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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 (PubMed:18931679, PubMed:21402738, PubMed:14993594, PubMed:17474149, PubMed:25686612, PubMed:18820679). Plays a role in defense against systemic mouse cytomegalovirus infection (PubMed:14993594). Controls lymphocyte response to Helicobacter infection (PubMed:17474149).6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei132CpG-DNABy similarity1
Binding sitei208CpG-DNABy similarity1

GO - Molecular functioni

GO - Biological processi

  • activation of innate immune response Source: UniProtKB
  • axonogenesis Source: GO_Central
  • cellular response to chloroquine Source: MGI
  • cellular response to lipopolysaccharide Source: Ensembl
  • cellular response to metal ion Source: Ensembl
  • cytokine production Source: UniProtKB
  • defense response to Gram-negative bacterium Source: MGI
  • defense response to virus Source: MGI
  • I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • I-kappaB phosphorylation Source: MGI
  • immune response Source: MGI
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: BHF-UCL
  • maintenance of gastrointestinal epithelium Source: BHF-UCL
  • male gonad development Source: Ensembl
  • microglial cell activation Source: Ensembl
  • MyD88-dependent toll-like receptor signaling pathway Source: UniProtKB
  • negative regulation of calcium-transporting ATPase activity Source: MGI
  • negative regulation of interleukin-6 production Source: BHF-UCL
  • negative regulation of interleukin-8 production Source: MGI
  • negative regulation of NF-kappaB transcription factor activity Source: MGI
  • negative regulation of toll-like receptor signaling pathway Source: MGI
  • positive regulation of autophagy Source: Ensembl
  • positive regulation of chemokine production Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of granulocyte macrophage colony-stimulating factor production Source: MGI
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of inflammatory response Source: InterPro
  • positive regulation of interferon-alpha biosynthetic process Source: UniProtKB
  • positive regulation of interferon-beta biosynthetic process Source: UniProtKB
  • positive regulation of interferon-beta production Source: BHF-UCL
  • positive regulation of interferon-gamma biosynthetic process Source: UniProtKB
  • positive regulation of interleukin-10 production Source: BHF-UCL
  • positive regulation of interleukin-12 production Source: BHF-UCL
  • positive regulation of interleukin-18 production Source: BHF-UCL
  • positive regulation of interleukin-6 production Source: BHF-UCL
  • positive regulation of interleukin-8 production Source: MGI
  • positive regulation of JUN kinase activity Source: MGI
  • positive regulation of NF-kappaB import into nucleus Source: MGI
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  • positive regulation of toll-like receptor 9 signaling pathway Source: UniProtKB
  • positive regulation of toll-like receptor signaling pathway Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of tumor necrosis factor production Source: BHF-UCL
  • regulation of B cell activation Source: MGI
  • regulation of cytokine secretion Source: InterPro
  • regulation of dendritic cell cytokine production Source: MGI
  • regulation of inflammatory response Source: BHF-UCL
  • regulation of protein phosphorylation Source: MGI
  • response to molecule of bacterial origin Source: BHF-UCL
  • response to virus Source: MGI
  • toll-like receptor 9 signaling pathway Source: InterPro
  • tumor necrosis factor production Source: UniProtKB

Keywordsi

Molecular functionReceptor
Biological processImmunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiR-MMU-109704. PI3K Cascade.
R-MMU-1679131. Trafficking and processing of endosomal TLR.
R-MMU-168138. Toll Like Receptor 9 (TLR9) Cascade.
R-MMU-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-MMU-975138. TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
R-MMU-975155. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1932389. Tlr9.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 818ExtracellularSequence analysisAdd BLAST793
Transmembranei819 – 839HelicalSequence analysisAdd BLAST21
Topological domaini840 – 1032CytoplasmicSequence analysisAdd BLAST193

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)DescriptionActionsGraphical viewLength
Mutagenesisi47W → A: Significantly decreased NF-kappa-B activation. 1 Publication1
Mutagenesisi74R → A: Significantly decreased NF-kappa-B activation. 1 Publication1
Mutagenesisi104S → A: Significantly decreased NF-kappa-B activation. 1 Publication1
Mutagenesisi108F → A: Significantly decreased NF-kappa-B activation. 1 Publication1
Mutagenesisi132Y → A: Significantly decreased NF-kappa-B activation. 1 Publication1
Mutagenesisi152H → A: Significantly decreased NF-kappa-B activation. 1 Publication1
Mutagenesisi179Y → A: Significantly decreased NF-kappa-B activation. 1 Publication1
Mutagenesisi229Y → A: Significantly decreased NF-kappa-B activation. 1 Publication1
Mutagenesisi499L → P: Highly susceptible to mouse cytomegalovirus infection. Shows low level of cytokine induction and natural killer activation on viral infection. 1 Publication1
Mutagenesisi642H → A: Loss of NF-kappa-B activation. 1 Publication1
Mutagenesisi668F → A: Significantly decreased NF-kappa-B activation. 1 Publication1
Mutagenesisi695N → A: Significantly decreased NF-kappa-B activation. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL6128.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000003473826 – 1032Toll-like receptor 9Add BLAST1007

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi35 ↔ 45Combined sources1 Publication
Glycosylationi64N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi98 ↔ 110Combined sources1 Publication
Glycosylationi129N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi147N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi178 ↔ 184Combined sources1 Publication
Glycosylationi200N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi210N-linked (GlcNAc...) asparagineSequence analysisCombined sources1 Publication1
Glycosylationi242N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi255 ↔ 268Combined sources1 Publication
Disulfide bondi258 ↔ 265Combined sources1 Publication
Glycosylationi300N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi309N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi332N-linked (GlcNAc...) asparagineSequence analysisCombined sources1 Publication1
Glycosylationi340N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi471 ↔ 501Combined sources1 Publication
Glycosylationi495N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi514N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi568N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi670N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi695N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi700N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi732N-linked (GlcNAc...) asparagineSequence analysisCombined sources1 Publication1
Glycosylationi752N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi765 ↔ 791Combined sources1 Publication
Disulfide bondi767 ↔ 810Combined sources1 Publication

Post-translational modificationi

Activated by proteolytic cleavage of the flexible loop between repeats LRR14 and LRR15 within the ectodomain (PubMed:18931679, PubMed:18820679). Cleavage requires UNC93B1 (PubMed:18820679). 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 (PubMed:21402738).3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9EQU3.
PaxDbiQ9EQU3.
PeptideAtlasiQ9EQU3.
PRIDEiQ9EQU3.

PTM databases

iPTMnetiQ9EQU3.
PhosphoSitePlusiQ9EQU3.

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

BgeeiENSMUSG00000045322.
CleanExiMM_TLR9.
GenevisibleiQ9EQU3. MM.

Interactioni

Subunit structurei

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 (PubMed:18820679). Interacts with BTK (By similarity). Interacts (via transmembrane domain) with UNC93B1 (PubMed:17452530, PubMed:18931679). Interacts with CD300LH; the interaction may promote full activation of TLR9-triggered innate responses (PubMed:21940676). Interacts with CNPY3 and HSP90B1; this interaction is required for proper folding in the endoplasmic reticulum (PubMed:18780723, PubMed:20865800). Interacts with SMPDL3B (PubMed:26095358).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Atp2a2P115074EBI-9979528,EBI-916319From Rattus norvegicus.

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9EQU3. 28 interactors.
STRINGi10090.ENSMUSP00000082207.

Structurei

Secondary structure

11032
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni31 – 34Combined sources4
Beta strandi35 – 38Combined sources4
Turni39 – 41Combined sources3
Beta strandi42 – 44Combined sources3
Beta strandi67 – 69Combined sources3
Turni80 – 83Combined sources4
Helixi84 – 86Combined sources3
Beta strandi90 – 93Combined sources4
Beta strandi100 – 102Combined sources3
Turni116 – 121Combined sources6
Beta strandi127 – 129Combined sources3
Beta strandi147 – 149Combined sources3
Helixi160 – 163Combined sources4
Beta strandi171 – 173Combined sources3
Beta strandi177 – 179Combined sources3
Turni192 – 197Combined sources6
Beta strandi203 – 205Combined sources3
Beta strandi223 – 226Combined sources4
Helixi237 – 239Combined sources3
Beta strandi247 – 250Combined sources4
Beta strandi254 – 256Combined sources3
Beta strandi269 – 272Combined sources4
Turni277 – 282Combined sources6
Beta strandi288 – 290Combined sources3
Helixi301 – 304Combined sources4
Beta strandi312 – 314Combined sources3
Beta strandi317 – 319Combined sources3
Helixi321 – 324Combined sources4
Helixi329 – 332Combined sources4
Beta strandi338 – 340Combined sources3
Beta strandi347 – 349Combined sources3
Helixi358 – 362Combined sources5
Beta strandi368 – 370Combined sources3
Beta strandi377 – 379Combined sources3
Turni381 – 384Combined sources4
Helixi385 – 387Combined sources3
Beta strandi395 – 397Combined sources3
Helixi408 – 412Combined sources5
Beta strandi413 – 416Combined sources4
Beta strandi419 – 421Combined sources3
Beta strandi473 – 475Combined sources3
Beta strandi477 – 479Combined sources3
Helixi490 – 493Combined sources4
Beta strandi501 – 503Combined sources3
Turni517 – 520Combined sources4
Beta strandi526 – 528Combined sources3
Turni539 – 544Combined sources6
Beta strandi550 – 552Combined sources3
Helixi570 – 574Combined sources5
Beta strandi580 – 582Combined sources3
Beta strandi590 – 592Combined sources3
Beta strandi597 – 600Combined sources4
Beta strandi603 – 605Combined sources3
Helixi611 – 615Combined sources5
Turni620 – 626Combined sources7
Beta strandi633 – 635Combined sources3
Helixi646 – 650Combined sources5
Beta strandi658 – 660Combined sources3
Helixi671 – 676Combined sources6
Beta strandi682 – 684Combined sources3
Beta strandi706 – 708Combined sources3
Turni719 – 724Combined sources6
Beta strandi730 – 732Combined sources3
Helixi743 – 745Combined sources3
Helixi747 – 751Combined sources5
Beta strandi754 – 757Combined sources4
Helixi771 – 777Combined sources7
Helixi779 – 781Combined sources3
Turni783 – 788Combined sources6
Beta strandi789 – 794Combined sources6
Turni795 – 797Combined sources3
Helixi807 – 809Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati62 – 85LRR 1Add BLAST24
Repeati87 – 110LRR 2Add BLAST24
Repeati122 – 147LRR 3Add BLAST26
Repeati150 – 166LRR 4Add BLAST17
Repeati167 – 190LRR 5Add BLAST24
Repeati198 – 221LRR 6Add BLAST24
Repeati223 – 242LRR 7Add BLAST20
Repeati243 – 268LRR 8Add BLAST26
Repeati283 – 306LRR 9Add BLAST24
Repeati308 – 332LRR 10Add BLAST25
Repeati333 – 356LRR 11Add BLAST24
Repeati363 – 386LRR 12Add BLAST24
Repeati390 – 413LRR 13Add BLAST24
Repeati415 – 440LRR 14Add BLAST26
Repeati471 – 495LRR 15Add BLAST25
Repeati497 – 520LRR 16Add BLAST24
Repeati521 – 544LRR 17Add BLAST24
Repeati546 – 573LRR 18Add BLAST28
Repeati575 – 599LRR 19Add BLAST25
Repeati601 – 623LRR 20Add BLAST23
Repeati628 – 651LRR 21Add BLAST24
Repeati653 – 676LRR 22Add BLAST24
Repeati677 – 700LRR 23Add BLAST24
Repeati702 – 724LRR 24Add BLAST23
Repeati725 – 748LRR 25Add BLAST24
Repeati750 – 773LRR 26Add BLAST24
Domaini868 – 1016TIRPROSITE-ProRule annotationAdd BLAST149

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni47 – 51Interaction with CpG-DNABy similarity5
Regioni72 – 77Interaction with CpG-DNABy similarity6
Regioni95 – 109Interaction with CpG-DNABy similarityAdd BLAST15
Regioni179 – 181Interaction with CpG-DNABy similarity3

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000230468.
HOVERGENiHBG018601.
InParanoidiQ9EQU3.
KOiK10161.
OMAiCRRCDHA.
OrthoDBiEOG091G0BWK.
TreeFamiTF325595.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 7 hits.
InterProiView protein in InterPro
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027181. TLR9.
PANTHERiPTHR24373:SF187. PTHR24373:SF187. 1 hit.
PfamiView protein in Pfam
PF13855. LRR_8. 3 hits.
PF01582. TIR. 1 hit.
SMARTiView protein in SMART
SM00369. LRR_TYP. 15 hits.
SM00255. TIR. 1 hit.
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF52200. SSF52200. 1 hit.
PROSITEiView protein in PROSITE
PS51450. LRR. 16 hits.
PS50104. TIR. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti325T → N in BAB19260 (PubMed:11130078).Curated1
Sequence conflicti325T → N in AAK29625 (PubMed:11470918).Curated1
Sequence conflicti325T → N in AAK28488 (PubMed:11867692).Curated1
Sequence conflicti325T → N in AAU04980 (PubMed:17474149).Curated1
Sequence conflicti378L → S in BAB19260 (PubMed:11130078).Curated1
Sequence conflicti378L → S in AAK29625 (PubMed:11470918).Curated1
Sequence conflicti378L → S in AAK28488 (PubMed:11867692).Curated1
Sequence conflicti378L → S in AAU04980 (PubMed:17474149).Curated1
Sequence conflicti554S → G in AAK28488 (PubMed:11867692).Curated1
Sequence conflicti562M → I in AAK28488 (PubMed:11867692).Curated1
Sequence conflicti573T → A in AAK29625 (PubMed:11470918).Curated1
Sequence conflicti573T → A in AAK28488 (PubMed:11867692).Curated1
Sequence conflicti573T → A in AAU04980 (PubMed:17474149).Curated1
Sequence conflicti579Q → H in AAK29625 (PubMed:11470918).Curated1
Sequence conflicti579Q → H in AAK28488 (PubMed:11867692).Curated1
Sequence conflicti579Q → H in AAU04980 (PubMed:17474149).Curated1
Sequence conflicti867T → A in AAK29625 (PubMed:11470918).Curated1
Sequence conflicti867T → A in AAK28488 (PubMed:11867692).Curated1
Sequence conflicti867T → A in AAU04980 (PubMed:17474149).Curated1
Sequence conflicti897E → G in AAK28488 (PubMed:11867692).Curated1

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.

Similar proteinsi

Entry informationi

Entry nameiTLR9_MOUSE
AccessioniPrimary (citable) accession number: Q9EQU3
Secondary accession number(s): F8VPN5
, Q4L0K3, Q4L0K4, Q99MF2, Q99MQ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: December 14, 2011
Last modified: July 5, 2017
This is version 152 of the entry and version 3 of the sequence. See 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