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Protein

Toll-like receptor 9

Gene

Tlr9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Plays a role in defense against systemic mouse cytomegalovirus infection. Controls lymphocyte response to Helicobacter infection.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_271614. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
REACT_297122. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_332866. PI3K Cascade.
REACT_338311. Trafficking and processing of endosomal TLR.
REACT_346614. Toll Like Receptor 9 (TLR9) Cascade.
REACT_348851. MyD88 dependent cascade initiated on endosome.

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-like receptor 9
Alternative name(s):
CD_antigen: CD289
Gene namesi
Name:Tlr9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1932389. Tlr9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 818793ExtracellularSequence AnalysisAdd
BLAST
Transmembranei819 – 83921HelicalSequence AnalysisAdd
BLAST
Topological domaini840 – 1032193CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • basolateral plasma membrane Source: MGI
  • cytoplasm Source: MGI
  • early phagosome Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • endosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • lysosome Source: UniProtKB
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Lysosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Reduced proliferation of lymphocytes, reduced interferon-gamma production by splenocytes and reduced neutrophil numbers following Helicobacter infection.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi499 – 4991L → P: Highly susceptible to mouse cytomegalovirus infection. Shows low level of cytokine induction and natural killer activation on viral infection. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 10321007Toll-like receptor 9PRO_0000034738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi495 – 4951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi514 – 5141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi568 – 5681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi670 – 6701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi695 – 6951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi700 – 7001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi732 – 7321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi752 – 7521N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9EQU3.
PRIDEiQ9EQU3.

PTM databases

PhosphoSiteiQ9EQU3.

Expressioni

Tissue specificityi

Expressed in the basolateral region of gastric epithelial cells with high levels detected in antrum and body mucosa (at protein level). Detected in spleen and stomach at higher levels in C57BL/6 mice than BALB/C.1 Publication

Inductioni

Following Helicobacter infection, down-regulated in C57BL/6 mice and up-regulated in BALB/C mice.1 Publication

Gene expression databases

BgeeiQ9EQU3.
CleanExiMM_TLR9.
GenevestigatoriQ9EQU3.

Interactioni

Subunit structurei

Interacts with MYD88 via their respective TIR domains (By similarity). Interacts with BTK (By similarity). Interacts (via transmembrane domain) with UNC93B1. Interacts with CD300LH; the interaction may promote full activation of TLR9-triggered innate responses. Interacts with CNPY3 and HSP90B1; this interaction is required for proper folding in the endoplasmic reticulum.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Atp2a2P115074EBI-9979528,EBI-916319From a different organism.

Protein-protein interaction databases

IntActiQ9EQU3. 28 interactions.
STRINGi10090.ENSMUSP00000082207.

Structurei

Secondary structure

1
1032
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni31 – 344Combined sources
Beta strandi35 – 384Combined sources
Turni39 – 413Combined sources
Beta strandi42 – 443Combined sources
Beta strandi67 – 693Combined sources
Turni80 – 834Combined sources
Helixi84 – 863Combined sources
Beta strandi90 – 934Combined sources
Beta strandi100 – 1023Combined sources
Turni116 – 1216Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi147 – 1493Combined sources
Helixi160 – 1634Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi177 – 1793Combined sources
Turni192 – 1976Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi223 – 2264Combined sources
Helixi237 – 2393Combined sources
Beta strandi247 – 2504Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi269 – 2724Combined sources
Turni277 – 2826Combined sources
Beta strandi288 – 2903Combined sources
Helixi301 – 3044Combined sources
Beta strandi312 – 3143Combined sources
Beta strandi317 – 3193Combined sources
Helixi321 – 3244Combined sources
Helixi329 – 3324Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi347 – 3493Combined sources
Helixi358 – 3625Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi377 – 3793Combined sources
Turni381 – 3844Combined sources
Helixi385 – 3873Combined sources
Beta strandi395 – 3973Combined sources
Helixi408 – 4125Combined sources
Beta strandi413 – 4164Combined sources
Beta strandi419 – 4213Combined sources
Beta strandi473 – 4753Combined sources
Beta strandi477 – 4793Combined sources
Helixi490 – 4934Combined sources
Beta strandi501 – 5033Combined sources
Turni517 – 5204Combined sources
Beta strandi526 – 5283Combined sources
Turni539 – 5446Combined sources
Beta strandi550 – 5523Combined sources
Helixi570 – 5745Combined sources
Beta strandi580 – 5823Combined sources
Beta strandi590 – 5923Combined sources
Beta strandi597 – 6004Combined sources
Beta strandi603 – 6053Combined sources
Helixi611 – 6155Combined sources
Turni620 – 6267Combined sources
Beta strandi633 – 6353Combined sources
Helixi646 – 6505Combined sources
Beta strandi658 – 6603Combined sources
Helixi671 – 6766Combined sources
Beta strandi682 – 6843Combined sources
Beta strandi706 – 7083Combined sources
Turni719 – 7246Combined sources
Beta strandi730 – 7323Combined sources
Helixi743 – 7453Combined sources
Helixi747 – 7515Combined sources
Beta strandi754 – 7574Combined sources
Helixi771 – 7777Combined sources
Helixi779 – 7813Combined sources
Turni783 – 7886Combined sources
Beta strandi789 – 7946Combined sources
Turni795 – 7973Combined sources
Helixi807 – 8093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WPFX-ray1.96A26-818[»]
3WPGX-ray2.25A26-818[»]
3WPHX-ray2.33A26-818[»]
3WPIX-ray2.25A26-818[»]
4QDHX-ray2.40A/B480-753[»]
ProteinModelPortaliQ9EQU3.
SMRiQ9EQU3. Positions 34-1013.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati62 – 8524LRR 1Add
BLAST
Repeati87 – 11024LRR 2Add
BLAST
Repeati122 – 14726LRR 3Add
BLAST
Repeati150 – 16617LRR 4Add
BLAST
Repeati167 – 19024LRR 5Add
BLAST
Repeati198 – 22124LRR 6Add
BLAST
Repeati223 – 24220LRR 7Add
BLAST
Repeati243 – 26826LRR 8Add
BLAST
Repeati283 – 30624LRR 9Add
BLAST
Repeati308 – 33225LRR 10Add
BLAST
Repeati333 – 35624LRR 11Add
BLAST
Repeati363 – 38624LRR 12Add
BLAST
Repeati390 – 41324LRR 13Add
BLAST
Repeati415 – 44026LRR 14Add
BLAST
Repeati471 – 49525LRR 15Add
BLAST
Repeati497 – 52024LRR 16Add
BLAST
Repeati521 – 54424LRR 17Add
BLAST
Repeati546 – 57328LRR 18Add
BLAST
Repeati575 – 59925LRR 19Add
BLAST
Repeati601 – 62323LRR 20Add
BLAST
Repeati628 – 65124LRR 21Add
BLAST
Repeati653 – 67624LRR 22Add
BLAST
Repeati677 – 70024LRR 23Add
BLAST
Repeati702 – 72423LRR 24Add
BLAST
Repeati725 – 74824LRR 25Add
BLAST
Repeati750 – 77324LRR 26Add
BLAST
Domaini868 – 1016149TIRPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated
Contains 26 LRR (leucine-rich) repeats.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000230468.
HOVERGENiHBG018601.
InParanoidiQ9EQU3.
KOiK10161.
OMAiVNCNWLF.
OrthoDBiEOG7C8GGD.
TreeFamiTF325595.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027181. TLR9.
[Graphical view]
PANTHERiPTHR24373:SF37. PTHR24373:SF37. 1 hit.
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 5 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 1 hit.
[Graphical view]
SUPFAMiSSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 16 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9EQU3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLRRRTLHP LSLLVQAAVL AETLALGTLP AFLPCELKPH GLVDCNWLFL
60 70 80 90 100
KSVPRFSAAA SCSNITRLSL ISNRIHHLHN SDFVHLSNLR QLNLKWNCPP
110 120 130 140 150
TGLSPLHFSC HMTIEPRTFL AMRTLEELNL SYNGITTVPR LPSSLVNLSL
160 170 180 190 200
SHTNILVLDA NSLAGLYSLR VLFMDGNCYY KNPCTGAVKV TPGALLGLSN
210 220 230 240 250
LTHLSLKYNN LTKVPRQLPP SLEYLLVSYN LIVKLGPEDL ANLTSLRVLD
260 270 280 290 300
VGGNCRRCDH APNPCIECGQ KSLHLHPETF HHLSHLEGLV LKDSSLHTLN
310 320 330 340 350
SSWFQGLVNL SVLDLSENFL YESITHTNAF QNLTRLRKLN LSFNYRKKVS
360 370 380 390 400
FARLHLASSF KNLVSLQELN MNGIFFRLLN KYTLRWLADL PKLHTLHLQM
410 420 430 440 450
NFINQAQLSI FGTFRALRFV DLSDNRISGP STLSEATPEE ADDAEQEELL
460 470 480 490 500
SADPHPAPLS TPASKNFMDR CKNFKFTMDL SRNNLVTIKP EMFVNLSRLQ
510 520 530 540 550
CLSLSHNSIA QAVNGSQFLP LTNLQVLDLS HNKLDLYHWK SFSELPQLQA
560 570 580 590 600
LDLSYNSQPF SMKGIGHNFS FVTHLSMLQS LSLAHNDIHT RVSSHLNSNS
610 620 630 640 650
VRFLDFSGNG MGRMWDEGGL YLHFFQGLSG LLKLDLSQNN LHILRPQNLD
660 670 680 690 700
NLPKSLKLLS LRDNYLSFFN WTSLSFLPNL EVLDLAGNQL KALTNGTLPN
710 720 730 740 750
GTLLQKLDVS SNSIVSVVPA FFALAVELKE VNLSHNILKT VDRSWFGPIV
760 770 780 790 800
MNLTVLDVRS NPLHCACGAA FVDLLLEVQT KVPGLANGVK CGSPGQLQGR
810 820 830 840 850
SIFAQDLRLC LDEVLSWDCF GLSLLAVAVG MVVPILHHLC GWDVWYCFHL
860 870 880 890 900
CLAWLPLLAR SRRSAQTLPY DAFVVFDKAQ SAVADWVYNE LRVRLEERRG
910 920 930 940 950
RRALRLCLED RDWLPGQTLF ENLWASIYGS RKTLFVLAHT DRVSGLLRTS
960 970 980 990 1000
FLLAQQRLLE DRKDVVVLVI LRPDAHRSRY VRLRQRLCRQ SVLFWPQQPN
1010 1020 1030
GQGGFWAQLS TALTRDNRHF YNQNFCRGPT AE
Length:1,032
Mass (Da):116,412
Last modified:December 14, 2011 - v3
Checksum:iC13A7888588CE297
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti325 – 3251T → N in BAB19260 (PubMed:11130078).Curated
Sequence conflicti325 – 3251T → N in AAK29625 (PubMed:11470918).Curated
Sequence conflicti325 – 3251T → N in AAK28488 (PubMed:11867692).Curated
Sequence conflicti325 – 3251T → N in AAU04980 (PubMed:17474149).Curated
Sequence conflicti378 – 3781L → S in BAB19260 (PubMed:11130078).Curated
Sequence conflicti378 – 3781L → S in AAK29625 (PubMed:11470918).Curated
Sequence conflicti378 – 3781L → S in AAK28488 (PubMed:11867692).Curated
Sequence conflicti378 – 3781L → S in AAU04980 (PubMed:17474149).Curated
Sequence conflicti554 – 5541S → G in AAK28488 (PubMed:11867692).Curated
Sequence conflicti562 – 5621M → I in AAK28488 (PubMed:11867692).Curated
Sequence conflicti573 – 5731T → A in AAK29625 (PubMed:11470918).Curated
Sequence conflicti573 – 5731T → A in AAK28488 (PubMed:11867692).Curated
Sequence conflicti573 – 5731T → A in AAU04980 (PubMed:17474149).Curated
Sequence conflicti579 – 5791Q → H in AAK29625 (PubMed:11470918).Curated
Sequence conflicti579 – 5791Q → H in AAK28488 (PubMed:11867692).Curated
Sequence conflicti579 – 5791Q → H in AAU04980 (PubMed:17474149).Curated
Sequence conflicti867 – 8671T → A in AAK29625 (PubMed:11470918).Curated
Sequence conflicti867 – 8671T → A in AAK28488 (PubMed:11867692).Curated
Sequence conflicti867 – 8671T → A in AAU04980 (PubMed:17474149).Curated
Sequence conflicti897 – 8971E → G in AAK28488 (PubMed:11867692).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045181 mRNA. Translation: BAB19260.1.
AF348140 mRNA. Translation: AAK29625.1.
AF314224 mRNA. Translation: AAK28488.1.
AC164430 Genomic DNA. No translation available.
AY649790 Genomic DNA. Translation: AAU04980.1.
AY649791 Genomic DNA. Translation: AAU04981.1.
CCDSiCCDS40755.1.
RefSeqiNP_112455.2. NM_031178.2.
UniGeneiMm.44889.

Genome annotation databases

EnsembliENSMUST00000062241; ENSMUSP00000082207; ENSMUSG00000045322.
GeneIDi81897.
KEGGimmu:81897.
UCSCiuc009rjh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045181 mRNA. Translation: BAB19260.1.
AF348140 mRNA. Translation: AAK29625.1.
AF314224 mRNA. Translation: AAK28488.1.
AC164430 Genomic DNA. No translation available.
AY649790 Genomic DNA. Translation: AAU04980.1.
AY649791 Genomic DNA. Translation: AAU04981.1.
CCDSiCCDS40755.1.
RefSeqiNP_112455.2. NM_031178.2.
UniGeneiMm.44889.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WPFX-ray1.96A26-818[»]
3WPGX-ray2.25A26-818[»]
3WPHX-ray2.33A26-818[»]
3WPIX-ray2.25A26-818[»]
4QDHX-ray2.40A/B480-753[»]
ProteinModelPortaliQ9EQU3.
SMRiQ9EQU3. Positions 34-1013.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9EQU3. 28 interactions.
STRINGi10090.ENSMUSP00000082207.

Chemistry

ChEMBLiCHEMBL6128.

PTM databases

PhosphoSiteiQ9EQU3.

Proteomic databases

PaxDbiQ9EQU3.
PRIDEiQ9EQU3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062241; ENSMUSP00000082207; ENSMUSG00000045322.
GeneIDi81897.
KEGGimmu:81897.
UCSCiuc009rjh.1. mouse.

Organism-specific databases

CTDi54106.
MGIiMGI:1932389. Tlr9.

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000230468.
HOVERGENiHBG018601.
InParanoidiQ9EQU3.
KOiK10161.
OMAiVNCNWLF.
OrthoDBiEOG7C8GGD.
TreeFamiTF325595.

Enzyme and pathway databases

ReactomeiREACT_271614. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
REACT_297122. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_332866. PI3K Cascade.
REACT_338311. Trafficking and processing of endosomal TLR.
REACT_346614. Toll Like Receptor 9 (TLR9) Cascade.
REACT_348851. MyD88 dependent cascade initiated on endosome.

Miscellaneous databases

NextBioi350461.
PROiQ9EQU3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQU3.
CleanExiMM_TLR9.
GenevestigatoriQ9EQU3.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027181. TLR9.
[Graphical view]
PANTHERiPTHR24373:SF37. PTHR24373:SF37. 1 hit.
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 5 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 1 hit.
[Graphical view]
SUPFAMiSSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 16 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human TLR9 confers responsiveness to bacterial DNA via species-specific CpG motif recognition."
    Bauer S.M., Kirschning C.J., Hacker H., Redecke V., Hausmann S., Akira S., Wagner H., Lipford G.B.
    Proc. Natl. Acad. Sci. U.S.A. 98:9237-9242(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage.
  3. "Toll-like receptor 9 mediates CpG-DNA signaling."
    Chuang T.-H., Lee J., Kline L., Mathison J.C., Ulevitch R.J.
    J. Leukoc. Biol. 71:538-544(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "TLR9 polymorphisms determine murine lymphocyte responses to Helicobacter: results from a genome-wide scan."
    Anderson A.E., Worku M.L., Khamri W., Bamford K.B., Walker M.M., Thursz M.R.
    Eur. J. Immunol. 37:1548-1561(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-964, FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
    Strain: BALB/c and C57BL/6.
  6. "Toll-like receptors 9 and 3 as essential components of innate immune defense against mouse cytomegalovirus infection."
    Tabeta K., Georgel P., Janssen E., Du X., Hoebe K., Crozat K., Mudd S., Shamel L., Sovath S., Goode J., Alexopoulou L., Flavell R.A., Beutler B.
    Proc. Natl. Acad. Sci. U.S.A. 101:3516-3521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYTOMEGALOVIRUS INFECTION, MUTAGENESIS OF LEU-499.
  7. "The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling."
    Brinkmann M.M., Spooner E., Hoebe K., Beutler B., Ploegh H.L., Kim Y.M.
    J. Cell Biol. 177:265-275(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH UNC93B1.
  8. "A single base mutation in the PRAT4A gene reveals differential interaction of PRAT4A with Toll-like receptors."
    Kiyokawa T., Akashi-Takamura S., Shibata T., Matsumoto F., Nishitani C., Kuroki Y., Seto Y., Miyake K.
    Int. Immunol. 20:1407-1415(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNPY3.
  9. "UNC93B1 delivers nucleotide-sensing toll-like receptors to endolysosomes."
    Kim Y.M., Brinkmann M.M., Paquet M.E., Ploegh H.L.
    Nature 452:234-238(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone."
    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. 1:79-79(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNPY3 AND HSP90B1.
  11. 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)
  12. "CMRF-35-like molecule 3 preferentially promotes TLR9-triggered proinflammatory cytokine production in macrophages by enhancing TNF receptor-associated factor 6 ubiquitination."
    Wu Y., Zhu X., Li N., Chen T., Yang M., Yao M., Liu X., Jin B., Wang X., Cao X.
    J. Immunol. 187:4881-4889(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD300LH.

Entry informationi

Entry nameiTLR9_MOUSE
AccessioniPrimary (citable) accession number: Q9EQU3
Secondary accession number(s): F8VPN5
, Q4L0K3, Q4L0K4, Q99MF2, Q99MQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: December 14, 2011
Last modified: May 27, 2015
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.