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Toll-like receptor 7
TOLL7_DROME Reviewed; 1446 AA.
Q7KIN0; E1NZA7; Q2XXU8;
06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 1.
28-MAR-2018, entry version 121.
RecName: Full=Toll-like receptor 7 {ECO:0000305};
Flags: Precursor;
Name=Toll-7 {ECO:0000312|FlyBase:FBgn0034476};
ORFNames=CG8595 {ECO:0000312|FlyBase:FBgn0034476};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
[1] {ECO:0000312|EMBL:AAF86225.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=10973475; DOI=10.1073/pnas.180130797;
Tauszig S., Jouanguy E., Hoffmann J.A., Imler J.L.;
"Toll-related receptors and the control of antimicrobial peptide
expression in Drosophila.";
Proc. Natl. Acad. Sci. U.S.A. 97:10520-10525(2000).
[2] {ECO:0000312|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000312|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000312|EMBL:ABA86520.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-1435.
STRAIN=Ral1 {ECO:0000312|EMBL:ABA86520.1};
PubMed=16120803; DOI=10.1093/molbev/msi246;
Comeron J.M., Guthrie T.B.;
"Intragenic Hill-Robertson interference influences selection intensity
on synonymous mutations in Drosophila.";
Mol. Biol. Evol. 22:2519-2530(2005).
[5] {ECO:0000312|EMBL:ADN32842.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-1031.
Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305}
DEVELOPMENTAL STAGE.
PubMed=12617819; DOI=10.1016/S1567-133X(02)00020-0;
Kambris Z., Hoffmann J.A., Imler J.L., Capovilla M.;
"Tissue and stage-specific expression of the Tolls in Drosophila
embryos.";
Gene Expr. Patterns 2:311-317(2002).
[7] {ECO:0000305}
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=21158756; DOI=10.1111/j.1440-169X.2010.01213.x;
Yagi Y., Nishida Y., Ip Y.T.;
"Functional analysis of Toll-related genes in Drosophila.";
Dev. Growth Differ. 52:771-783(2010).
[8] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY VIRAL INFECTION, AND
DISRUPTION PHENOTYPE.
PubMed=22464169; DOI=10.1016/j.immuni.2012.03.003;
Nakamoto M., Moy R.H., Xu J., Bambina S., Yasunaga A., Shelly S.S.,
Gold B., Cherry S.;
"Virus recognition by Toll-7 activates antiviral autophagy in
Drosophila.";
Immunity 36:658-667(2012).
[9] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=23892553; DOI=10.1038/nn.3474;
McIlroy G., Foldi I., Aurikko J., Wentzell J.S., Lim M.A.,
Fenton J.C., Gay N.J., Hidalgo A.;
"Toll-6 and Toll-7 function as neurotrophin receptors in the
Drosophila melanogaster CNS.";
Nat. Neurosci. 16:1248-1256(2013).
[10] {ECO:0000305}
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=25741726; DOI=10.1016/j.neuron.2015.02.003;
Ward A., Hong W., Favaloro V., Luo L.;
"Toll receptors instruct axon and dendrite targeting and participate
in synaptic partner matching in a Drosophila olfactory circuit.";
Neuron 85:1013-1028(2015).
-!- FUNCTION: Toll-related receptor which binds to the neurotrophins
NT1 and spz5 (PubMed:10973475, PubMed:23892553). Essential for
antiviral autophagy, it detects and binds to the vesicular
stomatitis virus (vsv) following infection (PubMed:22464169). This
role is likely to be independent of the canonical Toll, immune
deficiency, and JAK-STAT signaling pathways (PubMed:22464169).
Functions in olfactory circuit assembly by promoting synaptic
partner matching between olfactory receptor neurons (ORN) axons
and projection neurons (PN) dendrites partners in the antennal
lobe (PubMed:25741726). Function in the Va1d ORNs is necessary and
sufficient for correct targeting to their partner PN dendrites
(PubMed:25741726). Also involved in the targeting of other classes
of ORN axons (PubMed:25741726). Functions with Toll-6 to regulate
motor axon targeting and neuronal survival in the central nervous
system (CNS) (PubMed:23892553). May be an upstream component of
the NF-kappa-B (rel) regulatory cascade (PubMed:23892553).
{ECO:0000269|PubMed:10973475, ECO:0000269|PubMed:22464169,
ECO:0000269|PubMed:23892553, ECO:0000269|PubMed:25741726}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22464169};
Single-pass type I membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in the fan-shaped body and the
ellipsoid body, which are components of the locomotion center in
the CNS (at protein level) (PubMed:23892553).
{ECO:0000269|PubMed:23892553}.
-!- DEVELOPMENTAL STAGE: In embryos, expressed in the ventral neurons,
motor neurons and in the longitudinal interneuron axons (at
protein level) (PubMed:23892553). May also be expressed in the
motor neuron dendrites or possibly the glia (at protein level)
(PubMed:23892553). Expressed 48 hours after puparium formation in
the lateral glomeruli of the anterior and central regions of the
antennal lobe, including the DA1, VA1d and VA1v glomeruli (at
protein level) (PubMed:25741726). Expressed zygotically
(PubMed:12617819). High levels of expression in embryos and pupae,
and relatively low levels of expression in larvae and adults
(PubMed:10973475). At germ band extension, expressed as 14 stripes
in the embryo (PubMed:12617819). At germ band retraction,
expressed in a subset of neurons in the CNS, the precursors of the
leg imaginal disks and in the ventral epithelium of the large
intestine (PubMed:12617819). Expressed in the posterior and
anterior spiracles (PubMed:12617819). In stage 16 embryos,
expression decreases and is mainly localized to the CNS
(PubMed:12617819). Expressed in the proximal region of the wing
imaginal disks, around the wing pouch and hinge regions
(PubMed:21158756). Also expressed in the distal segments of the
leg imaginal disks, with high levels of expression around the A-P
border of the tarsal to tibia segments (PubMed:21158756). In
larvae, detected in the fat body (PubMed:12617819).
{ECO:0000269|PubMed:10973475, ECO:0000269|PubMed:12617819,
ECO:0000269|PubMed:21158756, ECO:0000269|PubMed:23892553,
ECO:0000269|PubMed:25741726}.
-!- INDUCTION: Up-regulated during vesicular stomatitis virus (VSV)
infection. {ECO:0000269|PubMed:22464169}.
-!- DISRUPTION PHENOTYPE: Mistargeting of VA1d ORN axons to a medial
position (PubMed:25741726). No effect on the immune response to
septic injury using a mixture of Gram-positive and Gram-negative
bacteria; adults are able induce expression of antibacterial
peptide genes (Drs, AttA, DptA and Mtk) and mount a proper innate
immune response (PubMed:21158756). RNAi-mediated knockdown results
in adults that are acutely sensitive to the vesicular stomatitis
virus (vsv) (PubMed:22464169). Following infection with vsv adult
survival is decreased, and adults show a dramatic increase in
viral RNA production 6 days post vsv infection and viral
replication 9 days post infection (PubMed:22464169). Reduced
autophagy in adult fat body cells following vsv infection
(PubMed:22464169). Starvation-induced autophagy is not affected
(PubMed:22464169). {ECO:0000269|PubMed:21158756,
ECO:0000269|PubMed:22464169, ECO:0000269|PubMed:25741726}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
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EMBL; AF247765; AAF86225.1; -; mRNA.
EMBL; DQ138914; ABA86520.1; -; Genomic_DNA.
EMBL; AE013599; AAF57514.1; -; Genomic_DNA.
EMBL; BT125656; ADN32842.1; -; mRNA.
RefSeq; NP_523797.1; NM_079073.3.
UniGene; Dm.2660; -.
ProteinModelPortal; Q7KIN0; -.
IntAct; Q7KIN0; 1.
STRING; 7227.FBpp0085638; -.
PaxDb; Q7KIN0; -.
PRIDE; Q7KIN0; -.
EnsemblMetazoa; FBtr0086336; FBpp0085638; FBgn0034476.
GeneID; 37272; -.
KEGG; dme:Dmel_CG8595; -.
UCSC; CG8595-RA; d. melanogaster.
CTD; 37272; -.
FlyBase; FBgn0034476; Toll-7.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000118777; -.
OMA; NHAFIGR; -.
OrthoDB; EOG091G0137; -.
PhylomeDB; Q7KIN0; -.
GenomeRNAi; 37272; -.
PRO; PR:Q7KIN0; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0034476; -.
ExpressionAtlas; Q7KIN0; differential.
GO; GO:0009897; C:external side of plasma membrane; IDA:FlyBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005030; F:neurotrophin receptor activity; IMP:FlyBase.
GO; GO:0008329; F:signaling pattern recognition receptor activity; IC:FlyBase.
GO; GO:0046790; F:virion binding; IDA:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IC:FlyBase.
GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0010508; P:positive regulation of autophagy; IMP:FlyBase.
GO; GO:0050688; P:regulation of defense response to virus; IMP:FlyBase.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 5.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
Pfam; PF00560; LRR_1; 1.
Pfam; PF13855; LRR_8; 5.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 20.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 23.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Developmental protein;
Disulfide bond; Immunity; Innate immunity; Leucine-rich repeat;
Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 1446 Toll-like receptor 7.
/FTId=PRO_5006489795.
TOPO_DOM 17 1049 Extracellular. {ECO:0000305}.
TRANSMEM 1050 1070 Helical. {ECO:0000255}.
TOPO_DOM 1071 1446 Cytoplasmic. {ECO:0000305}.
REPEAT 133 156 LRR 1. {ECO:0000255}.
REPEAT 158 180 LRR 2. {ECO:0000255}.
REPEAT 188 211 LRR 3. {ECO:0000255}.
REPEAT 213 235 LRR 4. {ECO:0000255}.
REPEAT 246 270 LRR 5. {ECO:0000255}.
REPEAT 271 294 LRR 6. {ECO:0000255}.
REPEAT 295 318 LRR 7. {ECO:0000255}.
REPEAT 320 342 LRR 8. {ECO:0000255}.
REPEAT 344 368 LRR 9. {ECO:0000255}.
REPEAT 369 392 LRR 10. {ECO:0000255}.
REPEAT 393 416 LRR 11. {ECO:0000255}.
REPEAT 417 440 LRR 12. {ECO:0000255}.
REPEAT 442 464 LRR 13. {ECO:0000255}.
REPEAT 465 488 LRR 14. {ECO:0000255}.
REPEAT 489 511 LRR 15. {ECO:0000255}.
REPEAT 513 535 LRR 16. {ECO:0000255}.
REPEAT 536 559 LRR 17. {ECO:0000255}.
REPEAT 561 582 LRR 18. {ECO:0000255}.
REPEAT 584 605 LRR 19. {ECO:0000255}.
REPEAT 606 629 LRR 20. {ECO:0000255}.
REPEAT 631 652 LRR 21. {ECO:0000255}.
REPEAT 653 675 LRR 22. {ECO:0000255}.
REPEAT 677 699 LRR 23. {ECO:0000255}.
DOMAIN 716 773 LRRCT. {ECO:0000255}.
REPEAT 828 851 LRR 24. {ECO:0000255}.
REPEAT 852 875 LRR 25. {ECO:0000255}.
REPEAT 876 899 LRR 26. {ECO:0000255}.
REPEAT 900 923 LRR 27. {ECO:0000255}.
REPEAT 925 947 LRR 28. {ECO:0000255}.
REPEAT 951 979 LRR 29. {ECO:0000255}.
DOMAIN 1096 1236 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
DISULFID 722 772 {ECO:0000250|UniProtKB:P08953}.
DISULFID 796 802 {ECO:0000250|UniProtKB:P08953}.
DISULFID 800 815 {ECO:0000250|UniProtKB:P08953}.
DISULFID 966 993 {ECO:0000250|UniProtKB:P08953}.
CONFLICT 58 58 P -> L (in Ref. 4; ABA86520).
{ECO:0000305}.
CONFLICT 124 124 T -> K (in Ref. 4; ABA86520).
{ECO:0000305}.
CONFLICT 1426 1426 Missing (in Ref. 4; ABA86520).
{ECO:0000305}.
SEQUENCE 1446 AA; 160950 MW; 80D281BDA9500ABC CRC64;
MAAILLLLLG FSWSLAVESA LAPKESESSA SAMLGAGTGA AATVSLSGDY SSLLSNVPAA
SPVPANPSQP SGPANQCSWS YNGTSSVHCA LRLIERQPGL DLQGADGSSQ LTIQCSELYL
FESTLPVAVF ARLQTLEALR LDSCKLLQLP NNAFEGLATL KSLRLSTHNS EWGPTRTLEL
FPDSLGGLKQ LTDLDLGDNN LRQLPSGFLC PVGNLQVLNL TRNRIRTAEQ MGFADMNCGA
GSGSAGSELQ VLDASHNELR SISESWGISR LRRLQHLNLA YNNLSELSGE ALAGLASLRI
VNLSNNHLET LPEGLFAGSK ELREIHLQQN ELYELPKGLF HRLEQLLVVD LSGNQLTSNH
VDNTTFAGLI RLIVLNLAHN ALTRIDYRTF KELYFLQILN LRNNSIGHIE DNAFLPLYNL
HTLNLAENRL HTLDDKLFNG LYVLSKLTLN NNLISVVEPA VFKNCSDLKE LDLSSNQLNE
VPRALQDLAM LRTLDLGENQ IRTFDNQSFK NLHQLTGLRL IDNQIGNITV GMFQDLPRLS
VLNLAKNRIQ SIERGSFDKN FELEAIRLDR NFLADINGVF ATLVSLLWLN LSENHLVWFD
YAFIPSNLKW LDIHGNYIEA LGNYYKLQEE IRVKTLDASH NRITEIGPMS IPNTIELLFI
NNNLIGNVQP NAFVDKANLA RVDLYANQLS KLQLQQLRVA PVVAPKPLPE FYLGGNPFEC
DCTMDWLQRI NNLTTRQHPR VMDMANIECV MPHARGAAVR PLSGLRPQDF LCRYESHCFA
LCHCCDFDAC DCEMTCPSNC TCYHDQIWST NVVDCGGQQT TELPRRVPMD SSVVYLDGNN
FPVLKNHAFI GRKNLRALYV NGSQVAAIQN RTFASLASLQ LLHLADNKLR TLHGYEFEQL
SALRELYLQN NQLTTIENAT LAPLAALELI RIDGNRLVTL PIWQMHATHF GTRLKSISLG
RNQWSCRCQF LQALTSYVAD NALIVQDAQD IYCMAASSGT GSAALEDSSS NSGSLEKREL
DFNATGAACT DYYSGGSMLQ HGIPESYIPL LAAALALLFL LVVIAMVFAF RESLRIWLFA
HYGVRVFGPR CEESEKLYDA VLLHSAKDSE FVCQHLAAQL ETGRPPLRVC LQHRDLAHDA
THYQLLEATR VSRRVVILLT RNFLQTEWAR CELRRSVHDA LRGRPQKLVI IEEPEVAFEA
ESDIELLPYL KTSAVHRIRR SDRHFWEKLR YALPVDYPTF RGNNYTLELD HHNHERVKQP
ASPGLLYRQA PPPAYCGPAD AVGIGAVPQV VPVNASVPAE QNYSTATTAT PSPRPQRRGE
QPGSGSGGNH HLHAQYYQHH GMRPPSEHIY SSIDSDYSTL DNEQHMLMMP GAPGGLAMEA
AQRAQTWRPK REQLHLQQAQ AGTLGSKASQ AAHQQQQQQQ QQQQQQPNPT AVSGQQQGPH
VQAYLV
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Pathways :
WP1067: Toll-like receptor signaling pathway
WP1183: Toll-like receptor signaling pathway
WP1271: Toll-like receptor signaling pathway
WP1309: Toll-like receptor signaling pathway
WP1345: T Cell Receptor Signaling Pathway
WP1384: Toll-like receptor signaling pathway
WP1449: Regulation of toll-like receptor signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP75: Toll-like receptor signaling pathway
WP829: Toll-like receptor signaling pathway
WP88: Toll Like Receptor signaling
WP949: Toll-like receptor signaling pathway
WP1004: Kit Receptor Signaling Pathway
WP1011: T Cell Receptor Signaling Pathway
WP1014: Androgen receptor signaling pathway
WP1025: B Cell Receptor Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1112: EPO Receptor Signaling
WP1121: Kit Receptor Signaling Pathway
WP1130: T Cell Receptor Signaling Pathway
WP1133: Androgen receptor signaling pathway
WP1144: B Cell Receptor Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP1162: Signaling of Hepatocyte Growth Factor Receptor
Related Genes :
[TLR2 TIL4] Toll-like receptor 2 (Toll/interleukin-1 receptor-like protein 4) (CD antigen CD282)
[TLR1 KIAA0012] Toll-like receptor 1 (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)
[Tlr1] Toll-like receptor 1 (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)
[TICAM2 TIRAP3 TIRP TRAM] TIR domain-containing adapter molecule 2 (TICAM-2) (Putative NF-kappa-B-activating protein 502) (TRIF-related adapter molecule) (Toll-like receptor adaptor protein 3) (Toll/interleukin-1 receptor domain-containing protein) (MyD88-4)
[Tlr4] Toll-like receptor 4 (Toll4) (CD antigen CD284)
[TLR5 TIL3] Toll-like receptor 5 (Toll/interleukin-1 receptor-like protein 3)
[Toll-7 CG8595] Toll-like receptor 7
[TLR4] Toll-like receptor 4 (hToll) (CD antigen CD284)
[Tlr2] Toll-like receptor 2 (CD antigen CD282)
[TLR6] Toll-like receptor 6 (CD antigen CD286)
[Tlr9] Toll-like receptor 9 (CD antigen CD289)
[TLR9 UNQ5798/PRO19605] Toll-like receptor 9 (CD antigen CD289)
[Tlr4 Lps] Toll-like receptor 4 (CD antigen CD284)
[Tlr6] Toll-like receptor 6 (CD antigen CD286)
[TLR2] Toll-like receptor 2 (CD antigen CD282)
[TLR2] Toll-like receptor 2 (CD antigen CD282)
[TLR6] Toll-like receptor 6 (CD antigen CD286)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[TICAM1 PRVTIRB TRIF] TIR domain-containing adapter molecule 1 (TICAM-1) (Proline-rich, vinculin and TIR domain-containing protein B) (Putative NF-kappa-B-activating protein 502H) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (MyD88-3) (TIR domain-containing adapter protein inducing IFN-beta)
[TLR8 UNQ249/PRO286] Toll-like receptor 8 (CD antigen CD288)
[TLR7 UNQ248/PRO285] Toll-like receptor 7
[Tlr8] Toll-like receptor 8 (CD antigen CD288)
[TLR4] Toll-like receptor 4 (CD antigen CD284)
[Tlr7] Toll-like receptor 7
[TLR3] Toll-like receptor 3 (CD antigen CD283)
[TIRAP MAL] Toll/interleukin-1 receptor domain-containing adapter protein (TIR domain-containing adapter protein) (Adaptor protein Wyatt) (MyD88 adapter-like protein) (MyD88-2)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[Toll-6 Tl-6 CG7250] Toll-like receptor 6
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