ID TLR5_HUMAN Reviewed; 858 AA. AC O60602; B1AZ05; B3Y633; B9VJ63; D1CS80; D3DTB8; O15456; Q32MI2; AC Q32MI3; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 4. DT 13-FEB-2019, entry version 173. DE RecName: Full=Toll-like receptor 5; DE AltName: Full=Toll/interleukin-1 receptor-like protein 3; DE Flags: Precursor; GN Name=TLR5; Synonyms=TIL3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-616 AND LEU-822. RC TISSUE=Leukocyte, and Prostate; RX PubMed=9596645; RA Chaudhary P.M., Ferguson C., Nguyen V., Nguyen O., Massa H.F., Eby M., RA Jasmin A., Trask B.J., Hood L., Nelson P.S.; RT "Cloning and characterization of two Toll/Interleukin-1 receptor-like RT genes TIL3 and TIL4: evidence for a multi-gene receptor family in RT humans."; RL Blood 91:4020-4027(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-822. RC TISSUE=Macrophage; RA Seya T., Tsukada H.; RT "Homo sapiens TLR5."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-822. RX PubMed=18810425; DOI=10.1007/s00251-008-0332-0; RA Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., RA Kimura A.; RT "Natural selection in the TLR-related genes in the course of primate RT evolution."; RL Immunogenetics 60:727-735(2008). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-822. RX PubMed=19179655; DOI=10.1093/molbev/msp018; RA Wlasiuk G., Khan S., Switzer W.M., Nachman M.W.; RT "A history of recurrent positive selection at the toll-like receptor 5 RT in primates."; RL Mol. Biol. Evol. 26:937-949(2009). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-644 AND LEU-822. RX PubMed=19924287; DOI=10.1371/journal.pone.0007803; RA Georgel P., Macquin C., Bahram S.; RT "The heterogeneous allelic repertoire of human Toll-Like receptor RT (TLR) genes."; RL PLoS ONE 4:E7803-E7803(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-822. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-822. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 494-858, AND VARIANT LEU-822. RC TISSUE=CNS; RX PubMed=9435236; DOI=10.1073/pnas.95.2.588; RA Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F.; RT "A family of human receptors structurally related to Drosophila RT Toll."; RL Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998). RN [10] RP PROTEIN SEQUENCE OF 21-35. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [11] RP TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=11489966; RA Gewirtz A.T., Navas T.A., Lyons S., Godowski P.J., Madara J.L.; RT "Cutting edge: bacterial flagellin activates basolaterally expressed RT TLR5 to induce epithelial proinflammatory gene expression."; RL J. Immunol. 167:1882-1885(2001). RN [12] RP FUNCTION. RX PubMed=11323673; DOI=10.1038/35074106; RA Hayashi F., Smith K.D., Ozinsky A., Hawn T.R., Yi E.C., Goodlett D.R., RA Eng J.K., Akira S., Underhill D.M., Aderem A.; RT "The innate immune response to bacterial flagellin is mediated by RT Toll-like receptor 5."; RL Nature 410:1099-1103(2001). RN [13] RP ASSOCIATION WITH RESISTANCE TO SLEB1, AND VARIANTS SER-592 AND RP LEU-616. RX PubMed=16027372; DOI=10.1073/pnas.0501165102; RA Hawn T.R., Wu H., Grossman J.M., Hahn B.H., Tsao B.P., Aderem A.; RT "A stop codon polymorphism of Toll-like receptor 5 is associated with RT resistance to systemic lupus erythematosus."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10593-10597(2005). RN [14] RP PHOSPHORYLATION AT TYR-798. RX PubMed=17157808; DOI=10.1016/j.bbrc.2006.11.132; RA Ivison S.M., Khan M.A., Graham N.R., Bernales C.Q., Kaleem A., RA Tirling C.O., Cherkasov A., Steiner T.S.; RT "A phosphorylation site in the Toll-like receptor 5 TIR domain is RT required for inflammatory signalling in response to flagellin."; RL Biochem. Biophys. Res. Commun. 352:936-941(2007). RN [15] RP PHOSPHORYLATION AT SER-805. RX PubMed=17442957; DOI=10.4049/jimmunol.178.9.5735; RA Ivison S.M., Graham N.R., Bernales C.Q., Kifayet A., Ng N., RA Shobab L.A., Steiner T.S.; RT "Protein kinase D interaction with TLR5 is required for inflammatory RT signaling in response to bacterial flagellin."; RL J. Immunol. 178:5735-5743(2007). RN [16] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=18490781; RA Blohmke C.J., Victor R.E., Hirschfeld A.F., Elias I.M., Hancock D.G., RA Lane C.R., Davidson A.G., Wilcox P.G., Smith K.D., Overhage J., RA Hancock R.E., Turvey S.E.; RT "Innate immunity mediated by TLR5 as a novel antiinflammatory target RT for cystic fibrosis lung disease."; RL J. Immunol. 180:7764-7773(2008). RN [17] RP FUNCTION, INTERACTION WITH TICAM1 AND MYD88, AND SUBCELLULAR LOCATION. RX PubMed=20855887; DOI=10.1074/jbc.M110.158394; RA Choi Y.J., Im E., Chung H.K., Pothoulakis C., Rhee S.H.; RT "TRIF mediates Toll-like receptor 5-induced signaling in intestinal RT epithelial cells."; RL J. Biol. Chem. 285:37570-37578(2010). RN [18] RP POLYMORPHISM, AND INVOLVEMENT IN RESISTANCE TO MELIOIDOSIS. RX PubMed=23447684; DOI=10.4049/jimmunol.1202974; RA West T.E., Chantratita N., Chierakul W., Limmathurotsakul D., RA Wuthiekanun V., Myers N.D., Emond M.J., Wurfel M.M., Hawn T.R., RA Peacock S.J., Skerrett S.J.; RT "Impaired TLR5 functionality is associated with survival in RT melioidosis."; RL J. Immunol. 190:3373-3379(2013). RN [19] RP INTERACTION WITH UNC93B1, AND SUBCELLULAR LOCATION. RX PubMed=24778236; DOI=10.1073/pnas.1322838111; RA Huh J.W., Shibata T., Hwang M., Kwon E.H., Jang M.S., Fukui R., RA Kanno A., Jung D.J., Jang M.H., Miyake K., Kim Y.M.; RT "UNC93B1 is essential for the plasma membrane localization and RT signaling of Toll-like receptor 5."; RL Proc. Natl. Acad. Sci. U.S.A. 111:7072-7077(2014). RN [20] RP FUNCTION. RX PubMed=29934223; DOI=10.1016/j.ijmm.2018.06.004; RA Bielaszewska M., Marejkova M., Bauwens A., Kunsmann-Prokscha L., RA Mellmann A., Karch H.; RT "Enterohemorrhagic Escherichia coli O157 outer membrane vesicles RT induce interleukin 8 production in human intestinal epithelial cells RT by signaling via Toll-like receptors TLR4 and TLR5 and activation of RT the nuclear factor NF-kappaB."; RL Int. J. Med. Microbiol. 308:882-889(2018). RN [21] RP STRUCTURE BY ELECTRON MICROSCOPY (26.0 ANGSTROMS) OF 23-858, RP GLYCOSYLATION AT ASN-37; ASN-46; ASN-245; ASN-342; ASN-422; ASN-595 RP AND ASN-598, DISULFIDE BONDS, LRR REPEATS, AND SUBUNIT. RX PubMed=22173220; DOI=10.1016/j.jsb.2011.12.002; RA Zhou K., Kanai R., Lee P., Wang H.W., Modis Y.; RT "Toll-like receptor 5 forms asymmetric dimers in the absence of RT flagellin."; RL J. Struct. Biol. 177:402-409(2012). RN [22] RP VARIANTS 392-ARG--SER-858 DEL; SER-592 AND LEU-616. RX PubMed=14623910; DOI=10.1084/jem.20031220; RA Hawn T.R., Verbon A., Lettinga K.D., Zhao L.P., Li S.S., Laws R.J., RA Skerrett S.J., Beutler B., Schroeder L., Nachman A., Ozinsky A., RA Smith K.D., Aderem A.; RT "A common dominant TLR5 stop codon polymorphism abolishes flagellin RT signaling and is associated with susceptibility to legionnaires' RT disease."; RL J. Exp. Med. 198:1563-1572(2003). CC -!- FUNCTION: Pattern recognition receptor (PRR) located on the cell CC surface that participates in the activation of innate immunity and CC inflammatory response (PubMed:11323673, PubMed:18490781). CC Recognizes small molecular motifs named pathogen-associated CC molecular pattern (PAMPs) expressed by pathogens and microbe- CC associated molecular patterns (MAMPs) usually expressed by CC resident microbiota (PubMed:29934223). Upon ligand binding such as CC bacterial flagellins, recruits intracellular adapter proteins CC MYD88 and TRIF leading to NF-kappa-B activation, cytokine CC secretion and induction of the inflammatory response CC (PubMed:20855887, PubMed:11489966). Plays thereby an important CC role in the relationship between the intestinal epithelium and CC enteric microbes and contributes to the gut microbiota composition CC throughout life (By similarity). {ECO:0000250|UniProtKB:Q9JLF7, CC ECO:0000269|PubMed:11323673, ECO:0000269|PubMed:11489966, CC ECO:0000269|PubMed:18490781, ECO:0000269|PubMed:20855887, CC ECO:0000269|PubMed:29934223}. CC -!- SUBUNIT: Homodimer (PubMed:22173220). Interacts with MYD88 (via CC TIR domain) (PubMed:20855887). Interacts with TICAM1 (via TIR CC domain) (PubMed:20855887). Interacts with UNC93B1; this CC interaction is essential for proper TLR5 localization to the CC plasma membrane (PubMed:24778236). {ECO:0000269|PubMed:20855887, CC ECO:0000269|PubMed:22173220, ECO:0000269|PubMed:24778236}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24778236}; CC Single-pass type I membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Highly expressed on the basolateral surface of CC intestinal epithelia (PubMed:11489966). Expressed also in other CC cells such as lung epithelial cells (PubMed:11489966, CC PubMed:18490781). {ECO:0000269|PubMed:11489966, CC ECO:0000269|PubMed:18490781}. CC -!- PTM: Phosphorylated at Ser-805 by PKD/PRKD1; phosphorylation CC induces the production of inflammatory cytokines. CC {ECO:0000269|PubMed:17157808, ECO:0000269|PubMed:17442957}. CC -!- PTM: Phosphorylated at Tyr-798 upon flagellin binding; required CC for signaling. {ECO:0000269|PubMed:17157808, CC ECO:0000269|PubMed:17442957}. CC -!- POLYMORPHISM: Individuals with a common stop codon polymorphism in CC position 392 are unable to mediate flagellin signaling. This CC polymorphism acts in a dominant fashion and is associated with CC susceptibility to pneumonia caused by Legionella pneumophila CC [MIM:608556]. It also provides protection against systemic lupus CC erythematosus. CC -!- POLYMORPHISM: A nonsense TLR5 polymorphism, resulting in CC p.Arg392Ter, confers resistance to melioidosis [MIM:615557], an CC infection caused by the Gram-negative, flagellated soil saprophyte CC Burkholderia pseudomallei. Carriers of this hypofunctional TLR5 CC variant may generate impaired inflammatory responses during CC melioidosis infection that result in reduced organ failure and CC lower mortality. CC -!- DISEASE: Systemic lupus erythematosus 1 (SLEB1) [MIM:601744]: A CC chronic, relapsing, inflammatory, and often febrile multisystemic CC disorder of connective tissue, characterized principally by CC involvement of the skin, joints, kidneys and serosal membranes. It CC is of unknown etiology, but is thought to represent a failure of CC the regulatory mechanisms of the autoimmune system. The disease is CC marked by a wide range of system dysfunctions, an elevated CC erythrocyte sedimentation rate, and the formation of LE cells in CC the blood or bone marrow. Note=Disease susceptibility is CC associated with variations affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the Toll-like receptor family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF051151; AAC34376.1; -; mRNA. DR EMBL; AB060695; BAB43955.1; -; mRNA. DR EMBL; AB445645; BAG55042.1; -; mRNA. DR EMBL; FJ556976; ACM69019.1; -; Genomic_DNA. DR EMBL; FJ556977; ACM69020.1; -; Genomic_DNA. DR EMBL; FJ556979; ACM69022.1; -; Genomic_DNA. DR EMBL; FJ556980; ACM69023.1; -; Genomic_DNA. DR EMBL; FJ556987; ACM69030.1; -; Genomic_DNA. DR EMBL; FJ556989; ACM69032.1; -; Genomic_DNA. DR EMBL; DQ026408; AAZ17463.1; -; Genomic_DNA. DR EMBL; DQ026409; AAZ17464.1; -; Genomic_DNA. DR EMBL; DQ026415; AAZ17469.1; -; Genomic_DNA. DR EMBL; AL929091; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471100; EAW93262.1; -; Genomic_DNA. DR EMBL; CH471100; EAW93263.1; -; Genomic_DNA. DR EMBL; BC109118; AAI09119.1; -; mRNA. DR EMBL; BC109119; AAI09120.1; -; mRNA. DR EMBL; U88881; AAC34136.1; -; mRNA. DR CCDS; CCDS31033.1; -. DR RefSeq; NP_003259.2; NM_003268.5. DR RefSeq; XP_005273298.2; XM_005273241.4. DR RefSeq; XP_005273299.2; XM_005273242.4. DR RefSeq; XP_005273300.2; XM_005273243.4. DR RefSeq; XP_006711567.1; XM_006711504.3. DR RefSeq; XP_006711568.1; XM_006711505.3. DR RefSeq; XP_006711569.1; XM_006711506.3. DR RefSeq; XP_011508239.1; XM_011509937.2. DR RefSeq; XP_016857697.1; XM_017002208.1. DR UniGene; Hs.604542; -. DR PDB; 1P95; Model; -; B=551-560. DR PDB; 3J0A; EM; 26.00 A; A/B=23-858. DR PDBsum; 1P95; -. DR PDBsum; 3J0A; -. DR ProteinModelPortal; O60602; -. DR SMR; O60602; -. DR BioGrid; 112955; 13. DR IntAct; O60602; 9. DR MINT; O60602; -. DR STRING; 9606.ENSP00000340089; -. DR ChEMBL; CHEMBL2176839; -. DR iPTMnet; O60602; -. DR PhosphoSitePlus; O60602; -. DR BioMuta; TLR5; -. DR jPOST; O60602; -. DR PaxDb; O60602; -. DR PeptideAtlas; O60602; -. DR PRIDE; O60602; -. DR ProteomicsDB; 49480; -. DR DNASU; 7100; -. DR Ensembl; ENST00000366881; ENSP00000355846; ENSG00000187554. DR Ensembl; ENST00000540964; ENSP00000440643; ENSG00000187554. DR GeneID; 7100; -. DR KEGG; hsa:7100; -. DR UCSC; uc001hnw.3; human. DR CTD; 7100; -. DR DisGeNET; 7100; -. DR EuPathDB; HostDB:ENSG00000187554.11; -. DR GeneCards; TLR5; -. DR HGNC; HGNC:11851; TLR5. DR HPA; CAB009013; -. DR MalaCards; TLR5; -. DR MIM; 109100; phenotype. DR MIM; 601744; phenotype. DR MIM; 603031; gene. DR MIM; 608556; phenotype. DR MIM; 615557; phenotype. DR neXtProt; NX_O60602; -. DR PharmGKB; PA36553; -. DR eggNOG; KOG4641; Eukaryota. DR eggNOG; COG4886; LUCA. DR HOGENOM; HOG000008675; -. DR HOVERGEN; HBG023182; -. DR InParanoid; O60602; -. DR KO; K10168; -. DR OrthoDB; 282372at2759; -. DR PhylomeDB; O60602; -. DR TreeFam; TF351113; -. DR Reactome; R-HSA-168176; Toll Like Receptor 5 (TLR5) Cascade. DR Reactome; R-HSA-5602680; MyD88 deficiency (TLR5). DR Reactome; R-HSA-5603037; IRAK4 deficiency (TLR5). DR Reactome; R-HSA-975871; MyD88 cascade initiated on plasma membrane. DR SIGNOR; O60602; -. DR ChiTaRS; TLR5; human. DR GeneWiki; TLR_5; -. DR GenomeRNAi; 7100; -. DR PRO; PR:O60602; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000187554; Expressed in 188 organ(s), highest expression level in blood. DR ExpressionAtlas; O60602; baseline and differential. DR Genevisible; O60602; HS. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005149; F:interleukin-1 receptor binding; IPI:UniProtKB. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; IEA:InterPro. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL. DR GO; GO:0034123; P:positive regulation of toll-like receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0050707; P:regulation of cytokine secretion; IEA:InterPro. DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome. DR Gene3D; 3.40.50.10140; -; 1. DR Gene3D; 3.80.10.10; -; 3. DR InterPro; IPR000483; Cys-rich_flank_reg_C. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR000157; TIR_dom. DR InterPro; IPR027176; TLR5. DR InterPro; IPR035897; Toll_tir_struct_dom_sf. DR PANTHER; PTHR44698:SF2; PTHR44698:SF2; 1. DR Pfam; PF13855; LRR_8; 5. DR Pfam; PF01582; TIR; 1. DR SMART; SM00369; LRR_TYP; 9. DR SMART; SM00082; LRRCT; 1. DR SMART; SM00255; TIR; 1. DR SUPFAM; SSF52200; SSF52200; 1. DR PROSITE; PS51450; LRR; 12. DR PROSITE; PS50104; TIR; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity; KW Inflammatory response; Innate immunity; Leucine-rich repeat; Membrane; KW Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; KW Signal; Systemic lupus erythematosus; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 20 {ECO:0000269|PubMed:15340161}. FT CHAIN 21 858 Toll-like receptor 5. FT /FTId=PRO_0000034729. FT TOPO_DOM 21 639 Extracellular. {ECO:0000255}. FT TRANSMEM 640 660 Helical. {ECO:0000255}. FT TOPO_DOM 661 858 Cytoplasmic. {ECO:0000255}. FT REPEAT 45 68 LRR 1. {ECO:0000269|PubMed:22173220}. FT REPEAT 71 93 LRR 2. {ECO:0000269|PubMed:22173220}. FT REPEAT 95 117 LRR 3. {ECO:0000269|PubMed:22173220}. FT REPEAT 120 143 LRR 4. {ECO:0000269|PubMed:22173220}. FT REPEAT 146 166 LRR 5. {ECO:0000269|PubMed:22173220}. FT REPEAT 171 192 LRR 6. {ECO:0000269|PubMed:22173220}. FT REPEAT 197 211 LRR 7. {ECO:0000269|PubMed:22173220}. FT REPEAT 214 229 LRR 8. {ECO:0000269|PubMed:22173220}. FT REPEAT 234 235 LRR 9. {ECO:0000269|PubMed:22173220}. FT REPEAT 260 284 LRR 11. {ECO:0000269|PubMed:22173220}. FT REPEAT 289 301 LRR 12. {ECO:0000269|PubMed:22173220}. FT REPEAT 313 334 LRR 13. {ECO:0000269|PubMed:22173220}. FT REPEAT 337 355 LRR 14. {ECO:0000269|PubMed:22173220}. FT REPEAT 385 401 LRR 16. {ECO:0000269|PubMed:22173220}. FT REPEAT 412 431 LRR 17. {ECO:0000269|PubMed:22173220}. FT REPEAT 449 470 LRR 18. {ECO:0000269|PubMed:22173220}. FT REPEAT 474 495 LRR 19. {ECO:0000269|PubMed:22173220}. FT REPEAT 503 524 LRR 20. {ECO:0000269|PubMed:22173220}. FT REPEAT 527 546 LRR 21. {ECO:0000269|PubMed:22173220}. FT REPEAT 549 567 LRR 22. {ECO:0000269|PubMed:22173220}. FT DOMAIN 579 631 LRRCT. FT DOMAIN 691 837 TIR. {ECO:0000255|PROSITE- FT ProRule:PRU00204}. FT MOD_RES 798 798 Phosphotyrosine. FT {ECO:0000269|PubMed:17157808}. FT MOD_RES 805 805 Phosphoserine; by PKD/PRKD1. FT {ECO:0000269|PubMed:17442957}. FT CARBOHYD 37 37 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22173220}. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22173220}. FT CARBOHYD 245 245 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22173220}. FT CARBOHYD 342 342 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22173220}. FT CARBOHYD 422 422 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22173220}. FT CARBOHYD 595 595 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22173220}. FT CARBOHYD 598 598 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22173220}. FT DISULFID 583 610 {ECO:0000269|PubMed:22173220}. FT DISULFID 585 629 {ECO:0000269|PubMed:22173220}. FT VARIANT 82 82 T -> I (in dbSNP:rs764535). FT /FTId=VAR_032455. FT VARIANT 112 112 P -> A (in dbSNP:rs5744166). FT /FTId=VAR_032456. FT VARIANT 143 143 N -> T (in dbSNP:rs5744167). FT /FTId=VAR_061856. FT VARIANT 181 181 Q -> K (in dbSNP:rs45528236). FT /FTId=VAR_061857. FT VARIANT 392 858 Missing (in 10% of the population; FT abolishes flagellin signaling; associated FT with resistance to SLEB1). FT {ECO:0000269|PubMed:14623910}. FT /FTId=VAR_018398. FT VARIANT 592 592 N -> S (in dbSNP:rs2072493). FT {ECO:0000269|PubMed:14623910, FT ECO:0000269|PubMed:16027372}. FT /FTId=VAR_018399. FT VARIANT 616 616 F -> L (in dbSNP:rs5744174). FT {ECO:0000269|PubMed:14623910, FT ECO:0000269|PubMed:16027372, FT ECO:0000269|PubMed:9596645}. FT /FTId=VAR_018400. FT VARIANT 644 644 I -> F (in dbSNP:rs5744175). FT {ECO:0000269|PubMed:19924287}. FT /FTId=VAR_070457. FT VARIANT 769 769 L -> F (in dbSNP:rs56243703). FT /FTId=VAR_061858. FT VARIANT 822 822 F -> L (in dbSNP:rs7512943). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:18810425, FT ECO:0000269|PubMed:19179655, FT ECO:0000269|PubMed:19924287, FT ECO:0000269|PubMed:9435236, FT ECO:0000269|PubMed:9596645, FT ECO:0000269|Ref.2, ECO:0000269|Ref.7}. FT /FTId=VAR_047454. FT CONFLICT 231 231 L -> V (in Ref. 1; AAC34376). FT {ECO:0000305}. FT CONFLICT 352 352 Y -> C (in Ref. 1; AAC34376). FT {ECO:0000305}. FT CONFLICT 387 387 Q -> R (in Ref. 8; AAI09120). FT {ECO:0000305}. SQ 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 //