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Q9QUK6

- TLR4_MOUSE

UniProt

Q9QUK6 - TLR4_MOUSE

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Protein

Toll-like receptor 4

Gene
Tlr4, Lps
Organism
Mus musculus (Mouse)
Status
Reviewed - 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). Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response By similarity.1 Publication

GO - Molecular functioni

  1. lipopolysaccharide receptor activity Source: UniProtKB
  2. protein binding Source: IntAct
  3. transmembrane signaling receptor activity Source: InterPro

GO - Biological processi

  1. activation of innate immune response Source: MGI
  2. activation of MAPK activity Source: BHF-UCL
  3. activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  4. B cell proliferation involved in immune response Source: MGI
  5. cellular response to lipopolysaccharide Source: BHF-UCL
  6. cellular response to lipoteichoic acid Source: MGI
  7. cellular response to mechanical stimulus Source: Ensembl
  8. defense response to Gram-negative bacterium Source: MGI
  9. detection of lipopolysaccharide Source: BHF-UCL
  10. I-kappaB phosphorylation Source: Ensembl
  11. innate immune response Source: BHF-UCL
  12. interferon-gamma production Source: MGI
  13. intestinal epithelial structure maintenance Source: BHF-UCL
  14. lipopolysaccharide-mediated signaling pathway Source: MGI
  15. macrophage activation Source: UniProtKB
  16. mast cell activation Source: UniProtKB
  17. MyD88-dependent toll-like receptor signaling pathway Source: InterPro
  18. negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  19. negative regulation of interferon-gamma production Source: BHF-UCL
  20. negative regulation of interleukin-17 production Source: BHF-UCL
  21. negative regulation of interleukin-23 production Source: BHF-UCL
  22. negative regulation of interleukin-6 production Source: BHF-UCL
  23. negative regulation of tumor necrosis factor production Source: BHF-UCL
  24. nitric oxide production involved in inflammatory response Source: MGI
  25. positive regulation of B cell proliferation Source: MGI
  26. positive regulation of chemokine production Source: BHF-UCL
  27. positive regulation of ERK1 and ERK2 cascade Source: MGI
  28. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  29. positive regulation of interferon-alpha production Source: BHF-UCL
  30. positive regulation of interferon-beta biosynthetic process Source: MGI
  31. positive regulation of interferon-beta production Source: BHF-UCL
  32. positive regulation of interferon-gamma production Source: BHF-UCL
  33. positive regulation of interleukin-10 production Source: BHF-UCL
  34. positive regulation of interleukin-12 biosynthetic process Source: Ensembl
  35. positive regulation of interleukin-12 production Source: BHF-UCL
  36. positive regulation of interleukin-13 biosynthetic process Source: UniProtKB
  37. positive regulation of interleukin-1 biosynthetic process Source: UniProtKB
  38. positive regulation of interleukin-1 production Source: BHF-UCL
  39. positive regulation of interleukin-6 biosynthetic process Source: UniProtKB
  40. positive regulation of interleukin-6 production Source: BHF-UCL
  41. positive regulation of interleukin-8 biosynthetic process Source: Ensembl
  42. positive regulation of interleukin-8 production Source: Ensembl
  43. positive regulation of JNK cascade Source: MGI
  44. positive regulation of lymphocyte proliferation Source: MGI
  45. positive regulation of macrophage cytokine production Source: MGI
  46. positive regulation of MHC class II biosynthetic process Source: MGI
  47. positive regulation of NF-kappaB import into nucleus Source: Ensembl
  48. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  49. positive regulation of nitric oxide biosynthetic process Source: MGI
  50. positive regulation of nitric-oxide synthase biosynthetic process Source: BHF-UCL
  51. positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway Source: MGI
  52. positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway Source: MGI
  53. positive regulation of platelet activation Source: BHF-UCL
  54. positive regulation of stress-activated MAPK cascade Source: MGI
  55. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  56. positive regulation of tumor necrosis factor biosynthetic process Source: Ensembl
  57. positive regulation of tumor necrosis factor production Source: BHF-UCL
  58. regulation of cytokine secretion Source: InterPro
  59. regulation of inflammatory response Source: BHF-UCL
  60. response to bacterium Source: MGI
  61. response to lipopolysaccharide Source: MGI
  62. toll-like receptor 4 signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_196636. TRIF-mediated programmed cell death.
REACT_198539. TRAF6 mediated induction of TAK1 complex.
REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_226192. IKK complex recruitment mediated by RIP1.

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
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:96824. Tlr4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 638613Extracellular Reviewed predictionAdd
BLAST
Transmembranei639 – 65921Helical; Reviewed predictionAdd
BLAST
Topological domaini660 – 835176Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: Ensembl
  2. integral component of plasma membrane Source: Ensembl
  3. lipopolysaccharide receptor complex Source: UniProtKB
  4. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed predictionAdd
BLAST
Chaini26 – 835810Toll-like receptor 4PRO_0000034723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 39
Glycosylationi34 – 341N-linked (GlcNAc...)1 Publication
Glycosylationi75 – 751N-linked (GlcNAc...)1 Publication
Glycosylationi172 – 1721N-linked (GlcNAc...)1 Publication
Glycosylationi204 – 2041N-linked (GlcNAc...)1 Publication
Glycosylationi237 – 2371N-linked (GlcNAc...)1 Publication
Disulfide bondi280 ↔ 304
Glycosylationi307 – 3071N-linked (GlcNAc...)1 Publication
Disulfide bondi388 ↔ 389
Glycosylationi492 – 4921N-linked (GlcNAc...)1 Publication
Glycosylationi495 – 4951N-linked (GlcNAc...)
Glycosylationi524 – 5241N-linked (GlcNAc...)1 Publication
Glycosylationi572 – 5721N-linked (GlcNAc...)1 Publication
Glycosylationi575 – 5751N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi580 ↔ 606
Disulfide bondi582 ↔ 625
Glycosylationi613 – 6131N-linked (GlcNAc...) Reviewed prediction
Glycosylationi621 – 6211N-linked (GlcNAc...) Reviewed prediction
Glycosylationi622 – 6221N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9QUK6.

PTM databases

PhosphoSiteiQ9QUK6.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9QUK6.
BgeeiQ9QUK6.
CleanExiMM_TLR4.
GenevestigatoriQ9QUK6.

Interactioni

Subunit structurei

Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4. Binding to bacterial LPS leads to homodimerization. Interacts with LY96 via the extracellular domain. Interacts with MYD88 and TIRAP via their respective TIR domains. Interacts with NOX4 By similarity. Interacts with CNPY3 and HSP90B1; this interaction is required for proper folding in the endoplasmic reticulum. Interacts with MLK4; this interaction leads to negative regulation of TLR4 signaling By similarity.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi204224. 21 interactions.
DIPiDIP-38573N.
IntActiQ9QUK6. 5 interactions.
STRINGi10090.ENSMUSP00000045770.

Structurei

Secondary structure

1
835
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 324
Turni33 – 353
Beta strandi36 – 383
Beta strandi40 – 423
Beta strandi49 – 513
Beta strandi57 – 593
Turni70 – 756
Beta strandi81 – 833
Turni94 – 996
Beta strandi105 – 1073
Turni118 – 1236
Beta strandi129 – 1313
Beta strandi140 – 1434
Beta strandi153 – 1553
Helixi168 – 1714
Beta strandi178 – 1803
Turni191 – 1944
Helixi195 – 1995
Beta strandi206 – 2083
Turni219 – 2246
Beta strandi226 – 2349
Helixi239 – 2479
Turni248 – 2514
Beta strandi253 – 2608
Helixi273 – 2764
Helixi279 – 2813
Beta strandi282 – 2898
Helixi297 – 3004
Helixi303 – 3053
Beta strandi309 – 3157
Beta strandi331 – 3377
Beta strandi353 – 3586
Beta strandi375 – 3773
Beta strandi380 – 3823
Beta strandi383 – 3886
Helixi391 – 3944
Beta strandi401 – 4033
Beta strandi408 – 4125
Beta strandi424 – 4263
Beta strandi430 – 4345
Turni435 – 4439
Beta strandi449 – 4513
Turni462 – 4676
Beta strandi473 – 4753
Helixi482 – 4843
Beta strandi498 – 5003
Turni511 – 5166
Beta strandi522 – 5243
Beta strandi532 – 5343
Helixi535 – 5373
Turni538 – 5403
Beta strandi546 – 5483
Beta strandi557 – 5593
Helixi561 – 5633
Beta strandi570 – 5723
Helixi582 – 5843
Helixi585 – 5884
Turni589 – 5935
Beta strandi594 – 6007
Helixi601 – 6033
Beta strandi608 – 6103
Helixi616 – 6183

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z64X-ray2.84A27-625[»]
3VQ1X-ray2.70A/B22-627[»]
3VQ2X-ray2.48A/B22-627[»]
ProteinModelPortaliQ9QUK6.
SMRiQ9QUK6. Positions 27-814.

Miscellaneous databases

EvolutionaryTraceiQ9QUK6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati54 – 7522LRR 1Add
BLAST
Repeati78 – 9922LRR 2Add
BLAST
Repeati102 – 12322LRR 3Add
BLAST
Repeati126 – 14722LRR 4Add
BLAST
Repeati150 – 17122LRR 5Add
BLAST
Repeati175 – 19824LRR 6Add
BLAST
Repeati204 – 22421LRR 7Add
BLAST
Repeati226 – 24722LRR 8Add
BLAST
Repeati248 – 26922LRR 9Add
BLAST
Repeati329 – 34921LRR 10Add
BLAST
Repeati350 – 37021LRR 11Add
BLAST
Repeati372 – 39221LRR 12Add
BLAST
Repeati398 – 42023LRR 13Add
BLAST
Repeati421 – 44222LRR 14Add
BLAST
Repeati446 – 46722LRR 15Add
BLAST
Repeati470 – 49021LRR 16Add
BLAST
Repeati495 – 51622LRR 17Add
BLAST
Repeati519 – 54022LRR 18Add
BLAST
Repeati543 – 56422LRR 19Add
BLAST
Domaini576 – 62752LRRCTAdd
BLAST
Domaini670 – 816147TIRAdd
BLAST

Domaini

The TIR domain mediates interaction with NOX4 By similarity.

Sequence similaritiesi

Contains 1 LRRCT domain.
Contains 1 TIR domain.

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG249751.
GeneTreeiENSGT00750000117512.
HOGENOMiHOG000037951.
HOVERGENiHBG018823.
InParanoidiQ9QUK6.
KOiK10160.
OMAiCHIHTIE.
OrthoDBiEOG7ZKS9G.
PhylomeDBiQ9QUK6.
TreeFamiTF351113.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR000157. TIR_dom.
IPR027168. TLR4.
IPR017241. Toll-like_receptor.
[Graphical view]
PANTHERiPTHR24365:SF230. PTHR24365:SF230. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01582. TIR. 1 hit.
[Graphical view]
PIRSFiPIRSF037595. Toll-like_receptor. 1 hit.
SMARTiSM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52200. 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

MMPPWLLART LIMALFFSCL TPGSLNPCIE VVPNITYQCM DQKLSKVPDD    50
IPSSTKNIDL SFNPLKILKS YSFSNFSELQ WLDLSRCEIE TIEDKAWHGL 100
HHLSNLILTG NPIQSFSPGS FSGLTSLENL VAVETKLASL ESFPIGQLIT 150
LKKLNVAHNF IHSCKLPAYF SNLTNLVHVD LSYNYIQTIT VNDLQFLREN 200
PQVNLSLDMS LNPIDFIQDQ AFQGIKLHEL TLRGNFNSSN IMKTCLQNLA 250
GLHVHRLILG EFKDERNLEI FEPSIMEGLC DVTIDEFRLT YTNDFSDDIV 300
KFHCLANVSA MSLAGVSIKY LEDVPKHFKW QSLSIIRCQL KQFPTLDLPF 350
LKSLTLTMNK GSISFKKVAL PSLSYLDLSR NALSFSGCCS YSDLGTNSLR 400
HLDLSFNGAI IMSANFMGLE ELQHLDFQHS TLKRVTEFSA FLSLEKLLYL 450
DISYTNTKID FDGIFLGLTS LNTLKMAGNS FKDNTLSNVF ANTTNLTFLD 500
LSKCQLEQIS WGVFDTLHRL QLLNMSHNNL LFLDSSHYNQ LYSLSTLDCS 550
FNRIETSKGI LQHFPKSLAF FNLTNNSVAC ICEHQKFLQW VKEQKQFLVN 600
VEQMTCATPV EMNTSLVLDF NNSTCYMYKT IISVSVVSVI VVSTVAFLIY 650
HFYFHLILIA GCKKYSRGES IYDAFVIYSS QNEDWVRNEL VKNLEEGVPR 700
FHLCLHYRDF IPGVAIAANI IQEGFHKSRK VIVVVSRHFI QSRWCIFEYE 750
IAQTWQFLSS RSGIIFIVLE KVEKSLLRQQ VELYRLLSRN TYLEWEDNPL 800
GRHIFWRRLK NALLDGKASN PEQTAEEEQE TATWT 835
Length:835
Mass (Da):95,519
Last modified:May 1, 2000 - v1
Checksum:i9C83B59F9A220C17
GO

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941D → N in strain: KK/HLJ. 1 Publication
Natural varianti209 – 2091M → I in strain: A/J, BALB/cJ, P/J, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK. 1 Publication
Natural varianti219 – 2191D → G in strain: SEA/GNJ. 1 Publication
Natural varianti254 – 2541V → I in strain: A/J, BALB/cJ and SEA/GNJ. 1 Publication
Natural varianti423 – 4231Q → L in strain: SEA/GNJ. 1 Publication
Natural varianti477 – 4771A → S in strain: P/J. 1 Publication
Natural varianti516 – 5161T → A in strain: LP/J. 1 Publication
Natural varianti593 – 5931E → D in strain: A/J, BALB/cJ, P/J, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK. 1 Publication
Natural varianti600 – 6001N → I in strain: KK/HLJ. 1 Publication
Natural varianti607 – 6071A → V in strain: P/J. 1 Publication
Natural varianti637 – 6371V → I in strain: P/J. 1 Publication
Natural varianti712 – 7121P → H in Lps-tolerant mice. 2 Publications
Natural varianti761 – 7611R → H in strain: A/J, BALB/cJ, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK. 1 Publication
Natural varianti811 – 8111N → K in strain: P/J. 1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 15468CEIET…TLKKL → EMNTESKSSEAHALALSHIL SPCQPSRRKLRVKLGSLSYQ RAEEGVRSSEIGYSCLHVDT RHDINAVD1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_021297.2.
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:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS18271.1.
RefSeqi NP_067272.1. NM_021297.2.
UniGenei Mm.38049.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Z64 X-ray 2.84 A 27-625 [» ]
3VQ1 X-ray 2.70 A/B 22-627 [» ]
3VQ2 X-ray 2.48 A/B 22-627 [» ]
ProteinModelPortali Q9QUK6.
SMRi Q9QUK6. Positions 27-814.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204224. 21 interactions.
DIPi DIP-38573N.
IntActi Q9QUK6. 5 interactions.
STRINGi 10090.ENSMUSP00000045770.

Chemistry

BindingDBi Q9QUK6.
ChEMBLi CHEMBL1795167.

PTM databases

PhosphoSitei Q9QUK6.

Proteomic databases

PRIDEi Q9QUK6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000048096 ; ENSMUSP00000045770 ; ENSMUSG00000039005 .
GeneIDi 21898.
KEGGi mmu:21898.
UCSCi uc008thv.1. mouse.

Organism-specific databases

CTDi 7099.
MGIi MGI:96824. Tlr4.

Phylogenomic databases

eggNOGi NOG249751.
GeneTreei ENSGT00750000117512.
HOGENOMi HOG000037951.
HOVERGENi HBG018823.
InParanoidi Q9QUK6.
KOi K10160.
OMAi CHIHTIE.
OrthoDBi EOG7ZKS9G.
PhylomeDBi Q9QUK6.
TreeFami TF351113.

Enzyme and pathway databases

Reactomei REACT_196636. TRIF-mediated programmed cell death.
REACT_198539. TRAF6 mediated induction of TAK1 complex.
REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_226192. IKK complex recruitment mediated by RIP1.

Miscellaneous databases

EvolutionaryTracei Q9QUK6.
NextBioi 301436.
PROi Q9QUK6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9QUK6.
Bgeei Q9QUK6.
CleanExi MM_TLR4.
Genevestigatori Q9QUK6.

Family and domain databases

Gene3Di 3.40.50.10140. 1 hit.
InterProi IPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR000157. TIR_dom.
IPR027168. TLR4.
IPR017241. Toll-like_receptor.
[Graphical view ]
PANTHERi PTHR24365:SF230. PTHR24365:SF230. 1 hit.
Pfami PF13855. LRR_8. 3 hits.
PF01582. TIR. 1 hit.
[Graphical view ]
PIRSFi PIRSF037595. Toll-like_receptor. 1 hit.
SMARTi SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view ]
SUPFAMi SSF52200. SSF52200. 1 hit.
PROSITEi PS50104. TIR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic and physical mapping of the Lps locus: identification of the Toll-4 receptor as a candidate gene in the critical region."
    Poltorak A., Smirnova I., He X., Liu M.-Y., Van Huffel C., Birdwell D., Alejos E., Silva M., Du X., Thompson P., Chan E.K.L., Ledesma J., Roe B., Clifton S., Vogel S.N., Beutler B.
    Blood Cells Mol. Dis. 24:340-355(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C3H/HeJ.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LPS-TOLERANT HIS-712.
    Strain: C3H/HeJ.
  3. "Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4)."
    Qureshi S.T., Lariviere L., Leveque G., Clermont S., Moore K.J., Gros P., Malo D.
    J. Exp. Med. 189:615-625(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LPS-TOLERANT HIS-712.
    Strain: C57BL/6J.
  4. "The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens."
    Underhill D.M., Ozinsky A., Hajjar A.M., Stevens A., Wilson C.B., Bassetti M., Aderem A.
    Nature 401:811-815(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage.
  5. "Phylogenetic variation and polymorphism at the Toll-like receptor 4 locus (TLR4)."
    Smirnova I., Poltorak A., Chan E.K.L., McBride C., Beutler B.
    Genome Biol. 1:RESEARCH002.1-RESEARCH002.10(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-94; ILE-209; GLY-219; ILE-254; LEU-423; SER-477; ALA-516; ASP-593; ILE-600; VAL-607; ILE-637; HIS-761 AND LYS-811.
    Strain: Various strains.
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-154.
    Strain: C57BL/6J.
    Tissue: Skin.
  7. "Murine Toll-like receptor 4 confers lipopolysaccharide responsiveness as determined by activation of NF kappa B and expression of the inducible cyclooxygenase."
    Rhee S.H., Hwang D.
    J. Biol. Chem. 275:34035-34040(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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. "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 HSP90B1.
  10. 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)
  11. "Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran."
    Kim H.M., Park B.S., Kim J.-I., Kim S.E., Lee J., Oh S.C., Enkhbayar P., Matsushima N., Lee H., Yoo O.J., Lee J.-O.
    Cell 130:906-917(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 27-625 IN COMPLEX WITH LY96, GLYCOSYLATION AT ASN-34; ASN-75; ASN-172; ASN-204; ASN-237; ASN-307; ASN-492; ASN-524 AND ASN-572.

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: September 3, 2014
This is version 131 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

External Data

Dasty 3

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