATL PSRLFANQPE LQILRLRAEL QSLPGDLFEH STQITNISLG 350
DNLLKTLPAT LLEHQVNLLS LDLSNNRLTH LPDSLFAHTT NLTDLRLEDN 400
LLTGISGDIF SNLGNLVTLV MSRNRLRTID SRAFVSTNGL RHLHLDHNDI 450
DLQQPLLDIM LQTQINSPFG YMHGLLTLNL RNNSIIFVYN DWKNTMLQLR 500
ELDLSYNNIS SLGYEDLAFL SQNRLHVNMT HNKIRRIALP EDVHLGEGYN 550
NNLVHVDLND NPLVCDCTIL WFIQLVRGVH KPQYSRQFKL RTDRLVCSQP 600
NVLEGTPVRQ IEPQTLICPL DFSDDPRERK CPRGCNCHVR TYDKALVINC 650
HSGNLTHVPR LPNLHKNMQL MELHLENNTL LRLPSANTPG YESVTSLHLA 700
GNNLTSIDVD QLPTNLTHLD ISWNHLQMLN ATVLGFLNRT MKWRSVKLSG 750
NPWMCDCTAK PLLLFTQDNF ERIGDRNEMM CVNAEMPTRM VELSTNDICP 800
AEKGVFIALA VVIALTGLLA GFTAALYYKF QTEIKIWLYA HNLLLWFVTE 850
EDLDKDKKFD AFISYSHKDQ SFIEDYLVPQ LEHGPQKFQL CVHERDWLVG 900
GHIPENIMRS VADSRRTIIV LSQNFIKSEW ARLEFRAAHR SALNEGRSRI 950
IVIIYSDIGD VEKLDEELKA YLKMNTYLKW GDPWFWDKLR FALPHRRPVG 1000
NIGNGALIKT ALKGSTDDKL ELIKPSPVTP PLTTPPAEAT KNPLVAQLNG 1050
VTPHQAIMIA NGKNGLTNLY TPNGKSHGNG HINGAFIINT NAKQSDV 1097
Length:1,097
Mass (Da):124,656
Last modified:November 1, 1988 - v1
Checksum:iD1BFC42245E3EABE
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti355 – 3551K → S in AAQ64932. 1 Publication
Sequence conflicti355 – 3551K → S in AAQ64933. 1 Publication
Sequence conflicti355 – 3551K → S in AAQ64934. 1 Publication
Sequence conflicti355 – 3551K → S in AAQ64935. 1 Publication
Sequence conflicti355 – 3551K → S in AAQ64936. 1 Publication
Sequence conflicti355 – 3551K → S in AAQ64937. 1 Publication
Sequence conflicti355 – 3551K → S in AAQ64938. 1 Publication
Sequence conflicti602 – 6021V → A in AAQ64933. 1 Publication
Sequence conflicti602 – 6021V → A in AAQ64934. 1 Publication
Sequence conflicti602 – 6021V → A in AAQ64937. 1 Publication
Sequence conflicti602 – 6021V → A in AAQ64938. 1 Publication
Sequence conflicti786 – 7861M → I in ABX00775. 1 Publication
Sequence conflicti825 – 8251A → T in ABX00775. 1 Publication

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_079794.2.
NP_733166.1. NM_170287.2.
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_079794.2.
NP_733166.1. NM_170287.2.
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...

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 ENSGT00710000106753.
InParanoidi P08953.
OrthoDBi EOG761BT1.
PhylomeDBi P08953.

Miscellaneous databases

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

Gene expression databases

Bgeei P08953.

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: July 9, 2014
This is version 162 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

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