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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.
17-JUN-2020, entry version 182.
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 OF PUBMED:20865800.
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; 47.
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]
Antibodypedia; 34940; 1035 antibodies.
DNASU; 54106; -.
Ensembl; ENST00000360658; ENSP00000353874; ENSG00000239732. [Q9NR96-1]
GeneID; 54106; -.
KEGG; hsa:54106; -.
UCSC; uc003dda.2; human. [Q9NR96-1]
CTD; 54106; -.
DisGeNET; 54106; -.
EuPathDB; HostDB:ENSG00000239732.3; -.
GeneCards; TLR9; -.
HGNC; HGNC:15633; TLR9.
HPA; ENSG00000239732; Tissue enriched (blood).
MIM; 605474; gene.
neXtProt; NX_Q9NR96; -.
OpenTargets; ENSG00000239732; -.
PharmGKB; PA38010; -.
eggNOG; KOG1747; Eukaryota.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00940000162493; -.
HOGENOM; CLU_006000_2_0_1; -.
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.
BioGRID-ORCS; 54106; 1 hit in 786 CRISPR screens.
GeneWiki; TLR9; -.
GenomeRNAi; 54106; -.
Pharos; Q9NR96; Tclin.
PRO; PR:Q9NR96; -.
Proteomes; UP000005640; Chromosome 3.
RNAct; Q9NR96; protein.
Bgee; ENSG00000239732; Expressed in blood and 68 other tissues.
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:0038187; F:pattern recognition receptor activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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; 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
/evidence="ECO:0000255"
CHAIN 26..1032
/note="Toll-like receptor 9"
/id="PRO_0000034737"
TOPO_DOM 26..818
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 819..839
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 840..1032
/note="Cytoplasmic"
/evidence="ECO:0000255"
REPEAT 62..85
/note="LRR 1"
REPEAT 87..110
/note="LRR 2"
REPEAT 122..147
/note="LRR 3"
REPEAT 150..166
/note="LRR 4"
REPEAT 167..190
/note="LRR 5"
REPEAT 198..221
/note="LRR 6"
REPEAT 223..242
/note="LRR 7"
REPEAT 243..268
/note="LRR 8"
REPEAT 283..306
/note="LRR 9"
REPEAT 308..332
/note="LRR 10"
REPEAT 333..356
/note="LRR 11"
REPEAT 363..386
/note="LRR 12"
REPEAT 390..413
/note="LRR 13"
REPEAT 415..440
/note="LRR 14"
REPEAT 470..494
/note="LRR 15"
REPEAT 496..519
/note="LRR 16"
REPEAT 520..543
/note="LRR 17"
REPEAT 545..572
/note="LRR 18"
REPEAT 574..598
/note="LRR 19"
REPEAT 600..622
/note="LRR 20"
REPEAT 627..650
/note="LRR 21"
REPEAT 652..675
/note="LRR 22"
REPEAT 676..699
/note="LRR 23"
REPEAT 701..723
/note="LRR 24"
REPEAT 724..747
/note="LRR 25"
REPEAT 749..772
/note="LRR 26"
DOMAIN 868..1013
/note="TIR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
REGION 47..51
/note="Interaction with CpG-DNA"
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
REGION 72..77
/note="Interaction with CpG-DNA"
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
REGION 95..109
/note="Interaction with CpG-DNA"
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
REGION 179..181
/note="Interaction with CpG-DNA"
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
BINDING 132
/note="CpG-DNA"
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
BINDING 208
/note="CpG-DNA"
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
CARBOHYD 64
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 129
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 200
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 210
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 242
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 300
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 340
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 469
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 474
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 513
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 567
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 694
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 731
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 35..45
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
DISULFID 98..110
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
DISULFID 178..184
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
DISULFID 255..268
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
DISULFID 258..265
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
DISULFID 470..500
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
DISULFID 764..790
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
DISULFID 766..809
/evidence="ECO:0000250|UniProtKB:Q2EEY0"
VAR_SEQ 1..57
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:11022119"
/id="VSP_006520"
VAR_SEQ 1..16
/note="MGFCRSALHPLSLLVQ -> M (in isoform 5)"
/evidence="ECO:0000303|PubMed:11022120"
/id="VSP_006523"
VAR_SEQ 1
/note="M -> MPMKWSGWRWSWGPATHTALPPPQ (in isoform 3)"
/evidence="ECO:0000303|PubMed:11022120"
/id="VSP_006521"
VAR_SEQ 1
/note="M -> MLYSSCKSRLLDSVEQDFHLEIAKK (in isoform 4)"
/evidence="ECO:0000303|PubMed:11022120"
/id="VSP_006522"
VARIANT 5
/note="R -> C (in dbSNP:rs5743842)"
/id="VAR_024668"
VARIANT 79
/note="H -> Q (in dbSNP:rs5743843)"
/id="VAR_052364"
VARIANT 863
/note="R -> Q (in dbSNP:rs5743845)"
/id="VAR_034555"
VARIANT 882
/note="A -> T (in dbSNP:rs5743846)"
/id="VAR_052365"
VARIANT 901
/note="R -> H (in a colorectal cancer sample; somatic
mutation; dbSNP:rs755472700)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036077"
VARIANT 933
/note="T -> M (in a colorectal cancer sample; somatic
mutation; dbSNP:rs746622200)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036078"
CONFLICT 200
/note="N -> S (in Ref. 7; AAQ89443)"
/evidence="ECO:0000305"
CONFLICT 330
/note="F -> L (in Ref. 7; AAQ89443)"
/evidence="ECO:0000305"
CONFLICT 530
/note="H -> R (in Ref. 2; AAF78037)"
/evidence="ECO:0000305"
CONFLICT 688
/note="Q -> R (in Ref. 2; AAF78037)"
/evidence="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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WP1067: Toll-like receptor signaling pathway
WP1384: Toll-like receptor signaling pathway
WP88: Toll Like Receptor signaling
WP1271: Toll-like receptor signaling pathway
WP75: Toll-like receptor signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP1449: Regulation of toll-like receptor signaling pathway
WP1183: Toll-like receptor signaling pathway
WP2328: Allograft rejection
WP1309: Toll-like receptor signaling pathway
WP949: Toll-like receptor signaling pathway
WP829: Toll-like receptor signaling pathway
WP252: Androgen Receptor Signaling Pathway
WP886: Kit Receptor Signaling Pathway
WP1004: Kit Receptor Signaling Pathway
WP1781: Advanced glycosylation endproduct receptor signaling
WP590: Cardiovascular Signaling
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP733: Serotonin Receptor 2 and STAT3 Signaling
WP1284: EPO Receptor Signaling
WP274: B Cell Receptor Signaling Pathway
WP908: B Cell Receptor Signaling Pathway
WP1025: B Cell Receptor Signaling Pathway
WP1918: Signaling by Robo receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor

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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)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[TLR9] Toll-like receptor 9 (CD antigen CD289)
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[TLR2 TIL4] Toll-like receptor 2 (EC 3.2.2.6) (Toll/interleukin-1 receptor-like protein 4) (CD antigen CD282)
[Tlr1] Toll-like receptor 1 (EC 3.2.2.6) (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)
[Tlr2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR4] Toll-like receptor 4 (EC 3.2.2.6) (hToll) (CD antigen CD284)
[TLR6] Toll-like receptor 6 (EC 3.2.2.6) (CD antigen CD286)
[TLR4] Toll-like receptor 4 (EC 3.2.2.6) (CD antigen CD284)
[CD36 GP3B GP4] Platelet glycoprotein 4 (Fatty acid translocase) (FAT) (Glycoprotein IIIb) (GPIIIB) (Leukocyte differentiation antigen CD36) (PAS IV) (PAS-4) (Platelet collagen receptor) (Platelet glycoprotein IV) (GPIV) (Thrombospondin receptor) (CD antigen CD36)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR1 KIAA0012] Toll-like receptor 1 (EC 3.2.2.6) (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)
[CD300A CMRF35H IGSF12 HSPC083] CMRF35-like molecule 8 (CLM-8) (CD300 antigen-like family member A) (CMRF-35-H9) (CMRF35-H9) (CMRF35-H) (IRC1/IRC2) (Immunoglobulin superfamily member 12) (IgSF12) (Inhibitory receptor protein 60) (IRp60) (NK inhibitory receptor) (CD antigen CD300a)
[Tlr4] Toll-like receptor 4 (Toll4) (EC 3.2.2.6) (CD antigen CD284)
[LILRA5 ILT11 LILRB7 LIR9] Leukocyte immunoglobulin-like receptor subfamily A member 5 (CD85 antigen-like family member F) (Immunoglobulin-like transcript 11) (ILT-11) (Leukocyte immunoglobulin-like receptor 9) (LIR-9) (CD antigen CD85f)
[LILRA4 ILT7] Leukocyte immunoglobulin-like receptor subfamily A member 4 (CD85 antigen-like family member G) (Immunoglobulin-like transcript 7) (ILT-7) (CD antigen CD85g)
[Tlr4 Lps] Toll-like receptor 4 (EC 3.2.2.6) (CD antigen CD284)
[TLR6] Toll-like receptor 6 (EC 3.2.2.6) (CD antigen CD286)
[Tlr6] Toll-like receptor 6 (EC 3.2.2.6) (CD antigen CD286)
[Cd44 Ly-24] CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Lymphocyte antigen 24) (Ly-24) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[TLR4] Toll-like receptor 4 (EC 3.2.2.6) (CD antigen CD284)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)

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[31335975] CD93 is a cell surface lectin receptor involved in the control of the inflammatory response stimulated by exogenous DNA.
[31010295] Photodynamic Therapy for Genital Warts Causes Activation of Local Immunity.
[30951392] Emerging views of mitophagy in immunity and autoimmune diseases.
[30822302] TLR9-mediated dendritic cell activation uncovers mammalian ganglioside species with specific ceramide backbones that activate invariant natural killer T cells.
[30761150] Toll-Like Receptor Signaling Drives Btk-Mediated Autoimmune Disease.
[30498494] CD180 Ligation Inhibits TLR7- and TLR9-Mediated Activation of Macrophages and Dendritic Cells Through the Lyn-SHP-1/2 Axis in Murine Lupus.
[30177023] Murine Models of Human IgA Nephropathy.
[30166549] Interferon priming is essential for human CD34+ cell-derived plasmacytoid dendritic cell maturation and function.
[29981383] Hydroxychloroquine efficiently suppresses inflammatory responses of human class-switched memory B cells via Toll-like receptor 9 inhibition.