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Toll-like receptor 5 (Toll/interleukin-1 receptor-like protein 3)

 TLR5_HUMAN              Reviewed;         858 AA.
O60602; B1AZ05; B3Y633; B9VJ63; D1CS80; D3DTB8; O15456; Q32MI2; Q32MI3;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 4.
11-DEC-2019, entry version 178.
RecName: Full=Toll-like receptor 5;
AltName: Full=Toll/interleukin-1 receptor-like protein 3;
Flags: Precursor;
Name=TLR5; Synonyms=TIL3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-616 AND LEU-822.
TISSUE=Leukocyte, and Prostate;
PubMed=9596645;
Chaudhary P.M., Ferguson C., Nguyen V., Nguyen O., Massa H.F., Eby M.,
Jasmin A., Trask B.J., Hood L., Nelson P.S.;
"Cloning and characterization of two Toll/Interleukin-1 receptor-like genes
TIL3 and TIL4: evidence for a multi-gene receptor family in humans.";
Blood 91:4020-4027(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-822.
TISSUE=Macrophage;
Seya T., Tsukada H.;
"Homo sapiens TLR5.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-822.
PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.;
"Natural selection in the TLR-related genes in the course of primate
evolution.";
Immunogenetics 60:727-735(2008).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-822.
PubMed=19179655; DOI=10.1093/molbev/msp018;
Wlasiuk G., Khan S., Switzer W.M., Nachman M.W.;
"A history of recurrent positive selection at the toll-like receptor 5 in
primates.";
Mol. Biol. Evol. 26:937-949(2009).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-644 AND LEU-822.
PubMed=19924287; DOI=10.1371/journal.pone.0007803;
Georgel P., Macquin C., Bahram S.;
"The heterogeneous allelic repertoire of human Toll-Like receptor (TLR)
genes.";
PLoS ONE 4:E7803-E7803(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-822.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-822.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 494-858, AND VARIANT LEU-822.
TISSUE=CNS;
PubMed=9435236; DOI=10.1073/pnas.95.2.588;
Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F.;
"A family of human receptors structurally related to Drosophila Toll.";
Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998).
[10]
PROTEIN SEQUENCE OF 21-35.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified
cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[11]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=11489966; DOI=10.4049/jimmunol.167.4.1882;
Gewirtz A.T., Navas T.A., Lyons S., Godowski P.J., Madara J.L.;
"Cutting edge: bacterial flagellin activates basolaterally expressed TLR5
to induce epithelial proinflammatory gene expression.";
J. Immunol. 167:1882-1885(2001).
[12]
FUNCTION.
PubMed=11323673; DOI=10.1038/35074106;
Hayashi F., Smith K.D., Ozinsky A., Hawn T.R., Yi E.C., Goodlett D.R.,
Eng J.K., Akira S., Underhill D.M., Aderem A.;
"The innate immune response to bacterial flagellin is mediated by Toll-like
receptor 5.";
Nature 410:1099-1103(2001).
[13]
ASSOCIATION WITH RESISTANCE TO SLEB1, AND VARIANTS SER-592 AND LEU-616.
PubMed=16027372; DOI=10.1073/pnas.0501165102;
Hawn T.R., Wu H., Grossman J.M., Hahn B.H., Tsao B.P., Aderem A.;
"A stop codon polymorphism of Toll-like receptor 5 is associated with
resistance to systemic lupus erythematosus.";
Proc. Natl. Acad. Sci. U.S.A. 102:10593-10597(2005).
[14]
PHOSPHORYLATION AT TYR-798.
PubMed=17157808; DOI=10.1016/j.bbrc.2006.11.132;
Ivison S.M., Khan M.A., Graham N.R., Bernales C.Q., Kaleem A.,
Tirling C.O., Cherkasov A., Steiner T.S.;
"A phosphorylation site in the Toll-like receptor 5 TIR domain is required
for inflammatory signalling in response to flagellin.";
Biochem. Biophys. Res. Commun. 352:936-941(2007).
[15]
PHOSPHORYLATION AT SER-805.
PubMed=17442957; DOI=10.4049/jimmunol.178.9.5735;
Ivison S.M., Graham N.R., Bernales C.Q., Kifayet A., Ng N., Shobab L.A.,
Steiner T.S.;
"Protein kinase D interaction with TLR5 is required for inflammatory
signaling in response to bacterial flagellin.";
J. Immunol. 178:5735-5743(2007).
[16]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18490781; DOI=10.4049/jimmunol.180.11.7764;
Blohmke C.J., Victor R.E., Hirschfeld A.F., Elias I.M., Hancock D.G.,
Lane C.R., Davidson A.G., Wilcox P.G., Smith K.D., Overhage J.,
Hancock R.E., Turvey S.E.;
"Innate immunity mediated by TLR5 as a novel antiinflammatory target for
cystic fibrosis lung disease.";
J. Immunol. 180:7764-7773(2008).
[17]
FUNCTION, INTERACTION WITH TICAM1 AND MYD88, AND SUBCELLULAR LOCATION.
PubMed=20855887; DOI=10.1074/jbc.m110.158394;
Choi Y.J., Im E., Chung H.K., Pothoulakis C., Rhee S.H.;
"TRIF mediates Toll-like receptor 5-induced signaling in intestinal
epithelial cells.";
J. Biol. Chem. 285:37570-37578(2010).
[18]
POLYMORPHISM, AND INVOLVEMENT IN RESISTANCE TO MELIOIDOSIS.
PubMed=23447684; DOI=10.4049/jimmunol.1202974;
West T.E., Chantratita N., Chierakul W., Limmathurotsakul D.,
Wuthiekanun V., Myers N.D., Emond M.J., Wurfel M.M., Hawn T.R.,
Peacock S.J., Skerrett S.J.;
"Impaired TLR5 functionality is associated with survival in melioidosis.";
J. Immunol. 190:3373-3379(2013).
[19]
INTERACTION WITH UNC93B1, AND SUBCELLULAR LOCATION.
PubMed=24778236; DOI=10.1073/pnas.1322838111;
Huh J.W., Shibata T., Hwang M., Kwon E.H., Jang M.S., Fukui R., Kanno A.,
Jung D.J., Jang M.H., Miyake K., Kim Y.M.;
"UNC93B1 is essential for the plasma membrane localization and signaling of
Toll-like receptor 5.";
Proc. Natl. Acad. Sci. U.S.A. 111:7072-7077(2014).
[20]
FUNCTION.
PubMed=29934223; DOI=10.1016/j.ijmm.2018.06.004;
Bielaszewska M., Marejkova M., Bauwens A., Kunsmann-Prokscha L.,
Mellmann A., Karch H.;
"Enterohemorrhagic Escherichia coli O157 outer membrane vesicles induce
interleukin 8 production in human intestinal epithelial cells by signaling
via Toll-like receptors TLR4 and TLR5 and activation of the nuclear factor
NF-kappaB.";
Int. J. Med. Microbiol. 308:882-889(2018).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (26.0 ANGSTROMS) OF 23-858, GLYCOSYLATION
AT ASN-37; ASN-46; ASN-245; ASN-342; ASN-422; ASN-595 AND ASN-598,
DISULFIDE BONDS, LRR REPEATS, AND SUBUNIT.
PubMed=22173220; DOI=10.1016/j.jsb.2011.12.002;
Zhou K., Kanai R., Lee P., Wang H.W., Modis Y.;
"Toll-like receptor 5 forms asymmetric dimers in the absence of
flagellin.";
J. Struct. Biol. 177:402-409(2012).
[22]
VARIANTS 392-ARG--SER-858 DEL; SER-592 AND LEU-616.
PubMed=14623910; DOI=10.1084/jem.20031220;
Hawn T.R., Verbon A., Lettinga K.D., Zhao L.P., Li S.S., Laws R.J.,
Skerrett S.J., Beutler B., Schroeder L., Nachman A., Ozinsky A.,
Smith K.D., Aderem A.;
"A common dominant TLR5 stop codon polymorphism abolishes flagellin
signaling and is associated with susceptibility to legionnaires' disease.";
J. Exp. Med. 198:1563-1572(2003).
-!- FUNCTION: Pattern recognition receptor (PRR) located on the cell
surface that participates in the activation of innate immunity and
inflammatory response (PubMed:11323673, PubMed:18490781). Recognizes
small molecular motifs named pathogen-associated molecular pattern
(PAMPs) expressed by pathogens and microbe-associated molecular
patterns (MAMPs) usually expressed by resident microbiota
(PubMed:29934223). Upon ligand binding such as bacterial flagellins,
recruits intracellular adapter proteins MYD88 and TRIF leading to NF-
kappa-B activation, cytokine secretion and induction of the
inflammatory response (PubMed:20855887, PubMed:11489966). Plays thereby
an important role in the relationship between the intestinal epithelium
and enteric microbes and contributes to the gut microbiota composition
throughout life (By similarity). {ECO:0000250|UniProtKB:Q9JLF7,
ECO:0000269|PubMed:11323673, ECO:0000269|PubMed:11489966,
ECO:0000269|PubMed:18490781, ECO:0000269|PubMed:20855887,
ECO:0000269|PubMed:29934223}.
-!- SUBUNIT: Homodimer (PubMed:22173220). Interacts with MYD88 (via TIR
domain) (PubMed:20855887). Interacts with TICAM1 (via TIR domain)
(PubMed:20855887). Interacts with UNC93B1; this interaction is
essential for proper TLR5 localization to the plasma membrane
(PubMed:24778236). {ECO:0000269|PubMed:20855887,
ECO:0000269|PubMed:22173220, ECO:0000269|PubMed:24778236}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24778236};
Single-pass type I membrane protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Highly expressed on the basolateral surface of
intestinal epithelia (PubMed:11489966). Expressed also in other cells
such as lung epithelial cells (PubMed:11489966, PubMed:18490781).
{ECO:0000269|PubMed:11489966, ECO:0000269|PubMed:18490781}.
-!- PTM: Phosphorylated at Ser-805 by PKD/PRKD1; phosphorylation induces
the production of inflammatory cytokines. {ECO:0000269|PubMed:17157808,
ECO:0000269|PubMed:17442957}.
-!- PTM: Phosphorylated at Tyr-798 upon flagellin binding; required for
signaling. {ECO:0000269|PubMed:17157808, ECO:0000269|PubMed:17442957}.
-!- POLYMORPHISM: Individuals with a common stop codon polymorphism in
position 392 are unable to mediate flagellin signaling. This
polymorphism acts in a dominant fashion and is associated with
susceptibility to pneumonia caused by Legionella pneumophila
[MIM:608556]. It also provides protection against systemic lupus
erythematosus.
-!- POLYMORPHISM: A nonsense TLR5 polymorphism, resulting in p.Arg392Ter,
confers resistance to melioidosis [MIM:615557], an infection caused by
the Gram-negative, flagellated soil saprophyte Burkholderia
pseudomallei. Carriers of this hypofunctional TLR5 variant may generate
impaired inflammatory responses during melioidosis infection that
result in reduced organ failure and lower mortality.
-!- DISEASE: Systemic lupus erythematosus 1 (SLEB1) [MIM:601744]: A
chronic, relapsing, inflammatory, and often febrile multisystemic
disorder of connective tissue, characterized principally by involvement
of the skin, joints, kidneys and serosal membranes. It is of unknown
etiology, but is thought to represent a failure of the regulatory
mechanisms of the autoimmune system. The disease is marked by a wide
range of system dysfunctions, an elevated erythrocyte sedimentation
rate, and the formation of LE cells in the blood or bone marrow.
Note=Disease susceptibility is associated with variations affecting the
gene represented in this entry.
-!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
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EMBL; AF051151; AAC34376.1; -; mRNA.
EMBL; AB060695; BAB43955.1; -; mRNA.
EMBL; AB445645; BAG55042.1; -; mRNA.
EMBL; FJ556976; ACM69019.1; -; Genomic_DNA.
EMBL; FJ556977; ACM69020.1; -; Genomic_DNA.
EMBL; FJ556979; ACM69022.1; -; Genomic_DNA.
EMBL; FJ556980; ACM69023.1; -; Genomic_DNA.
EMBL; FJ556987; ACM69030.1; -; Genomic_DNA.
EMBL; FJ556989; ACM69032.1; -; Genomic_DNA.
EMBL; DQ026408; AAZ17463.1; -; Genomic_DNA.
EMBL; DQ026409; AAZ17464.1; -; Genomic_DNA.
EMBL; DQ026415; AAZ17469.1; -; Genomic_DNA.
EMBL; AL929091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471100; EAW93262.1; -; Genomic_DNA.
EMBL; CH471100; EAW93263.1; -; Genomic_DNA.
EMBL; BC109118; AAI09119.1; -; mRNA.
EMBL; BC109119; AAI09120.1; -; mRNA.
EMBL; U88881; AAC34136.1; -; mRNA.
CCDS; CCDS31033.1; -.
RefSeq; NP_003259.2; NM_003268.5.
RefSeq; XP_005273298.2; XM_005273241.4.
RefSeq; XP_005273299.2; XM_005273242.4.
RefSeq; XP_005273300.2; XM_005273243.4.
RefSeq; XP_006711567.1; XM_006711504.3.
RefSeq; XP_006711568.1; XM_006711505.3.
RefSeq; XP_006711569.1; XM_006711506.3.
RefSeq; XP_011508239.1; XM_011509937.2.
RefSeq; XP_016857697.1; XM_017002208.1.
PDB; 1P95; Model; -; B=551-560.
PDB; 3J0A; EM; 26.00 A; A/B=23-858.
PDBsum; 1P95; -.
PDBsum; 3J0A; -.
SMR; O60602; -.
BioGrid; 112955; 13.
IntAct; O60602; 20.
MINT; O60602; -.
STRING; 9606.ENSP00000440643; -.
ChEMBL; CHEMBL2176839; -.
iPTMnet; O60602; -.
PhosphoSitePlus; O60602; -.
BioMuta; TLR5; -.
jPOST; O60602; -.
MassIVE; O60602; -.
PaxDb; O60602; -.
PeptideAtlas; O60602; -.
PRIDE; O60602; -.
ProteomicsDB; 49480; -.
DNASU; 7100; -.
Ensembl; ENST00000366881; ENSP00000355846; ENSG00000187554.
Ensembl; ENST00000540964; ENSP00000440643; ENSG00000187554.
GeneID; 7100; -.
KEGG; hsa:7100; -.
UCSC; uc001hnw.3; human.
CTD; 7100; -.
DisGeNET; 7100; -.
EuPathDB; HostDB:ENSG00000187554.11; -.
GeneCards; TLR5; -.
HGNC; HGNC:11851; TLR5.
HPA; CAB009013; -.
MalaCards; TLR5; -.
MIM; 109100; phenotype.
MIM; 601744; phenotype.
MIM; 603031; gene.
MIM; 608556; phenotype.
MIM; 615557; phenotype.
neXtProt; NX_O60602; -.
PharmGKB; PA36553; -.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000008675; -.
InParanoid; O60602; -.
KO; K10168; -.
OrthoDB; 282372at2759; -.
PhylomeDB; O60602; -.
TreeFam; TF351113; -.
Reactome; R-HSA-168176; Toll Like Receptor 5 (TLR5) Cascade.
Reactome; R-HSA-5602680; MyD88 deficiency (TLR5).
Reactome; R-HSA-5603037; IRAK4 deficiency (TLR5).
Reactome; R-HSA-975871; MyD88 cascade initiated on plasma membrane.
SIGNOR; O60602; -.
GeneWiki; TLR_5; -.
GenomeRNAi; 7100; -.
Pharos; O60602; Tbio.
PRO; PR:O60602; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; O60602; protein.
Bgee; ENSG00000187554; Expressed in 188 organ(s), highest expression level in blood.
ExpressionAtlas; O60602; baseline and differential.
Genevisible; O60602; HS.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005149; F:interleukin-1 receptor binding; IPI:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:0034123; P:positive regulation of toll-like receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0050707; P:regulation of cytokine secretion; IEA:InterPro.
GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome.
GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 3.
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; IPR027176; TLR5.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR24365:SF525; PTHR24365:SF525; 1.
Pfam; PF13855; LRR_8; 5.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 9.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 12.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunity; Inflammatory response; Innate immunity;
Leucine-rich repeat; Membrane; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Systemic lupus erythematosus;
Transmembrane; Transmembrane helix.
SIGNAL 1..20
/evidence="ECO:0000269|PubMed:15340161"
CHAIN 21..858
/note="Toll-like receptor 5"
/id="PRO_0000034729"
TOPO_DOM 21..639
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 640..660
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 661..858
/note="Cytoplasmic"
/evidence="ECO:0000255"
REPEAT 45..68
/note="LRR 1"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 71..93
/note="LRR 2"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 95..117
/note="LRR 3"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 120..143
/note="LRR 4"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 146..166
/note="LRR 5"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 171..192
/note="LRR 6"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 197..211
/note="LRR 7"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 214..229
/note="LRR 8"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 234..235
/note="LRR 9"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 260..284
/note="LRR 11"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 289..301
/note="LRR 12"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 313..334
/note="LRR 13"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 337..355
/note="LRR 14"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 385..401
/note="LRR 16"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 412..431
/note="LRR 17"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 449..470
/note="LRR 18"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 474..495
/note="LRR 19"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 503..524
/note="LRR 20"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 527..546
/note="LRR 21"
/evidence="ECO:0000269|PubMed:22173220"
REPEAT 549..567
/note="LRR 22"
/evidence="ECO:0000269|PubMed:22173220"
DOMAIN 579..631
/note="LRRCT"
DOMAIN 691..837
/note="TIR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
MOD_RES 798
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:17157808"
MOD_RES 805
/note="Phosphoserine; by PKD/PRKD1"
/evidence="ECO:0000269|PubMed:17442957"
CARBOHYD 37
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:22173220"
CARBOHYD 46
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:22173220"
CARBOHYD 245
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:22173220"
CARBOHYD 342
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:22173220"
CARBOHYD 422
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:22173220"
CARBOHYD 595
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:22173220"
CARBOHYD 598
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:22173220"
DISULFID 583..610
/evidence="ECO:0000269|PubMed:22173220"
DISULFID 585..629
/evidence="ECO:0000269|PubMed:22173220"
VARIANT 82
/note="T -> I (in dbSNP:rs764535)"
/id="VAR_032455"
VARIANT 112
/note="P -> A (in dbSNP:rs5744166)"
/id="VAR_032456"
VARIANT 143
/note="N -> T (in dbSNP:rs5744167)"
/id="VAR_061856"
VARIANT 181
/note="Q -> K (in dbSNP:rs45528236)"
/id="VAR_061857"
VARIANT 392..858
/note="Missing (in 10% of the population; abolishes
flagellin signaling; associated with resistance to SLEB1)"
/evidence="ECO:0000269|PubMed:14623910"
/id="VAR_018398"
VARIANT 592
/note="N -> S (in dbSNP:rs2072493)"
/evidence="ECO:0000269|PubMed:14623910,
ECO:0000269|PubMed:16027372"
/id="VAR_018399"
VARIANT 616
/note="F -> L (in dbSNP:rs5744174)"
/evidence="ECO:0000269|PubMed:14623910,
ECO:0000269|PubMed:16027372, ECO:0000269|PubMed:9596645"
/id="VAR_018400"
VARIANT 644
/note="I -> F (in dbSNP:rs5744175)"
/evidence="ECO:0000269|PubMed:19924287"
/id="VAR_070457"
VARIANT 769
/note="L -> F (in dbSNP:rs56243703)"
/id="VAR_061858"
VARIANT 822
/note="F -> L (in dbSNP:rs7512943)"
/evidence="ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18810425, ECO:0000269|PubMed:19179655,
ECO:0000269|PubMed:19924287, ECO:0000269|PubMed:9435236,
ECO:0000269|PubMed:9596645, ECO:0000269|Ref.2,
ECO:0000269|Ref.7"
/id="VAR_047454"
CONFLICT 231
/note="L -> V (in Ref. 1; AAC34376)"
/evidence="ECO:0000305"
CONFLICT 352
/note="Y -> C (in Ref. 1; AAC34376)"
/evidence="ECO:0000305"
CONFLICT 387
/note="Q -> R (in Ref. 8; AAI09120)"
/evidence="ECO:0000305"
SEQUENCE 858 AA; 97834 MW; 9EE0AB6EEFEA9051 CRC64;
MGDHLDLLLG VVLMAGPVFG IPSCSFDGRI AFYRFCNLTQ VPQVLNTTER LLLSFNYIRT
VTASSFPFLE QLQLLELGSQ YTPLTIDKEA FRNLPNLRIL DLGSSKIYFL HPDAFQGLFH
LFELRLYFCG LSDAVLKDGY FRNLKALTRL DLSKNQIRSL YLHPSFGKLN SLKSIDFSSN
QIFLVCEHEL EPLQGKTLSF FSLAANSLYS RVSVDWGKCM NPFRNMVLEI LDVSGNGWTV
DITGNFSNAI SKSQAFSLIL AHHIMGAGFG FHNIKDPDQN TFAGLARSSV RHLDLSHGFV
FSLNSRVFET LKDLKVLNLA YNKINKIADE AFYGLDNLQV LNLSYNLLGE LYSSNFYGLP
KVAYIDLQKN HIAIIQDQTF KFLEKLQTLD LRDNALTTIH FIPSIPDIFL SGNKLVTLPK
INLTANLIHL SENRLENLDI LYFLLRVPHL QILILNQNRF SSCSGDQTPS ENPSLEQLFL
GENMLQLAWE TELCWDVFEG LSHLQVLYLN HNYLNSLPPG VFSHLTALRG LSLNSNRLTV
LSHNDLPANL EILDISRNQL LAPNPDVFVS LSVLDITHNK FICECELSTF INWLNHTNVT
IAGPPADIYC VYPDSFSGVS LFSLSTEGCD EEEVLKSLKF SLFIVCTVTL TLFLMTILTV
TKFRGFCFIC YKTAQRLVFK DHPQGTEPDM YKYDAYLCFS SKDFTWVQNA LLKHLDTQYS
DQNRFNLCFE ERDFVPGENR IANIQDAIWN SRKIVCLVSR HFLRDGWCLE AFSYAQGRCL
SDLNSALIMV VVGSLSQYQL MKHQSIRGFV QKQQYLRWPE DFQDVGWFLH KLSQQILKKE
KEKKKDNNIP LQTVATIS


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WP1309: Toll-like receptor signaling pathway
WP75: Toll-like receptor signaling pathway
WP1384: Toll-like receptor signaling pathway
WP829: Toll-like receptor signaling pathway
WP1449: Regulation of toll-like receptor signaling pathway
WP1271: Toll-like receptor signaling pathway
WP1067: Toll-like receptor signaling pathway
WP88: Toll Like Receptor signaling
WP2292: Chemokine signaling pathway
WP2079: Serotonin Receptor 2 and STAT3 Signaling
WP480: T Cell Receptor Signaling Pathway
WP1004: Kit Receptor Signaling Pathway
WP2355: Corticotropin-releasing hormone
WP783: Androgen Receptor Signaling Pathway
WP258: TGF-beta Receptor Signaling Pathway
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1249: EPO Receptor Signaling
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WP57: Signal Transduction of S1P Receptor
WP1025: B Cell Receptor Signaling Pathway
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Related Genes :
[TLR5 TIL3] Toll-like receptor 5 (Toll/interleukin-1 receptor-like protein 3)
[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)
[Tlr1] Toll-like receptor 1 (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)
[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)
[Ticam1 Trif] TIR domain-containing adapter molecule 1 (TICAM-1) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (TIR domain-containing adapter protein inducing IFN-beta)
[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)
[TIRAP MAL] Toll/interleukin-1 receptor domain-containing adapter protein (TIR domain-containing adapter protein) (Adaptor protein Wyatt) (MyD88 adapter-like protein) (MyD88-2)
[Ticam2 Tirp Tram] TIR domain-containing adapter molecule 2 (TICAM-2) (TRIF-related adapter molecule) (Toll/interleukin-1 receptor domain-containing protein)
[Sigirr Tir8] Single Ig IL-1-related receptor (Single Ig IL-1R-related molecule) (Single immunoglobulin domain-containing IL1R-related protein) (Toll/interleukin-1 receptor 8) (TIR8)
[Tlr4 Lps] Toll-like receptor 4 (CD antigen CD284)
[Tlr4] Toll-like receptor 4 (Toll4) (CD antigen CD284)
[TLR4] Toll-like receptor 4 (hToll) (CD antigen CD284)
[Tlr2] Toll-like receptor 2 (CD antigen CD282)
[Tlr9] Toll-like receptor 9 (CD antigen CD289)
[TLR9 UNQ5798/PRO19605] Toll-like receptor 9 (CD antigen CD289)
[TLR8 UNQ249/PRO286] Toll-like receptor 8 (CD antigen CD288)
[Tlr6] Toll-like receptor 6 (CD antigen CD286)
[TLR6] Toll-like receptor 6 (CD antigen CD286)
[TLR4] Toll-like receptor 4 (CD antigen CD284)
[Tlr8] Toll-like receptor 8 (CD antigen CD288)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[TLR7 UNQ248/PRO285] Toll-like receptor 7
[TLR2] Toll-like receptor 2 (CD antigen CD282)
[TLR2] Toll-like receptor 2 (CD antigen CD282)
[Toll-7 CG8595] Toll-like receptor 7
[Tlr7] Toll-like receptor 7
[TLR9] Toll-like receptor 9 (CD antigen CD289)

Bibliography :