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Q9QUK6

- TLR4_MOUSE

UniProt

Q9QUK6 - TLR4_MOUSE

Protein

Toll-like receptor 4

Gene

Tlr4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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. Also involved in LPS-independent inflammatory responses triggered by free fatty acids such as palmitate.2 Publications

    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

    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

    Membrane By similarity; Single-pass type I membrane protein By similarity

    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

    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 – 2525Sequence AnalysisAdd
    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...)Sequence Analysis
    Disulfide bondi580 ↔ 606
    Disulfide bondi582 ↔ 625
    Glycosylationi613 – 6131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi621 – 6211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi622 – 6221N-linked (GlcNAc...)Sequence Analysis

    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.By similarity

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9QUK6.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 638613ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini660 – 835176CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei639 – 65921HelicalSequence AnalysisAdd
    BLAST

    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 – 816147TIRPROSITE-ProRule annotationAdd
    BLAST

    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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 15468CEIET…TLKKL → EMNTESKSSEAHALALSHIL SPCQPSRRKLRVKLGSLSYQ RAEEGVRSSEIGYSCLHVDT RHDINAVD(PubMed:16141072)CuratedAdd
    BLAST

    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 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

    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. "Toll-like receptor-4 mediates vascular inflammation and insulin resistance in diet-induced obesity."
      Kim F., Pham M., Luttrell I., Bannerman D.D., Tupper J., Thaler J., Hawn T.R., Raines E.W., Schwartz M.W.
      Circ. Res. 100:1589-1596(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "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.
    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 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. "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: October 1, 2014
    This is version 132 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