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Protein

Toll-like receptor 4

Gene

Tlr4

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

Functioni

Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:9851930, PubMed:9989976, PubMed:20133493). Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:24380872). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate. In complex with TLR6, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. Binds electronegative LDL (LDL-) and mediates the cytokine release induced by LDL- (By similarity).By similarity8 Publications

GO - Molecular functioni

GO - Biological processi

  • activation of innate immune response Source: MGI
  • activation of MAPK activity Source: BHF-UCL
  • activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  • astrocyte development Source: MGI
  • B cell proliferation involved in immune response Source: MGI
  • cellular response to lipopolysaccharide Source: BHF-UCL
  • cellular response to lipoteichoic acid Source: MGI
  • cellular response to mechanical stimulus Source: Ensembl
  • defense response to Gram-negative bacterium Source: MGI
  • detection of lipopolysaccharide Source: BHF-UCL
  • I-kappaB phosphorylation Source: MGI
  • innate immune response Source: BHF-UCL
  • interferon-gamma production Source: MGI
  • interleukin-1 beta secretion Source: UniProtKB
  • intestinal epithelial structure maintenance Source: BHF-UCL
  • lipopolysaccharide-mediated signaling pathway Source: MGI
  • macrophage activation Source: UniProtKB
  • mast cell activation Source: UniProtKB
  • MyD88-dependent toll-like receptor signaling pathway Source: InterPro
  • negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • negative regulation of interferon-gamma production Source: BHF-UCL
  • negative regulation of interleukin-17 production Source: BHF-UCL
  • negative regulation of interleukin-23 production Source: BHF-UCL
  • negative regulation of interleukin-6 production Source: BHF-UCL
  • negative regulation of tumor necrosis factor production Source: BHF-UCL
  • nitric oxide production involved in inflammatory response Source: MGI
  • positive regulation of B cell proliferation Source: MGI
  • positive regulation of chemokine production Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of interferon-alpha production Source: BHF-UCL
  • positive regulation of interferon-beta biosynthetic process Source: MGI
  • positive regulation of interferon-beta production Source: BHF-UCL
  • positive regulation of interferon-gamma production Source: BHF-UCL
  • positive regulation of interleukin-10 production Source: BHF-UCL
  • positive regulation of interleukin-12 biosynthetic process Source: MGI
  • positive regulation of interleukin-12 production Source: BHF-UCL
  • positive regulation of interleukin-13 biosynthetic process Source: UniProtKB
  • positive regulation of interleukin-1 biosynthetic process Source: UniProtKB
  • positive regulation of interleukin-1 production Source: BHF-UCL
  • positive regulation of interleukin-6 biosynthetic process Source: UniProtKB
  • positive regulation of interleukin-6 production Source: BHF-UCL
  • positive regulation of interleukin-8 biosynthetic process Source: MGI
  • positive regulation of interleukin-8 production Source: MGI
  • positive regulation of JNK cascade Source: MGI
  • positive regulation of lymphocyte proliferation Source: MGI
  • positive regulation of macrophage cytokine production Source: MGI
  • positive regulation of MHC class II biosynthetic process Source: MGI
  • positive regulation of NF-kappaB import into nucleus Source: MGI
  • positive regulation of NF-kappaB transcription factor activity Source: MGI
  • positive regulation of nitric oxide biosynthetic process Source: MGI
  • positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  • positive regulation of NLRP3 inflammasome complex assembly Source: UniProtKB
  • positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway Source: MGI
  • positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway Source: MGI
  • positive regulation of platelet activation Source: BHF-UCL
  • positive regulation of stress-activated MAPK cascade Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of tumor necrosis factor biosynthetic process Source: MGI
  • positive regulation of tumor necrosis factor production Source: BHF-UCL
  • regulation of cytokine secretion Source: InterPro
  • regulation of dendritic cell cytokine production Source: MGI
  • regulation of inflammatory response Source: BHF-UCL
  • response to bacterium Source: MGI
  • response to lipopolysaccharide Source: MGI
  • toll-like receptor 4 signaling pathway Source: InterPro
  • toll-like receptor signaling pathway Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiR-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-MMU-166166. MyD88-independent TLR3/TLR4 cascade.
R-MMU-5686938. Regulation of TLR by endogenous ligand.

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-like receptor 4
Alternative name(s):
CD_antigen: CD284
Gene namesi
Name:Tlr4
Synonyms:Lps
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:96824. Tlr4.

Subcellular locationi

  • Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

  • Note: Upon complex formation with CD36 and TLR6, internalized through dynamin-dependent endocytosis.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 638ExtracellularSequence analysisAdd BLAST613
Transmembranei639 – 659HelicalSequence analysisAdd BLAST21
Topological domaini660 – 835CytoplasmicSequence analysisAdd BLAST176

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

The protein is encoded by the Lps locus, an important susceptibility locus, influencing the propensity to develop a disseminated Gram-negative infection.

Disruption phenotypei

Animals with a double knockout of APOE and TLR4, fed a Western diet for 12 weeks, have less aortic plaque formation than single APOE knockout mice. They also show lower serum concentrations of IL1A, ILB and IL18.1 Publication

Keywords - Diseasei

Disease mutation

Chemistry databases

ChEMBLiCHEMBL1795167.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000003472326 – 835Toll-like receptor 4Add BLAST810

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 391 Publication
Glycosylationi34N-linked (GlcNAc...)1 Publication1
Glycosylationi75N-linked (GlcNAc...)1 Publication1
Glycosylationi172N-linked (GlcNAc...)1 Publication1
Glycosylationi204N-linked (GlcNAc...)1 Publication1
Glycosylationi237N-linked (GlcNAc...)1 Publication1
Disulfide bondi280 ↔ 3041 Publication
Glycosylationi307N-linked (GlcNAc...)1 Publication1
Disulfide bondi388 ↔ 3891 Publication
Glycosylationi492N-linked (GlcNAc...)1 Publication1
Glycosylationi495N-linked (GlcNAc...)1
Glycosylationi524N-linked (GlcNAc...)1 Publication1
Glycosylationi572N-linked (GlcNAc...)1 Publication1
Glycosylationi575N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi580 ↔ 6061 Publication
Disulfide bondi582 ↔ 6251 Publication
Glycosylationi613N-linked (GlcNAc...)Sequence analysis1
Glycosylationi621N-linked (GlcNAc...)Sequence analysis1
Glycosylationi622N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9QUK6.
PaxDbiQ9QUK6.
PRIDEiQ9QUK6.

PTM databases

PhosphoSitePlusiQ9QUK6.

Expressioni

Tissue specificityi

Highly expressed in heart, spleen, lung and muscle. Lower levels are found in liver and kidney. Expressed in macrophages.1 Publication

Gene expression databases

BgeeiENSMUSG00000039005.
CleanExiMM_TLR4.
ExpressionAtlasiQ9QUK6. baseline and differential.
GenevisibleiQ9QUK6. MM.

Interactioni

Subunit structurei

Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 (PubMed:24380872). Binding to bacterial LPS leads to homodimerization (PubMed:20133493, PubMed:24380872, PubMed:22532668). Interacts with LY96 via the extracellular domain (PubMed:17803912, PubMed:22532668). Interacts with MYD88 (via the TIR domain). Interacts with TICAM2 and TIRAP (PubMed:24380872). Interacts with NOX4 (By similarity). Interacts with CNPY3 and HSP90B1; this interaction is required for proper folding in the endoplasmic reticulum (PubMed:18780723, PubMed:20865800). Interacts with MLK4; this interaction leads to negative regulation of TLR4 signaling (By similarity). Interacts with CD36, following CD36 stimulation by oxLDL or amyloid-beta 42, and forms a heterodimer with TLR6. The trimeric complex is internalized and triggers inflammatory response. LYN kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation (By similarity). Interacts with TICAM1 in response to LPS in a WDFY1-dependent manner (PubMed:25736436). Interacts with WDFY1 in response to LPS (PubMed:25736436). Interacts with SMPDL3B (PubMed:26095358). Interacts with CEACAM1; upon lipopolysaccharide stimulation, forms a complex including TLR4 and the phosphorylated form of SYK and CEACAM1, which in turn, recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome (PubMed:22496641).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ly96Q9JHF93EBI-1534575,EBI-1534566

Protein-protein interaction databases

BioGridi204224. 24 interactors.
DIPiDIP-38573N.
IntActiQ9QUK6. 8 interactors.
STRINGi10090.ENSMUSP00000045770.

Chemistry databases

BindingDBiQ9QUK6.

Structurei

Secondary structure

1835
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 32Combined sources4
Turni33 – 35Combined sources3
Beta strandi36 – 38Combined sources3
Beta strandi40 – 42Combined sources3
Beta strandi49 – 51Combined sources3
Beta strandi57 – 59Combined sources3
Turni70 – 75Combined sources6
Beta strandi81 – 83Combined sources3
Turni94 – 99Combined sources6
Beta strandi105 – 107Combined sources3
Turni118 – 121Combined sources4
Beta strandi129 – 131Combined sources3
Beta strandi140 – 143Combined sources4
Beta strandi153 – 155Combined sources3
Helixi168 – 171Combined sources4
Beta strandi178 – 180Combined sources3
Turni191 – 194Combined sources4
Helixi195 – 199Combined sources5
Beta strandi206 – 208Combined sources3
Turni219 – 224Combined sources6
Beta strandi226 – 234Combined sources9
Helixi239 – 247Combined sources9
Turni248 – 251Combined sources4
Beta strandi253 – 260Combined sources8
Helixi273 – 276Combined sources4
Helixi279 – 281Combined sources3
Beta strandi282 – 289Combined sources8
Helixi297 – 300Combined sources4
Helixi303 – 305Combined sources3
Beta strandi309 – 315Combined sources7
Beta strandi331 – 337Combined sources7
Beta strandi353 – 358Combined sources6
Beta strandi375 – 377Combined sources3
Beta strandi380 – 382Combined sources3
Beta strandi383 – 388Combined sources6
Helixi391 – 394Combined sources4
Beta strandi401 – 403Combined sources3
Beta strandi408 – 412Combined sources5
Beta strandi424 – 426Combined sources3
Beta strandi430 – 434Combined sources5
Turni435 – 443Combined sources9
Beta strandi449 – 451Combined sources3
Turni462 – 467Combined sources6
Beta strandi473 – 475Combined sources3
Helixi482 – 484Combined sources3
Turni489 – 492Combined sources4
Beta strandi498 – 500Combined sources3
Turni511 – 516Combined sources6
Beta strandi522 – 524Combined sources3
Beta strandi532 – 534Combined sources3
Helixi535 – 537Combined sources3
Turni538 – 540Combined sources3
Beta strandi546 – 548Combined sources3
Beta strandi557 – 559Combined sources3
Helixi561 – 563Combined sources3
Beta strandi570 – 572Combined sources3
Helixi582 – 584Combined sources3
Helixi585 – 588Combined sources4
Turni589 – 593Combined sources5
Beta strandi594 – 600Combined sources7
Helixi601 – 603Combined sources3
Beta strandi608 – 610Combined sources3
Helixi616 – 618Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z64X-ray2.84A27-625[»]
3VQ1X-ray2.70A/B22-627[»]
3VQ2X-ray2.48A/B22-627[»]
5IJBX-ray2.91A/B26-544[»]
5IJCX-ray2.57A/B26-544[»]
5IJDX-ray2.70A/B26-544[»]
ProteinModelPortaliQ9QUK6.
SMRiQ9QUK6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QUK6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati54 – 75LRR 1Add BLAST22
Repeati78 – 99LRR 2Add BLAST22
Repeati102 – 123LRR 3Add BLAST22
Repeati126 – 147LRR 4Add BLAST22
Repeati150 – 171LRR 5Add BLAST22
Repeati175 – 198LRR 6Add BLAST24
Repeati204 – 224LRR 7Add BLAST21
Repeati226 – 247LRR 8Add BLAST22
Repeati248 – 269LRR 9Add BLAST22
Repeati329 – 349LRR 10Add BLAST21
Repeati350 – 370LRR 11Add BLAST21
Repeati372 – 392LRR 12Add BLAST21
Repeati398 – 420LRR 13Add BLAST23
Repeati421 – 442LRR 14Add BLAST22
Repeati446 – 467LRR 15Add BLAST22
Repeati470 – 490LRR 16Add BLAST21
Repeati495 – 516LRR 17Add BLAST22
Repeati519 – 540LRR 18Add BLAST22
Repeati543 – 564LRR 19Add BLAST22
Domaini576 – 627LRRCTAdd BLAST52
Domaini670 – 816TIRPROSITE-ProRule annotationAdd BLAST147

Domaini

The TIR domain mediates interaction with NOX4.By similarity

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated
Contains 19 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000037951.
HOVERGENiHBG018823.
InParanoidiQ9QUK6.
KOiK10160.
OMAiSVACICE.
OrthoDBiEOG091G01RC.
PhylomeDBiQ9QUK6.
TreeFamiTF351113.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 4 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027168. TLR4.
[Graphical view]
PANTHERiPTHR24365:SF230. PTHR24365:SF230. 2 hits.
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 2 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 8 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9QUK6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMPPWLLART LIMALFFSCL TPGSLNPCIE VVPNITYQCM DQKLSKVPDD
60 70 80 90 100
IPSSTKNIDL SFNPLKILKS YSFSNFSELQ WLDLSRCEIE TIEDKAWHGL
110 120 130 140 150
HHLSNLILTG NPIQSFSPGS FSGLTSLENL VAVETKLASL ESFPIGQLIT
160 170 180 190 200
LKKLNVAHNF IHSCKLPAYF SNLTNLVHVD LSYNYIQTIT VNDLQFLREN
210 220 230 240 250
PQVNLSLDMS LNPIDFIQDQ AFQGIKLHEL TLRGNFNSSN IMKTCLQNLA
260 270 280 290 300
GLHVHRLILG EFKDERNLEI FEPSIMEGLC DVTIDEFRLT YTNDFSDDIV
310 320 330 340 350
KFHCLANVSA MSLAGVSIKY LEDVPKHFKW QSLSIIRCQL KQFPTLDLPF
360 370 380 390 400
LKSLTLTMNK GSISFKKVAL PSLSYLDLSR NALSFSGCCS YSDLGTNSLR
410 420 430 440 450
HLDLSFNGAI IMSANFMGLE ELQHLDFQHS TLKRVTEFSA FLSLEKLLYL
460 470 480 490 500
DISYTNTKID FDGIFLGLTS LNTLKMAGNS FKDNTLSNVF ANTTNLTFLD
510 520 530 540 550
LSKCQLEQIS WGVFDTLHRL QLLNMSHNNL LFLDSSHYNQ LYSLSTLDCS
560 570 580 590 600
FNRIETSKGI LQHFPKSLAF FNLTNNSVAC ICEHQKFLQW VKEQKQFLVN
610 620 630 640 650
VEQMTCATPV EMNTSLVLDF NNSTCYMYKT IISVSVVSVI VVSTVAFLIY
660 670 680 690 700
HFYFHLILIA GCKKYSRGES IYDAFVIYSS QNEDWVRNEL VKNLEEGVPR
710 720 730 740 750
FHLCLHYRDF IPGVAIAANI IQEGFHKSRK VIVVVSRHFI QSRWCIFEYE
760 770 780 790 800
IAQTWQFLSS RSGIIFIVLE KVEKSLLRQQ VELYRLLSRN TYLEWEDNPL
810 820 830
GRHIFWRRLK NALLDGKASN PEQTAEEEQE TATWT
Length:835
Mass (Da):95,519
Last modified:May 1, 2000 - v1
Checksum:i9C83B59F9A220C17
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti87 – 154CEIET…TLKKL → EMNTESKSSEAHALALSHIL SPCQPSRRKLRVKLGSLSYQ RAEEGVRSSEIGYSCLHVDT RHDINAVD (PubMed:16141072).CuratedAdd BLAST68

Polymorphismi

Interstrain analyzes reveals that TLR4 is a polymorphic protein and that the extracellular domain is far more variable than the cytoplasmic domain, which is variable at the C-terminal.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti94D → N in strain: KK/HLJ. 1 Publication1
Natural varianti209M → I in strain: A/J, BALB/cJ, P/J, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK. 1 Publication1
Natural varianti219D → G in strain: SEA/GNJ. 1 Publication1
Natural varianti254V → I in strain: A/J, BALB/cJ and SEA/GNJ. 1 Publication1
Natural varianti423Q → L in strain: SEA/GNJ. 1 Publication1
Natural varianti477A → S in strain: P/J. 1 Publication1
Natural varianti516T → A in strain: LP/J. 1 Publication1
Natural varianti593E → D in strain: A/J, BALB/cJ, P/J, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK. 1 Publication1
Natural varianti600N → I in strain: KK/HLJ. 1 Publication1
Natural varianti607A → V in strain: P/J. 1 Publication1
Natural varianti637V → I in strain: P/J. 1 Publication1
Natural varianti712P → H in Lps-tolerant mice. 2 Publications1
Natural varianti761R → H in strain: A/J, BALB/cJ, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK. 1 Publication1
Natural varianti811N → K in strain: P/J. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095353 mRNA. Translation: AAC99411.1.
AF110133 mRNA. Translation: AAD29272.1.
AF185285 mRNA. Translation: AAF04278.1.
AF177767 Genomic DNA. Translation: AAF05317.1.
AK014533 mRNA. No translation available.
CCDSiCCDS18271.1.
RefSeqiNP_067272.1. NM_021297.3.
UniGeneiMm.38049.

Genome annotation databases

EnsembliENSMUST00000048096; ENSMUSP00000045770; ENSMUSG00000039005.
GeneIDi21898.
KEGGimmu:21898.
UCSCiuc008thv.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095353 mRNA. Translation: AAC99411.1.
AF110133 mRNA. Translation: AAD29272.1.
AF185285 mRNA. Translation: AAF04278.1.
AF177767 Genomic DNA. Translation: AAF05317.1.
AK014533 mRNA. No translation available.
CCDSiCCDS18271.1.
RefSeqiNP_067272.1. NM_021297.3.
UniGeneiMm.38049.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z64X-ray2.84A27-625[»]
3VQ1X-ray2.70A/B22-627[»]
3VQ2X-ray2.48A/B22-627[»]
5IJBX-ray2.91A/B26-544[»]
5IJCX-ray2.57A/B26-544[»]
5IJDX-ray2.70A/B26-544[»]
ProteinModelPortaliQ9QUK6.
SMRiQ9QUK6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204224. 24 interactors.
DIPiDIP-38573N.
IntActiQ9QUK6. 8 interactors.
STRINGi10090.ENSMUSP00000045770.

Chemistry databases

BindingDBiQ9QUK6.
ChEMBLiCHEMBL1795167.

PTM databases

PhosphoSitePlusiQ9QUK6.

Proteomic databases

MaxQBiQ9QUK6.
PaxDbiQ9QUK6.
PRIDEiQ9QUK6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048096; ENSMUSP00000045770; ENSMUSG00000039005.
GeneIDi21898.
KEGGimmu:21898.
UCSCiuc008thv.1. mouse.

Organism-specific databases

CTDi7099.
MGIiMGI:96824. Tlr4.

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000037951.
HOVERGENiHBG018823.
InParanoidiQ9QUK6.
KOiK10160.
OMAiSVACICE.
OrthoDBiEOG091G01RC.
PhylomeDBiQ9QUK6.
TreeFamiTF351113.

Enzyme and pathway databases

ReactomeiR-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-MMU-166166. MyD88-independent TLR3/TLR4 cascade.
R-MMU-5686938. Regulation of TLR by endogenous ligand.

Miscellaneous databases

EvolutionaryTraceiQ9QUK6.
PROiQ9QUK6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000039005.
CleanExiMM_TLR4.
ExpressionAtlasiQ9QUK6. baseline and differential.
GenevisibleiQ9QUK6. MM.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 4 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027168. TLR4.
[Graphical view]
PANTHERiPTHR24365:SF230. PTHR24365:SF230. 2 hits.
PfamiPF00560. LRR_1. 1 hit.
PF13855. LRR_8. 2 hits.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 8 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTLR4_MOUSE
AccessioniPrimary (citable) accession number: Q9QUK6
Secondary accession number(s): Q9D691, Q9QZF5, Q9Z203
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 153 of the entry and version 1 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

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 one 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.