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P08953

- TOLL_DROME

UniProt

P08953 - TOLL_DROME

Protein

Protein toll

Gene

Tl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    4. TIR domain binding Source: FlyBase
    5. 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

    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

    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.

    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.
    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

    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_079794.2.
    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...
    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 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

    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 1, 2014
    This is version 163 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