P08953 (TOLL_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein toll

Gene names

Name:	Tl
ORF Names:	CG5490

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1097 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.7 Ref.8 Ref.9
Subunit structure	Homodimer; disulfide-linked.
Subcellular location	Cell membrane; Single-pass type I membrane protein.
Developmental stage	Expressed both maternally and zygotically. Ref.1
Sequence similarities	Belongs to the Toll-like receptor family. Contains 18 LRR (leucine-rich) repeats. Contains 2 LRRCT domains. Contains 1 LRRNT domain. Contains 1 TIR domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Toll signaling pathway Non-traceable author statement PubMed 10449356. Source: FlyBase antifungal humoral response Inferred from mutant phenotype Ref.8. Source: FlyBase cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Inferred from mutant phenotype PubMed 14527345. Source: FlyBase defense response to Gram-positive bacterium Traceable author statement PubMed 12888789PubMed 14557290PubMed 15199954. Source: FlyBase heart development Inferred from mutant phenotype PubMed 15870289. Source: FlyBase hemocyte proliferation Inferred from mutant phenotype PubMed 15882582. Source: FlyBase hemopoiesis Traceable author statement PubMed 10793472. Source: FlyBase innate immune response Inferred from direct assay PubMed 18583479. Source: FlyBase positive regulation of antibacterial peptide biosynthetic process Inferred from mutant phenotype PubMed 9405661. Source: FlyBase positive regulation of antifungal peptide biosynthetic process Inferred from mutant phenotype PubMed 10369678PubMed 9405661. Source: FlyBase regulation of hemocyte differentiation Inferred from mutant phenotype PubMed 15381778. Source: FlyBase synapse assembly Inferred from mutant phenotype PubMed 10699982. Source: FlyBase synaptic target inhibition Inferred from mutant phenotype PubMed 20504957. Source: FlyBase zygotic specification of dorsal/ventral axis Non-traceable author statement PubMed 15199954. Source: FlyBase
Cellular_component	ESCRT-0 complex Inferred from direct assay PubMed 20404143. Source: FlyBase external side of plasma membrane Inferred from direct assay PubMed 22464169. Source: FlyBase integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cytokine binding Traceable author statement PubMed 12888789. Source: FlyBase transmembrane signaling receptor activity Non-traceable author statement PubMed 10449356. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Myd88	Q7K105	3	EBI-143610,EBI-129988

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Potential

Chain

28 – 1097

1070

Protein toll

PRO_0000034740

Regions

Topological domain

28 – 807

780

Extracellular Potential

Transmembrane

808 – 828

21

Helical; Potential

Topological domain

829 – 1097

269

Cytoplasmic Potential

Repeat

175 – 195

21

LRR 1

Repeat

198 – 219

22

LRR 2

Repeat

222 – 243

22

LRR 3

Repeat

246 – 267

22

LRR 4

Repeat

270 – 291

22

LRR 5

Repeat

294 – 314

21

LRR 6

Repeat

320 – 340

21

LRR 7

Repeat

343 – 364

22

LRR 8

Repeat

367 – 388

22

LRR 9

Repeat

391 – 412

22

LRR 10

Repeat

415 – 436

22

LRR 11

Repeat

439 – 460

22

LRR 12

Repeat

474 – 495

22

LRR 13

Repeat

498 – 521

24

LRR 14

Repeat

523 – 544

22

LRR 15

Domain

561 – 620

60

LRRCT 1

Domain

622 – 663

42

LRRNT

Repeat

669 – 690

22

LRR 16

Repeat

693 – 713

21

LRR 17

Repeat

715 – 738

24

LRR 18

Domain

751 – 801

51

LRRCT 2

Domain

857 – 996

140

TIR

Amino acid modifications

Glycosylation

80

1

N-linked (GlcNAc...) Potential

Glycosylation

140

1

N-linked (GlcNAc...) Potential

Glycosylation

175

1

N-linked (GlcNAc...) Potential

Glycosylation

235

1

N-linked (GlcNAc...) Potential

Glycosylation

270

1

N-linked (GlcNAc...) Potential

Glycosylation

275

1

N-linked (GlcNAc...) Potential

Glycosylation

346

1

N-linked (GlcNAc...) Potential

Glycosylation

391

1

N-linked (GlcNAc...) Potential

Glycosylation

482

1

N-linked (GlcNAc...) Potential

Glycosylation

508

1

N-linked (GlcNAc...) Potential

Glycosylation

528

1

N-linked (GlcNAc...) Potential

Glycosylation

654

1

N-linked (GlcNAc...) Potential

Glycosylation

677

1

N-linked (GlcNAc...) Potential

Glycosylation

703

1

N-linked (GlcNAc...) Potential

Glycosylation

715

1

N-linked (GlcNAc...) Potential

Glycosylation

730

1

N-linked (GlcNAc...) Potential

Glycosylation

738

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

98

1

E → G in strain: MelZim6.

Natural variant

218

1

G → S in strain: MelZim7.

Natural variant

245

1

T → S in strain: MelZim3.

Natural variant

390

1

T → I in strain: MelZim3 and MelZim7.

Natural variant

414

1

G → A in strain: MelZim3.

Natural variant

435

1

V → L in strain: MelZim8.

Natural variant

460

1

M → T in strain: MelZim6.

Natural variant

471

1

Y → D in strain: MelZim1, MelZim4, MelZim5 and MelZim6.

Natural variant

486

1

I → R in strain: MelZim6.

Natural variant

513

1

G → R in strain: MelZim1, MelZim5 and MelZim6.

Natural variant

538

1

A → E in strain: MelZim1, MelZim5 and MelZim6.

Natural variant

544

1

H → Y in strain: MelZim1, MelZim5 and MelZim6.

Natural variant

568

1

T → M in strain: MelZim1, MelZim5 and MelZim6.

Natural variant

592

1

T → A in strain: MelZim6.

Natural variant

603

1

L → M in strain: MelZim1, MelZim5 and MelZim6.

Natural variant

681

1

L → V in strain: MelZim1, MelZim3, MelZim4, MelZim5, MelZim6 and MelZim7.

Natural variant

714

1

T → I in strain: MelZim5 and MelZim8.

Natural variant

732

1

T → S in strain: MelZim8.

Natural variant

741

1

M → I in strain: MelZim1.

Experimental info

Sequence conflict

355

1

K → S in AAQ64932. Ref.5

Sequence conflict

355

1

K → S in AAQ64933. Ref.5

Sequence conflict

355

1

K → S in AAQ64934. Ref.5

Sequence conflict

355

1

K → S in AAQ64935. Ref.5

Sequence conflict

355

1

K → S in AAQ64936. Ref.5

Sequence conflict

355

1

K → S in AAQ64937. Ref.5

Sequence conflict

355

1

K → S in AAQ64938. Ref.5

Sequence conflict

602

1

V → A in AAQ64933. Ref.5

Sequence conflict

602

1

V → A in AAQ64934. Ref.5

Sequence conflict

602

1

V → A in AAQ64937. Ref.5

Sequence conflict

602

1

V → A in AAQ64938. Ref.5

Sequence conflict

786

1

M → I in ABX00775. Ref.4

Sequence conflict

825

1

A → T in ABX00775. Ref.4

Secondary structure

1

.

.

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.

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1097

Helix Strand Turn

Details...

Helix

31 – 40

10

Beta strand

42 – 48

7

Beta strand

51 – 57

7

Beta strand

64 – 70

7

Turn

71 – 73

3

Beta strand

74 – 79

6

Helix

84 – 89

6

Beta strand

100 – 106

7

Beta strand

111 – 113

3

Helix

116 – 121

6

Beta strand

124 – 126

3

Beta strand

128 – 133

6

Helix

143 – 146

4

Beta strand

153 – 158

6

Turn

167 – 172

6

Beta strand

178 – 183

6

Turn

190 – 195

6

Beta strand

201 – 203

3

Turn

214 – 219

6

Beta strand

225 – 227

3

Sequences

	Sequence		Length	Mass (Da)
	P08953 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: D1BFC42245E3EABE	FASTA	1,097	124,656
	10 20 30 40 50 60 MSRLKAASEL ALLVIILQLL QWPGSEASFG RDACSEMSID GLCQCAPIMS EYEIICPANA 70 80 90 100 110 120 ENPTFRLTIQ PKDYVQIMCN LTDTTDYQQL PKKLRIGEVD RVQMRRCMLP GHTPIASILD 130 140 150 160 170 180 YLGIVSPTTL IFESDNLGMN ITRQHLDRLH GLKRFRFTTR RLTHIPANLL TDMRNLSHLE 190 200 210 220 230 240 LRANIEEMPS HLFDDLENLE SIEFGSNKLR QMPRGIFGKM PKLKQLNLWS NQLHNLTKHD 250 260 270 280 290 300 FEGATSVLGI DIHDNGIEQL PHDVFAHLTN VTDINLSANL FRSLPQGLFD HNKHLNEVRL 310 320 330 340 350 360 MNNRVPLATL PSRLFANQPE LQILRLRAEL QSLPGDLFEH STQITNISLG DNLLKTLPAT 370 380 390 400 410 420 LLEHQVNLLS LDLSNNRLTH LPDSLFAHTT NLTDLRLEDN LLTGISGDIF SNLGNLVTLV 430 440 450 460 470 480 MSRNRLRTID SRAFVSTNGL RHLHLDHNDI DLQQPLLDIM LQTQINSPFG YMHGLLTLNL 490 500 510 520 530 540 RNNSIIFVYN DWKNTMLQLR ELDLSYNNIS SLGYEDLAFL SQNRLHVNMT HNKIRRIALP 550 560 570 580 590 600 EDVHLGEGYN NNLVHVDLND NPLVCDCTIL WFIQLVRGVH KPQYSRQFKL RTDRLVCSQP 610 620 630 640 650 660 NVLEGTPVRQ IEPQTLICPL DFSDDPRERK CPRGCNCHVR TYDKALVINC HSGNLTHVPR 670 680 690 700 710 720 LPNLHKNMQL MELHLENNTL LRLPSANTPG YESVTSLHLA GNNLTSIDVD QLPTNLTHLD 730 740 750 760 770 780 ISWNHLQMLN ATVLGFLNRT MKWRSVKLSG NPWMCDCTAK PLLLFTQDNF ERIGDRNEMM 790 800 810 820 830 840 CVNAEMPTRM VELSTNDICP AEKGVFIALA VVIALTGLLA GFTAALYYKF QTEIKIWLYA 850 860 870 880 890 900 HNLLLWFVTE EDLDKDKKFD AFISYSHKDQ SFIEDYLVPQ LEHGPQKFQL CVHERDWLVG 910 920 930 940 950 960 GHIPENIMRS VADSRRTIIV LSQNFIKSEW ARLEFRAAHR SALNEGRSRI IVIIYSDIGD 970 980 990 1000 1010 1020 VEKLDEELKA YLKMNTYLKW GDPWFWDKLR FALPHRRPVG NIGNGALIKT ALKGSTDDKL 1030 1040 1050 1060 1070 1080 ELIKPSPVTP PLTTPPAEAT KNPLVAQLNG VTPHQAIMIA NGKNGLTNLY TPNGKSHGNG 1090 HINGAFIINT NAKQSDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] 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]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A29943.

RefSeq

NP_524518.1. NM_079794.2.
NP_733166.1. NM_170287.2.

UniGene

Dm.2347.

3D structure databases

PDBe
RCSB PDB
PDBj

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	28-233	[»]

ProteinModelPortal

P08953.

SMR

P08953. Positions 123-993.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34358N.

IntAct

P08953. 3 interactions.

STRING

7227.FBpp0084431.

Proteomic databases

PaxDb

P08953.

PRIDE

P08953.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0085059; FBpp0084431; FBgn0262473.
FBtr0330155; FBpp0303188; FBgn0262473.

GeneID

43222.

KEGG

dme:Dmel_CG5490.

Organism-specific databases

CTD

109651.

FlyBase

FBgn0262473. Tl.

Phylogenomic databases

eggNOG

COG4886.

GeneTree

ENSGT00700000104286.

InParanoid

P08953.

OMA

STNDICP.

OrthoDB

EOG4SF7MS.

PhylomeDB

P08953.

Gene expression databases

Bgee

P08953.

GermOnline

CG5490. Drosophila melanogaster.

Family and domain databases

InterPro

IPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR000157. TIR_dom.
IPR027202. Toll.
[Graphical view]

PANTHER

PTHR24371:SF0. PTHR24371:SF0. 1 hit.

Pfam

PF00560. LRR_1. 2 hits.
PF01462. LRRNT. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]

SMART

SM00369. LRR_TYP. 3 hits.
SM00082. LRRCT. 2 hits.
SM00013. LRRNT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]

SUPFAM

SSF52200. TIR. 1 hit.

PROSITE

PS51450. LRR. 13 hits.
PS50104. TIR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

Tl. drosophila.

GenomeRNAi

43222.

NextBio

832799.

Entry information

Entry name

TOLL_DROME

Accession

Primary (citable) accession number: P08953
Secondary accession number(s): A4V3G7 , A8WHK7, Q8MRF3, Q9VBB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	May 29, 2013
This is version 150 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project