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Toll-like receptor 9 (CD antigen CD289)

 TLR9_HUMAN              Reviewed;        1032 AA.
Q9NR96; B3Y661; D1CS56; Q6UVZ2; Q9HD68; Q9HD69; Q9HD70; Q9NYC2;
Q9NYC3;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
31-JAN-2002, sequence version 2.
16-OCT-2019, entry version 178.
RecName: Full=Toll-like receptor 9;
AltName: CD_antigen=CD289;
Flags: Precursor;
Name=TLR9; ORFNames=UNQ5798/PRO19605;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Monocytic leukemia;
PubMed=11022119;
Du X., Poltorak A., Wei Y., Beutler B.;
"Three novel mammalian Toll-like receptors: gene structure,
expression, and evolution.";
Eur. Cytokine Netw. 11:362-371(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5).
TISSUE=Placenta;
PubMed=11022120;
Chuang T.-H., Ulevitch R.J.;
"Cloning and characterization of a sub-family of human Toll-like
receptors: hTLR7, hTLR8 and hTLR9.";
Eur. Cytokine Netw. 11:372-378(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11130078; DOI=10.1038/35047123;
Hemmi H., Takeuchi O., Kawai T., Kaisho T., Sato S., Sanjo H.,
Matsumoto M., Hoshino K., Wagner H., Takeda K., Akira S.;
"A Toll-like receptor recognizes bacterial DNA.";
Nature 408:740-745(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Liu Z., Wang J., Xiao W.;
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
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).
[10]
FUNCTION.
PubMed=11564765; DOI=10.4049/jimmunol.167.7.3555;
Takeshita F., Leifer C.A., Gursel I., Ishii K.J., Takeshita S.,
Gursel M., Klinman D.M.;
"Role of Toll-like receptor 9 in CpG DNA-induced activation of human
cells.";
J. Immunol. 167:3555-3558(2001).
[11]
FUNCTION, AND INTERACTION WITH BTK.
PubMed=17932028; DOI=10.1074/jbc.m707682200;
Doyle S.L., Jefferies C.A., Feighery C., O'Neill L.A.;
"Signaling by Toll-like receptors 8 and 9 requires Bruton's tyrosine
kinase.";
J. Biol. Chem. 282:36953-36960(2007).
[12]
INTERACTION WITH CNPY3 AND HSP90B1.
PubMed=20865800; DOI=10.1038/ncomms1070;
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y.,
Hao B., Bona R., Han D., Li Z.;
"Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a
substrate-specific cochaperone.";
Nat. Commun. 1:79-79(2010).
[13]
ERRATUM.
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y.,
Hao B., Bona R., Han D., Li Z.;
Nat. Commun. 3:653-653(2012).
[14]
FUNCTION.
PubMed=23857366; DOI=10.1002/eji.201243068;
Li F.J., Schreeder D.M., Li R., Wu J., Davis R.S.;
"FCRL3 promotes TLR9-induced B-cell activation and suppresses plasma
cell differentiation.";
Eur. J. Immunol. 43:2980-2992(2013).
[15]
VARIANTS [LARGE SCALE ANALYSIS] HIS-901 AND MET-933.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Key component of innate and adaptive immunity. TLRs
(Toll-like receptors) control host immune response against
pathogens through recognition of molecular patterns specific to
microorganisms. TLR9 is a nucleotide-sensing TLR which is
activated by unmethylated cytidine-phosphate-guanosine (CpG)
dinucleotides. Acts via MYD88 and TRAF6, leading to NF-kappa-B
activation, cytokine secretion and the inflammatory response
(PubMed:11564765, PubMed:17932028). Controls lymphocyte response
to Helicobacter infection (By similarity). Upon CpG stimulation,
induces B-cell proliferation, activation, survival and antibody
production (PubMed:23857366). {ECO:0000250|UniProtKB:Q9EQU3,
ECO:0000269|PubMed:11564765, ECO:0000269|PubMed:17932028,
ECO:0000269|PubMed:23857366}.
-!- SUBUNIT: Monomer and homodimer. Exists as a monomer in the absence
of unmethylated cytidine-phosphate-guanosine (CpG) ligand.
Proteolytic processing of an insertion loop (Z-loop) is required
for homodimerization upon binding to the unmethylated CpG ligand
leading to its activation (By similarity). Interacts with MYD88
via their respective TIR domains (By similarity). Interacts with
BTK (PubMed:17932028). Interacts (via transmembrane domain) with
UNC93B1. Interacts with CD300LH; the interaction may promote full
activation of TLR9-triggered innate responses (By similarity).
Interacts with CNPY3 and HSP90B1; this interaction is required for
proper folding in the endoplasmic reticulum (PubMed:20865800).
Interacts with SMPDL3B (By similarity).
{ECO:0000250|UniProtKB:Q2EEY0, ECO:0000250|UniProtKB:Q9EQU3,
ECO:0000269|PubMed:17932028, ECO:0000269|PubMed:20865800}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9EQU3}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q9EQU3}. Endosome
{ECO:0000250|UniProtKB:Q9EQU3}. Lysosome
{ECO:0000250|UniProtKB:Q9EQU3}. Cytoplasmic vesicle, phagosome
{ECO:0000250|UniProtKB:Q9EQU3}. Note=Relocalizes from endoplasmic
reticulum to endosome and lysosome upon stimulation with agonist.
Exit from the ER requires UNC93B1. Endolysosomal localization is
required for proteolytic cleavage and subsequent activation.
Intracellular localization of the active receptor may prevent from
responding to self nucleic acid. {ECO:0000250|UniProtKB:Q9EQU3}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=A;
IsoId=Q9NR96-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=Q9NR96-2; Sequence=VSP_006520;
Name=3;
IsoId=Q9NR96-3; Sequence=VSP_006521;
Name=4;
IsoId=Q9NR96-4; Sequence=VSP_006522;
Name=5;
IsoId=Q9NR96-5; Sequence=VSP_006523;
-!- TISSUE SPECIFICITY: Highly expressed in spleen, lymph node, tonsil
and peripheral blood leukocytes, especially in plasmacytoid pre-
dendritic cells. Levels are much lower in monocytes and CD11c+
immature dendritic cells. Also detected in lung and liver.
-!- PTM: Activated by proteolytic cleavage of the flexible loop
between repeats LRR14 and LRR15 within the ectodomain. Cleavage
requires UNC93B1. Proteolytically processed by first removing the
majority of the ectodomain by either asparagine endopeptidase
(AEP) or a cathepsin followed by a trimming event that is solely
cathepsin mediated and required for optimal receptor signaling.
{ECO:0000250|UniProtKB:Q9EQU3}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
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EMBL; AF259262; AAF72189.1; -; mRNA.
EMBL; AF259263; AAF72190.1; -; mRNA.
EMBL; AF245704; AAF78037.1; -; mRNA.
EMBL; AF246972; AAG01734.1; -; mRNA.
EMBL; AF246973; AAG01735.1; -; mRNA.
EMBL; AF246974; AAG01736.1; -; mRNA.
EMBL; AB045180; BAB19259.1; -; mRNA.
EMBL; EU170540; ABW37075.1; -; Genomic_DNA.
EMBL; EU170541; ABW37076.1; -; Genomic_DNA.
EMBL; EU170542; ABW37077.1; -; Genomic_DNA.
EMBL; EU170543; ABW37078.1; -; Genomic_DNA.
EMBL; AB445673; BAG55070.1; -; mRNA.
EMBL; DQ019992; AAZ95513.1; -; Genomic_DNA.
EMBL; DQ019993; AAZ95514.1; -; Genomic_DNA.
EMBL; DQ019994; AAZ95515.1; -; Genomic_DNA.
EMBL; DQ019995; AAZ95516.1; -; Genomic_DNA.
EMBL; DQ019996; AAZ95517.1; -; Genomic_DNA.
EMBL; DQ019999; AAZ95520.1; -; Genomic_DNA.
EMBL; AY359085; AAQ89443.1; -; mRNA.
EMBL; CH471055; EAW65191.1; -; Genomic_DNA.
EMBL; BC032713; AAH32713.1; -; mRNA.
CCDS; CCDS2848.1; -. [Q9NR96-1]
RefSeq; NP_059138.1; NM_017442.3. [Q9NR96-1]
SMR; Q9NR96; -.
BioGrid; 119902; 46.
DIP; DIP-52371N; -.
IntAct; Q9NR96; 13.
STRING; 9606.ENSP00000417517; -.
BindingDB; Q9NR96; -.
ChEMBL; CHEMBL5804; -.
DrugBank; DB00608; Chloroquine.
DrugBank; DB05530; CPG 10101.
DrugBank; DB05475; Golotimod.
DrugBank; DB01611; Hydroxychloroquine.
DrugBank; DB05463; ISS-1018.
DrugCentral; Q9NR96; -.
GuidetoPHARMACOLOGY; 1759; -.
iPTMnet; Q9NR96; -.
PhosphoSitePlus; Q9NR96; -.
BioMuta; TLR9; -.
DMDM; 20140872; -.
jPOST; Q9NR96; -.
MassIVE; Q9NR96; -.
MaxQB; Q9NR96; -.
PaxDb; Q9NR96; -.
PeptideAtlas; Q9NR96; -.
PRIDE; Q9NR96; -.
ProteomicsDB; 82308; -. [Q9NR96-1]
ProteomicsDB; 82309; -. [Q9NR96-2]
ProteomicsDB; 82310; -. [Q9NR96-3]
ProteomicsDB; 82311; -. [Q9NR96-4]
ProteomicsDB; 82312; -. [Q9NR96-5]
DNASU; 54106; -.
Ensembl; ENST00000360658; ENSP00000353874; ENSG00000239732. [Q9NR96-1]
GeneID; 54106; -.
KEGG; hsa:54106; -.
UCSC; uc003dda.2; human. [Q9NR96-1]
CTD; 54106; -.
DisGeNET; 54106; -.
GeneCards; TLR9; -.
HGNC; HGNC:15633; TLR9.
MIM; 605474; gene.
neXtProt; NX_Q9NR96; -.
OpenTargets; ENSG00000239732; -.
PharmGKB; PA38010; -.
eggNOG; KOG1747; Eukaryota.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00940000162493; -.
InParanoid; Q9NR96; -.
KO; K10161; -.
OrthoDB; 264244at2759; -.
PhylomeDB; Q9NR96; -.
TreeFam; TF325595; -.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-HSA-168138; Toll Like Receptor 9 (TLR9) Cascade.
Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-HSA-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
Reactome; R-HSA-975155; MyD88 dependent cascade initiated on endosome.
GeneWiki; TLR9; -.
GenomeRNAi; 54106; -.
Pharos; Q9NR96; -.
PRO; PR:Q9NR96; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000239732; Expressed in 69 organ(s), highest expression level in blood.
Genevisible; Q9NR96; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
GO; GO:0036019; C:endolysosome; ISS:UniProtKB.
GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0005149; F:interleukin-1 receptor binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0008329; F:signaling pattern recognition receptor activity; IBA:GO_Central.
GO; GO:0035197; F:siRNA binding; IMP:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0045322; F:unmethylated CpG binding; ISS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; NAS:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0007252; P:I-kappaB phosphorylation; IDA:BHF-UCL.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISS:BHF-UCL.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
GO; GO:1901895; P:negative regulation of ATPase-coupled calcium transmembrane transporter activity; IDA:CACAO.
GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:BHF-UCL.
GO; GO:0032717; P:negative regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0050871; P:positive regulation of B cell activation; IDA:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:UniProtKB.
GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:CACAO.
GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:CACAO.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
GO; GO:0002639; P:positive regulation of immunoglobulin production; IDA:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0045356; P:positive regulation of interferon-alpha biosynthetic process; IDA:UniProtKB.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; IDA:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:BHF-UCL.
GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; IDA:UniProtKB.
GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:BHF-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
GO; GO:0032741; P:positive regulation of interleukin-18 production; ISS:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; IBA:GO_Central.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:0046330; P:positive regulation of JNK cascade; IC:BHF-UCL.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:BHF-UCL.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISS:BHF-UCL.
GO; GO:0034123; P:positive regulation of toll-like receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:BHF-UCL.
GO; GO:0045577; P:regulation of B cell differentiation; IDA:UniProtKB.
GO; GO:0050707; P:regulation of cytokine secretion; IEA:InterPro.
GO; GO:0034163; P:regulation of toll-like receptor 9 signaling pathway; IDA:UniProtKB.
GO; GO:0002237; P:response to molecule of bacterial origin; TAS:BHF-UCL.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
GO; GO:0032640; P:tumor necrosis factor production; IDA:CACAO.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR041283; LRR_12.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027181; TLR9.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR47410:SF3; PTHR47410:SF3; 1.
Pfam; PF18837; LRR_12; 1.
Pfam; PF13516; LRR_6; 2.
Pfam; PF13855; LRR_8; 7.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 18.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 17.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasmic vesicle;
Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein;
Immunity; Inflammatory response; Innate immunity; Leucine-rich repeat;
Lysosome; Membrane; Polymorphism; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1032 Toll-like receptor 9.
/FTId=PRO_0000034737.
TOPO_DOM 26 818 Extracellular. {ECO:0000255}.
TRANSMEM 819 839 Helical. {ECO:0000255}.
TOPO_DOM 840 1032 Cytoplasmic. {ECO:0000255}.
REPEAT 62 85 LRR 1.
REPEAT 87 110 LRR 2.
REPEAT 122 147 LRR 3.
REPEAT 150 166 LRR 4.
REPEAT 167 190 LRR 5.
REPEAT 198 221 LRR 6.
REPEAT 223 242 LRR 7.
REPEAT 243 268 LRR 8.
REPEAT 283 306 LRR 9.
REPEAT 308 332 LRR 10.
REPEAT 333 356 LRR 11.
REPEAT 363 386 LRR 12.
REPEAT 390 413 LRR 13.
REPEAT 415 440 LRR 14.
REPEAT 470 494 LRR 15.
REPEAT 496 519 LRR 16.
REPEAT 520 543 LRR 17.
REPEAT 545 572 LRR 18.
REPEAT 574 598 LRR 19.
REPEAT 600 622 LRR 20.
REPEAT 627 650 LRR 21.
REPEAT 652 675 LRR 22.
REPEAT 676 699 LRR 23.
REPEAT 701 723 LRR 24.
REPEAT 724 747 LRR 25.
REPEAT 749 772 LRR 26.
DOMAIN 868 1016 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
REGION 47 51 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
REGION 72 77 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
REGION 95 109 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
REGION 179 181 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
BINDING 132 132 CpG-DNA. {ECO:0000250|UniProtKB:Q2EEY0}.
BINDING 208 208 CpG-DNA. {ECO:0000250|UniProtKB:Q2EEY0}.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 469 469 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 474 474 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 567 567 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 694 694 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 731 731 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 45 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 98 110 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 178 184 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 255 268 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 258 265 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 470 500 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 764 790 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 766 809 {ECO:0000250|UniProtKB:Q2EEY0}.
VAR_SEQ 1 57 Missing (in isoform 2).
{ECO:0000303|PubMed:11022119}.
/FTId=VSP_006520.
VAR_SEQ 1 16 MGFCRSALHPLSLLVQ -> M (in isoform 5).
{ECO:0000303|PubMed:11022120}.
/FTId=VSP_006523.
VAR_SEQ 1 1 M -> MPMKWSGWRWSWGPATHTALPPPQ (in isoform
3). {ECO:0000303|PubMed:11022120}.
/FTId=VSP_006521.
VAR_SEQ 1 1 M -> MLYSSCKSRLLDSVEQDFHLEIAKK (in
isoform 4).
{ECO:0000303|PubMed:11022120}.
/FTId=VSP_006522.
VARIANT 5 5 R -> C (in dbSNP:rs5743842).
/FTId=VAR_024668.
VARIANT 79 79 H -> Q (in dbSNP:rs5743843).
/FTId=VAR_052364.
VARIANT 863 863 R -> Q (in dbSNP:rs5743845).
/FTId=VAR_034555.
VARIANT 882 882 A -> T (in dbSNP:rs5743846).
/FTId=VAR_052365.
VARIANT 901 901 R -> H (in a colorectal cancer sample;
somatic mutation; dbSNP:rs755472700).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036077.
VARIANT 933 933 T -> M (in a colorectal cancer sample;
somatic mutation; dbSNP:rs746622200).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036078.
CONFLICT 200 200 N -> S (in Ref. 7; AAQ89443).
{ECO:0000305}.
CONFLICT 330 330 F -> L (in Ref. 7; AAQ89443).
{ECO:0000305}.
CONFLICT 530 530 H -> R (in Ref. 2; AAF78037).
{ECO:0000305}.
CONFLICT 688 688 Q -> R (in Ref. 2; AAF78037).
{ECO:0000305}.
SEQUENCE 1032 AA; 115860 MW; 71280AA9680EDCE2 CRC64;
MGFCRSALHP LSLLVQAIML AMTLALGTLP AFLPCELQPH GLVNCNWLFL KSVPHFSMAA
PRGNVTSLSL SSNRIHHLHD SDFAHLPSLR HLNLKWNCPP VGLSPMHFPC HMTIEPSTFL
AVPTLEELNL SYNNIMTVPA LPKSLISLSL SHTNILMLDS ASLAGLHALR FLFMDGNCYY
KNPCRQALEV APGALLGLGN LTHLSLKYNN LTVVPRNLPS SLEYLLLSYN RIVKLAPEDL
ANLTALRVLD VGGNCRRCDH APNPCMECPR HFPQLHPDTF SHLSRLEGLV LKDSSLSWLN
ASWFRGLGNL RVLDLSENFL YKCITKTKAF QGLTQLRKLN LSFNYQKRVS FAHLSLAPSF
GSLVALKELD MHGIFFRSLD ETTLRPLARL PMLQTLRLQM NFINQAQLGI FRAFPGLRYV
DLSDNRISGA SELTATMGEA DGGEKVWLQP GDLAPAPVDT PSSEDFRPNC STLNFTLDLS
RNNLVTVQPE MFAQLSHLQC LRLSHNCISQ AVNGSQFLPL TGLQVLDLSH NKLDLYHEHS
FTELPRLEAL DLSYNSQPFG MQGVGHNFSF VAHLRTLRHL SLAHNNIHSQ VSQQLCSTSL
RALDFSGNAL GHMWAEGDLY LHFFQGLSGL IWLDLSQNRL HTLLPQTLRN LPKSLQVLRL
RDNYLAFFKW WSLHFLPKLE VLDLAGNQLK ALTNGSLPAG TRLRRLDVSC NSISFVAPGF
FSKAKELREL NLSANALKTV DHSWFGPLAS ALQILDVSAN PLHCACGAAF MDFLLEVQAA
VPGLPSRVKC GSPGQLQGLS IFAQDLRLCL DEALSWDCFA LSLLAVALGL GVPMLHHLCG
WDLWYCFHLC LAWLPWRGRQ SGRDEDALPY DAFVVFDKTQ SAVADWVYNE LRGQLEECRG
RWALRLCLEE RDWLPGKTLF ENLWASVYGS RKTLFVLAHT DRVSGLLRAS FLLAQQRLLE
DRKDVVVLVI LSPDGRRSRY VRLRQRLCRQ SVLLWPHQPS GQRSFWAQLG MALTRDNHHF
YNRNFCQGPT AE


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[Tlr9] Toll-like receptor 9 (CD antigen CD289)
[TLR9 UNQ5798/PRO19605] Toll-like receptor 9 (CD antigen CD289)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
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[Tlr1] Toll-like receptor 1 (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)
[Tlr2] Toll-like receptor 2 (CD antigen CD282)
[TLR4] Toll-like receptor 4 (hToll) (CD antigen CD284)
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[TLR6] Toll-like receptor 6 (CD antigen CD286)
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Bibliography :
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