TLR1_HUMAN
ID TLR1_HUMAN Reviewed; 786 AA.
AC Q15399; D1CS39; D1CS41; O15452; Q32MK3; Q32MK4; Q9UG90;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Toll-like receptor 1;
DE AltName: Full=Toll/interleukin-1 receptor-like protein;
DE Short=TIL;
DE AltName: CD_antigen=CD281;
DE Flags: Precursor;
GN Name=TLR1; Synonyms=KIAA0012;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-248 AND ILE-602.
RC TISSUE=Erythroleukemia;
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 Toll.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
RA Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.;
RT "Natural selection in the TLR-related genes in the course of primate
RT evolution.";
RL Immunogenetics 60:727-735(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-80 AND ILE-602.
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 (TLR)
RT genes.";
RL PLoS ONE 4:E7803-E7803(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-80.
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-248 AND ILE-602.
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-248 AND ILE-602.
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 25-39.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TLR2 AND CD14.
RX PubMed=16880211; DOI=10.1074/jbc.m602794200;
RA Triantafilou M., Gamper F.G., Haston R.M., Mouratis M.A., Morath S.,
RA Hartung T., Triantafilou K.;
RT "Membrane sorting of toll-like receptor (TLR)-2/6 and TLR2/1 heterodimers
RT at the cell surface determines heterotypic associations with CD36 and
RT intracellular targeting.";
RL J. Biol. Chem. 281:31002-31011(2006).
RN [9]
RP INVOLVEMENT IN PROTECTION AGAINST LEPROSY.
RX PubMed=17548585; DOI=10.4049/jimmunol.178.12.7520;
RA Johnson C.M., Lyle E.A., Omueti K.O., Stepensky V.A., Yegin O., Alpsoy E.,
RA Hamann L., Schumann R.R., Tapping R.I.;
RT "Cutting edge: A common polymorphism impairs cell surface trafficking and
RT functional responses of TLR1 but protects against leprosy.";
RL J. Immunol. 178:7520-7524(2007).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-163.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP FUNCTION.
RC TISSUE=T-cell;
RX PubMed=21078852; DOI=10.1128/iai.00806-10;
RA Lancioni C.L., Li Q., Thomas J.J., Ding X., Thiel B., Drage M.G.,
RA Pecora N.D., Ziady A.G., Shank S., Harding C.V., Boom W.H., Rojas R.E.;
RT "Mycobacterium tuberculosis lipoproteins directly regulate human memory
RT CD4(+) T cell activation via Toll-like receptors 1 and 2.";
RL Infect. Immun. 79:663-673(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 625-785.
RX PubMed=11081518; DOI=10.1038/35040600;
RA Xu Y., Tao X., Shen B., Horng T., Medzhitov R., Manley J.L., Tong L.;
RT "Structural basis for signal transduction by the Toll/interleukin-1
RT receptor domains.";
RL Nature 408:111-115(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-476 IN COMPLEX WITH TLR2 AND
RP BACTERIAL LIPOPEPTIDE ANALOG, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-51;
RP ASN-163; ASN-330 AND ASN-429.
RX PubMed=17889651; DOI=10.1016/j.cell.2007.09.008;
RA Jin M.S., Kim S.E., Heo J.Y., Lee M.E., Kim H.M., Paik S.-G., Lee H.,
RA Lee J.-O.;
RT "Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a
RT tri-acylated lipopeptide.";
RL Cell 130:1071-1082(2007).
RN [14]
RP ASSOCIATION OF VARIANT SER-248 WITH SUSCEPTIBILITY TO LEPROSY.
RX PubMed=19456232; DOI=10.1086/599121;
RA Schuring R.P., Hamann L., Faber W.R., Pahan D., Richardus J.H.,
RA Schumann R.R., Oskam L.;
RT "Polymorphism N248S in the human Toll-like receptor 1 gene is related to
RT leprosy and leprosy reactions.";
RL J. Infect. Dis. 199:1816-1819(2009).
RN [15]
RP VARIANTS PRO-44; THR-75; THR-80; TYR-118; SER-248; LEU-305; LEU-315;
RP ASN-352; VAL-460; ALA-542; CYS-554; GLY-587; ILE-602; ALA-651; ALA-674;
RP PRO-720 AND LEU-733, AND CHARACTERIZATION OF VARIANTS LEU-315; CYS-554;
RP ILE-602; ALA-651 AND PRO-720.
RX PubMed=21618349; DOI=10.1002/humu.21486;
RA Ben-Ali M., Corre B., Manry J., Barreiro L.B., Quach H., Boniotto M.,
RA Pellegrini S., Quintana-Murci L.;
RT "Functional characterization of naturally occurring genetic variants in the
RT human TLR1-2-6 gene family.";
RL Hum. Mutat. 32:643-652(2011).
CC -!- FUNCTION: Participates in the innate immune response to microbial
CC agents. Specifically recognizes diacylated and triacylated
CC lipopeptides. Cooperates with TLR2 to mediate the innate immune
CC response to bacterial lipoproteins or lipopeptides (PubMed:21078852).
CC Forms the activation cluster TLR2:TLR1:CD14 in response to triacylated
CC lipopeptides, this cluster triggers signaling from the cell surface and
CC subsequently is targeted to the Golgi in a lipid-raft dependent pathway
CC (PubMed:16880211). Acts via MYD88 and TRAF6, leading to NF-kappa-B
CC activation, cytokine secretion and the inflammatory response.
CC {ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:21078852}.
CC -!- SUBUNIT: Interacts (via extracellular domain) with TLR2. TLR2 seems to
CC exist in heterodimers with either TLR1 or TLR6 before stimulation by
CC the ligand. The heterodimers form bigger oligomers in response to their
CC corresponding ligands as well as further heterotypic associations with
CC other receptors such as CD14 and/or CD36 (PubMed:16880211,
CC PubMed:17889651). The activation cluster TLR2:TLR1:CD14 forms in
CC response to triacylated lipopeptides (PubMed:16880211). Binds MYD88
CC (via TIR domain). Interacts with CNPY3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9EPQ1, ECO:0000269|PubMed:16880211,
CC ECO:0000269|PubMed:17889651}.
CC -!- INTERACTION:
CC Q15399; Q15399: TLR1; NbExp=3; IntAct=EBI-9009517, EBI-9009517;
CC Q15399; Q9BXR5: TLR10; NbExp=3; IntAct=EBI-9009517, EBI-16825459;
CC Q15399; O60603: TLR2; NbExp=3; IntAct=EBI-9009517, EBI-973722;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16880211};
CC Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000250|UniProtKB:Q9EPQ1}; Single-pass type I
CC membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000269|PubMed:16880211}. Golgi apparatus
CC {ECO:0000269|PubMed:16880211}. Note=Does not reside in lipid rafts
CC before stimulation but accumulates increasingly in the raft upon the
CC presence of the microbial ligand. In response to triacylated
CC lipoproteins, TLR2:TLR1 heterodimers are recruited in lipid rafts, this
CC recruitment determine the intracellular targeting to the Golgi
CC apparatus. {ECO:0000269|PubMed:16880211}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen, ovary,
CC peripheral blood leukocytes, thymus and small intestine.
CC -!- POLYMORPHISM: Genetic variations in TLR1 may influence susceptibility
CC to or protection against contracting leprosy and define the leprosy
CC susceptibility locus 5 [MIM:613223]. Ser-602 is a common allele in
CC Caucasians. It is associated with impaired cell surface expression and
CC receptor function resulting in protection against leprosy.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
CC -!- CAUTION: In some plant proteins and in human SARM1, the TIR domain has
CC NAD(+) hydrolase (NADase) activity (By similarity). However, despite
CC the presence of the catalytic Asp residue, the isolated TIR domain of
CC human TLR4 lacks NADase activity (By similarity). Based on this, it is
CC unlikely that Toll-like receptors have NADase activity.
CC {ECO:0000250|UniProtKB:O00206, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02801.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U88540; AAC34137.1; -; mRNA.
DR EMBL; AB445617; BAG55014.1; -; mRNA.
DR EMBL; DQ012259; AAY85638.1; -; mRNA.
DR EMBL; DQ012260; AAY85639.1; -; mRNA.
DR EMBL; DQ012261; AAY85640.1; -; mRNA.
DR EMBL; D13637; BAA02801.2; ALT_INIT; mRNA.
DR EMBL; AL050262; CAB43364.1; -; mRNA.
DR EMBL; BC109093; AAI09094.1; -; mRNA.
DR EMBL; BC109094; AAI09095.1; -; mRNA.
DR CCDS; CCDS33973.1; -.
DR PIR; T08664; T08664.
DR RefSeq; NP_003254.2; NM_003263.3.
DR RefSeq; XP_005262719.1; XM_005262662.4.
DR RefSeq; XP_011512044.1; XM_011513742.2.
DR RefSeq; XP_011512045.1; XM_011513743.2.
DR RefSeq; XP_011512046.1; XM_011513744.2.
DR RefSeq; XP_011512047.1; XM_011513745.2.
DR RefSeq; XP_016864060.1; XM_017008571.1.
DR RefSeq; XP_016864061.1; XM_017008572.1.
DR PDB; 1FYV; X-ray; 2.90 A; A=625-785.
DR PDB; 2Z7X; X-ray; 2.10 A; B=25-475.
DR PDB; 6NIH; X-ray; 2.30 A; A/B=1-475.
DR PDB; 7NT7; NMR; -; A=625-786.
DR PDB; 7NUW; X-ray; 1.90 A; A=625-785.
DR PDB; 7NUX; X-ray; 2.47 A; A=625-785.
DR PDBsum; 1FYV; -.
DR PDBsum; 2Z7X; -.
DR PDBsum; 6NIH; -.
DR PDBsum; 7NT7; -.
DR PDBsum; 7NUW; -.
DR PDBsum; 7NUX; -.
DR AlphaFoldDB; Q15399; -.
DR SMR; Q15399; -.
DR BioGRID; 112951; 22.
DR ComplexPortal; CPX-2699; TLR1-TLR10 toll-like receptor complex.
DR ComplexPortal; CPX-893; TLR1-TLR2 toll-like receptor complex.
DR CORUM; Q15399; -.
DR IntAct; Q15399; 6.
DR STRING; 9606.ENSP00000354932; -.
DR BindingDB; Q15399; -.
DR ChEMBL; CHEMBL3714412; -.
DR TCDB; 8.A.43.1.25; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR GlyGen; Q15399; 6 sites.
DR iPTMnet; Q15399; -.
DR PhosphoSitePlus; Q15399; -.
DR BioMuta; TLR1; -.
DR DMDM; 146291086; -.
DR EPD; Q15399; -.
DR jPOST; Q15399; -.
DR MassIVE; Q15399; -.
DR PaxDb; Q15399; -.
DR PeptideAtlas; Q15399; -.
DR PRIDE; Q15399; -.
DR ProteomicsDB; 60569; -.
DR Antibodypedia; 10459; 677 antibodies from 43 providers.
DR DNASU; 7096; -.
DR Ensembl; ENST00000308979.7; ENSP00000354932.2; ENSG00000174125.8.
DR Ensembl; ENST00000502213.6; ENSP00000421259.1; ENSG00000174125.8.
DR GeneID; 7096; -.
DR KEGG; hsa:7096; -.
DR MANE-Select; ENST00000308979.7; ENSP00000354932.2; NM_003263.4; NP_003254.2.
DR UCSC; uc003gtl.4; human.
DR CTD; 7096; -.
DR DisGeNET; 7096; -.
DR GeneCards; TLR1; -.
DR HGNC; HGNC:11847; TLR1.
DR HPA; ENSG00000174125; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; TLR1; -.
DR MIM; 601194; gene.
DR MIM; 613223; phenotype.
DR neXtProt; NX_Q15399; -.
DR OpenTargets; ENSG00000174125; -.
DR PharmGKB; PA36549; -.
DR VEuPathDB; HostDB:ENSG00000174125; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000162884; -.
DR HOGENOM; CLU_006000_3_0_1; -.
DR InParanoid; Q15399; -.
DR OMA; GTRMIHM; -.
DR OrthoDB; 282372at2759; -.
DR PhylomeDB; Q15399; -.
DR TreeFam; TF351113; -.
DR PathwayCommons; Q15399; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1461957; Beta defensins.
DR Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR Reactome; R-HSA-168179; Toll Like Receptor TLR1:TLR2 Cascade.
DR Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
DR Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q15399; -.
DR BioGRID-ORCS; 7096; 11 hits in 1075 CRISPR screens.
DR EvolutionaryTrace; Q15399; -.
DR GeneWiki; TLR_1; -.
DR GenomeRNAi; 7096; -.
DR Pharos; Q15399; Tbio.
DR PRO; PR:Q15399; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q15399; protein.
DR Bgee; ENSG00000174125; Expressed in monocyte and 144 other tissues.
DR ExpressionAtlas; Q15399; baseline and differential.
DR Genevisible; Q15399; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IPI:ComplexPortal.
DR GO; GO:0035354; C:Toll-like receptor 1-Toll-like receptor 2 protein complex; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0071723; F:lipopeptide binding; IBA:GO_Central.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0035663; F:Toll-like receptor 2 binding; IPI:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0001775; P:cell activation; IDA:AgBase.
DR GO; GO:0071221; P:cellular response to bacterial lipopeptide; IBA:GO_Central.
DR GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; IDA:UniProtKB.
DR GO; GO:0042495; P:detection of triacyl bacterial lipopeptide; IDA:MGI.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IC:ComplexPortal.
DR GO; GO:0042116; P:macrophage activation; NAS:UniProtKB.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IGI:ARUK-UCL.
DR GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0034130; P:toll-like receptor 1 signaling pathway; IEA:InterPro.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IDA:ComplexPortal.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
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; IPR027190; TLR1.
DR InterPro; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR PANTHER; PTHR24365:SF261; PTHR24365:SF261; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF01463; LRRCT; 1.
DR Pfam; PF01582; TIR; 1.
DR PIRSF; PIRSF037595; Toll-like_receptor; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 10.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Immunity; Inflammatory response; Innate immunity; Leucine-rich repeat;
KW Membrane; NAD; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 25..786
FT /note="Toll-like receptor 1"
FT /id="PRO_0000034705"
FT TOPO_DOM 25..580
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..786
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 54..77
FT /note="LRR 1"
FT REPEAT 78..101
FT /note="LRR 2"
FT REPEAT 102..125
FT /note="LRR 3"
FT REPEAT 126..150
FT /note="LRR 4"
FT REPEAT 151..175
FT /note="LRR 5"
FT REPEAT 176..199
FT /note="LRR 6"
FT REPEAT 200..223
FT /note="LRR 7"
FT REPEAT 224..250
FT /note="LRR 8"
FT REPEAT 251..278
FT /note="LRR 9"
FT REPEAT 279..308
FT /note="LRR 10"
FT REPEAT 309..337
FT /note="LRR 11"
FT REPEAT 338..361
FT /note="LRR 12"
FT REPEAT 362..388
FT /note="LRR 13"
FT REPEAT 389..414
FT /note="LRR 14"
FT REPEAT 415..437
FT /note="LRR 15"
FT REPEAT 438..457
FT /note="LRR 16"
FT REPEAT 458..478
FT /note="LRR 17"
FT REPEAT 479..500
FT /note="LRR 18"
FT REPEAT 501..524
FT /note="LRR 19"
FT DOMAIN 525..579
FT /note="LRRCT"
FT DOMAIN 635..776
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 313..316
FT /note="Interaction with bacterial lipopeptide"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17889651"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17889651,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17889651"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17889651"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..132
FT /evidence="ECO:0000269|PubMed:17889651"
FT DISULFID 223..230
FT /evidence="ECO:0000269|PubMed:17889651"
FT DISULFID 343..368
FT /evidence="ECO:0000269|PubMed:17889651"
FT DISULFID 419..442
FT /evidence="ECO:0000269|PubMed:17889651"
FT VARIANT 44
FT /note="S -> P (in dbSNP:rs76600635)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_066340"
FT VARIANT 75
FT /note="I -> T (in dbSNP:rs137853170)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_066341"
FT VARIANT 80
FT /note="R -> T (in dbSNP:rs5743611)"
FT /evidence="ECO:0000269|PubMed:19924287,
FT ECO:0000269|PubMed:21618349, ECO:0000269|PubMed:7584026"
FT /id="VAR_031916"
FT VARIANT 118
FT /note="H -> Y (in dbSNP:rs5743612)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_018474"
FT VARIANT 248
FT /note="N -> S (may confer susceptibility to leprosy;
FT dbSNP:rs4833095)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:21618349,
FT ECO:0000269|PubMed:9435236"
FT /id="VAR_031917"
FT VARIANT 305
FT /note="H -> L (in dbSNP:rs3923647)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_031918"
FT VARIANT 315
FT /note="P -> L (severe impairment of activity;
FT dbSNP:rs5743613)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_031919"
FT VARIANT 352
FT /note="H -> N (in dbSNP:rs76796448)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_066342"
FT VARIANT 460
FT /note="I -> V (in dbSNP:rs137853171)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_066343"
FT VARIANT 542
FT /note="V -> A (in dbSNP:rs137853172)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_066344"
FT VARIANT 554
FT /note="Y -> C (severe impairment of activity;
FT dbSNP:rs137853173)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_066345"
FT VARIANT 587
FT /note="V -> G (in dbSNP:rs5743617)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_031920"
FT VARIANT 602
FT /note="S -> I (severe impairment of activity;
FT dbSNP:rs5743618)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:19924287,
FT ECO:0000269|PubMed:21618349, ECO:0000269|PubMed:9435236"
FT /id="VAR_031921"
FT VARIANT 631
FT /note="L -> R (in dbSNP:rs5743619)"
FT /id="VAR_052358"
FT VARIANT 651
FT /note="V -> A (severe impairment of activity;
FT dbSNP:rs137853174)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_066346"
FT VARIANT 674
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_066347"
FT VARIANT 720
FT /note="H -> P (severe impairment of activity;
FT dbSNP:rs113706342)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_066348"
FT VARIANT 733
FT /note="P -> L (in dbSNP:rs5743621)"
FT /evidence="ECO:0000269|PubMed:21618349"
FT /id="VAR_052359"
FT CONFLICT 182
FT /note="E -> G (in Ref. 5; CAB43364)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="N -> S (in Ref. 5; CAB43364)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="F -> S (in Ref. 5; CAB43364)"
FT /evidence="ECO:0000305"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:2Z7X"
FT TURN 173..178
FT /evidence="ECO:0007829|PDB:6NIH"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2Z7X"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 274..285
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:2Z7X"
FT TURN 362..367
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 437..441
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 462..466
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:2Z7X"
FT TURN 487..491
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 504..516
FT /evidence="ECO:0007829|PDB:2Z7X"
FT TURN 517..520
FT /evidence="ECO:0007829|PDB:2Z7X"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:2Z7X"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:2Z7X"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:7NUW"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:7NUW"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:7NUW"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:7NUW"
FT HELIX 648..653
FT /evidence="ECO:0007829|PDB:7NUW"
FT HELIX 655..660
FT /evidence="ECO:0007829|PDB:7NUW"
FT TURN 661..663
FT /evidence="ECO:0007829|PDB:7NUW"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:7NUW"
FT TURN 669..671
FT /evidence="ECO:0007829|PDB:7NUW"
FT HELIX 679..688
FT /evidence="ECO:0007829|PDB:7NUW"
FT STRAND 690..698
FT /evidence="ECO:0007829|PDB:7NUW"
FT HELIX 699..704
FT /evidence="ECO:0007829|PDB:7NUW"
FT HELIX 706..713
FT /evidence="ECO:0007829|PDB:7NUW"
FT STRAND 726..732
FT /evidence="ECO:0007829|PDB:7NUW"
FT HELIX 736..738
FT /evidence="ECO:0007829|PDB:7NUW"
FT HELIX 744..751
FT /evidence="ECO:0007829|PDB:7NUW"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:7NT7"
FT HELIX 762..764
FT /evidence="ECO:0007829|PDB:7NUW"
FT HELIX 765..777
FT /evidence="ECO:0007829|PDB:7NUW"
SQ SEQUENCE 786 AA; 90291 MW; 1BFCCC5E42EA5242 CRC64;
MTSIFHFAII FMLILQIRIQ LSEESEFLVD RSKNGLIHVP KDLSQKTTIL NISQNYISEL
WTSDILSLSK LRILIISHNR IQYLDISVFK FNQELEYLDL SHNKLVKISC HPTVNLKHLD
LSFNAFDALP ICKEFGNMSQ LKFLGLSTTH LEKSSVLPIA HLNISKVLLV LGETYGEKED
PEGLQDFNTE SLHIVFPTNK EFHFILDVSV KTVANLELSN IKCVLEDNKC SYFLSILAKL
QTNPKLSNLT LNNIETTWNS FIRILQLVWH TTVWYFSISN VKLQGQLDFR DFDYSGTSLK
ALSIHQVVSD VFGFPQSYIY EIFSNMNIKN FTVSGTRMVH MLCPSKISPF LHLDFSNNLL
TDTVFENCGH LTELETLILQ MNQLKELSKI AEMTTQMKSL QQLDISQNSV SYDEKKGDCS
WTKSLLSLNM SSNILTDTIF RCLPPRIKVL DLHSNKIKSI PKQVVKLEAL QELNVAFNSL
TDLPGCGSFS SLSVLIIDHN SVSHPSADFF QSCQKMRSIK AGDNPFQCTC ELGEFVKNID
QVSSEVLEGW PDSYKCDYPE SYRGTLLKDF HMSELSCNIT LLIVTIVATM LVLAVTVTSL
CSYLDLPWYL RMVCQWTQTR RRARNIPLEE LQRNLQFHAF ISYSGHDSFW VKNELLPNLE
KEGMQICLHE RNFVPGKSIV ENIITCIEKS YKSIFVLSPN FVQSEWCHYE LYFAHHNLFH
EGSNSLILIL LEPIPQYSIP SSYHKLKSLM ARRTYLEWPK EKSKRGLFWA NLRAAINIKL
TEQAKK
