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Q99MB1

- TLR3_MOUSE

UniProt

Q99MB1 - TLR3_MOUSE

Protein

Toll-like receptor 3

Gene

Tlr3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (31 Jan 2002)
      Previous versions | rss
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    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. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response By similarity.By similarity

    GO - Molecular functioni

    1. double-stranded RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. transmembrane signaling receptor activity Source: InterPro

    GO - Biological processi

    1. cellular response to drug Source: Ensembl
    2. cellular response to exogenous dsRNA Source: Ensembl
    3. cellular response to interferon-beta Source: Ensembl
    4. cellular response to interferon-gamma Source: Ensembl
    5. cellular response to mechanical stimulus Source: Ensembl
    6. defense response Source: MGI
    7. defense response to virus Source: BHF-UCL
    8. extrinsic apoptotic signaling pathway Source: Ensembl
    9. I-kappaB phosphorylation Source: Ensembl
    10. inflammatory response Source: UniProtKB-KW
    11. innate immune response Source: BHF-UCL
    12. male gonad development Source: Ensembl
    13. microglial cell activation involved in immune response Source: Ensembl
    14. MyD88-independent toll-like receptor signaling pathway Source: InterPro
    15. necroptotic signaling pathway Source: Ensembl
    16. pathogen-associated molecular pattern dependent induction by symbiont of host innate immune response Source: Ensembl
    17. positive regulation of apoptotic process Source: Ensembl
    18. positive regulation of chemokine biosynthetic process Source: MGI
    19. positive regulation of chemokine production Source: InterPro
    20. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
    21. positive regulation of inflammatory response Source: InterPro
    22. positive regulation of interferon-alpha biosynthetic process Source: UniProtKB
    23. positive regulation of interferon-beta biosynthetic process Source: UniProtKB
    24. positive regulation of interferon-beta production Source: BHF-UCL
    25. positive regulation of interferon-gamma biosynthetic process Source: UniProtKB
    26. positive regulation of interleukin-12 production Source: BHF-UCL
    27. positive regulation of interleukin-6 production Source: BHF-UCL
    28. positive regulation of interleukin-8 production Source: Ensembl
    29. positive regulation of JNK cascade Source: MGI
    30. positive regulation of NF-kappaB import into nucleus Source: Ensembl
    31. positive regulation of NF-kappaB transcription factor activity Source: MGI
    32. positive regulation of protein phosphorylation Source: Ensembl
    33. positive regulation of toll-like receptor signaling pathway Source: Ensembl
    34. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    35. positive regulation of tumor necrosis factor production Source: BHF-UCL
    36. positive regulation of type III interferon production Source: MGI
    37. positive regulation of type I interferon production Source: MGI
    38. response to exogenous dsRNA Source: MGI
    39. response to virus Source: MGI
    40. toll-like receptor 3 signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_196636. TRIF-mediated programmed cell death.
    REACT_198539. TRAF6 mediated induction of TAK1 complex.
    REACT_198976. Trafficking and processing of endosomal TLR.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    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 3
    Alternative name(s):
    CD_antigen: CD283
    Gene namesi
    Name:Tlr3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:2156367. Tlr3.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. endosome membrane Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW
    5. lysosomal membrane Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Endosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 905880Toll-like receptor 3PRO_0000034716Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 381 Publication
    Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi71 – 711N-linked (GlcNAc...)1 Publication
    Disulfide bondi96 ↔ 1231 Publication
    Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi197 – 1971N-linked (GlcNAc...)1 Publication
    Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi253 – 2531N-linked (GlcNAc...)1 Publication
    Glycosylationi276 – 2761N-linked (GlcNAc...)1 Publication
    Glycosylationi292 – 2921N-linked (GlcNAc...)1 Publication
    Glycosylationi399 – 3991N-linked (GlcNAc...)1 Publication
    Glycosylationi414 – 4141N-linked (GlcNAc...)1 Publication
    Glycosylationi425 – 4251N-linked (GlcNAc...)1 Publication
    Glycosylationi508 – 5081N-linked (GlcNAc...)1 Publication
    Disulfide bondi650 ↔ 6781 Publication
    Disulfide bondi652 ↔ 6971 Publication
    Glycosylationi663 – 6631N-linked (GlcNAc...)1 Publication
    Glycosylationi668 – 6681N-linked (GlcNAc...)1 Publication
    Modified residuei760 – 7601PhosphotyrosineBy similarity
    Modified residuei859 – 8591PhosphotyrosineBy similarity

    Post-translational modificationi

    TLR3 signaling requires a proteolytic cleavage mediated by cathepsins CTSB and CTSH, the cleavage occurs between amino acids 252 and 346. The cleaved form of TLR3 is the predominant form found in endosomes By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ99MB1.
    PaxDbiQ99MB1.
    PRIDEiQ99MB1.

    PTM databases

    PhosphoSiteiQ99MB1.

    Expressioni

    Tissue specificityi

    Highly expressed in lung. After intraperitoneal injection of lipopolysaccharide, highly expressed in brain, heart, kidney, liver, lung and spleen.

    Gene expression databases

    ArrayExpressiQ99MB1.
    BgeeiQ99MB1.
    CleanExiMM_TLR3.
    GenevestigatoriQ99MB1.

    Interactioni

    Subunit structurei

    Monomer and homodimer; dimerization is triggered by ligand-binding, the signaling unit is composed of one ds-RNA of around 40 bp and two TLR3 molecules, and lateral clustering of signaling units along the length of the ds-RNA ligand is required for TLR3 signal transduction. Interacts (via transmembrane domain) with UNC93B1; the interaction is required for transport from the ER to the endosomes. Interacts with TICAM1 (via the TIR domain); mediates TLR3 signaling. Interacts with SRC; upon binding of double-stranded RNA By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ99MB1. 1 interaction.
    MINTiMINT-4138015.

    Structurei

    Secondary structure

    1
    905
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 375
    Beta strandi55 – 584
    Turni69 – 724
    Turni74 – 774
    Beta strandi79 – 824
    Helixi94 – 985
    Beta strandi104 – 1063
    Helixi117 – 1204
    Beta strandi128 – 1303
    Turni143 – 1464
    Beta strandi152 – 1543
    Beta strandi167 – 1693
    Beta strandi176 – 1783
    Helixi190 – 1956
    Beta strandi199 – 2046
    Turni215 – 2206
    Beta strandi221 – 2244
    Beta strandi226 – 2283
    Helixi236 – 24611
    Beta strandi247 – 2493
    Beta strandi253 – 2553
    Beta strandi262 – 2643
    Turni266 – 2694
    Helixi270 – 2723
    Beta strandi279 – 2813
    Turni292 – 2976
    Beta strandi303 – 3053
    Turni316 – 3216
    Beta strandi327 – 3293
    Beta strandi339 – 3413
    Turni349 – 3546
    Beta strandi360 – 3623
    Turni373 – 3786
    Beta strandi384 – 3863
    Beta strandi391 – 3933
    Turni399 – 4024
    Helixi403 – 4053
    Beta strandi412 – 4143
    Turni425 – 4306
    Beta strandi436 – 4383
    Beta strandi445 – 4473
    Helixi451 – 4533
    Beta strandi461 – 4633
    Beta strandi468 – 4714
    Turni474 – 4796
    Beta strandi485 – 4873
    Beta strandi493 – 4953
    Beta strandi497 – 5004
    Turni502 – 5054
    Beta strandi511 – 5133
    Turni524 – 5296
    Beta strandi535 – 5373
    Beta strandi567 – 5693
    Turni580 – 5856
    Beta strandi591 – 5933
    Turni604 – 6096
    Beta strandi615 – 6173
    Helixi628 – 6358
    Beta strandi639 – 6424
    Helixi652 – 66413
    Helixi672 – 6754
    Beta strandi677 – 6815
    Helixi682 – 6843
    Helixi689 – 6913
    Helixi694 – 6963

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CIGX-ray2.66A28-704[»]
    3CIYX-ray3.41A/B28-704[»]
    ProteinModelPortaliQ99MB1.
    SMRiQ99MB1. Positions 28-698, 757-898.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99MB1.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 705680LumenalSequence AnalysisAdd
    BLAST
    Topological domaini727 – 905179CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei706 – 72621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 5227LRRNTAdd
    BLAST
    Repeati53 – 7422LRR 1Add
    BLAST
    Repeati77 – 9822LRR 2Add
    BLAST
    Repeati101 – 12222LRR 3Add
    BLAST
    Repeati125 – 14622LRR 4Add
    BLAST
    Repeati149 – 17022LRR 5Add
    BLAST
    Repeati173 – 19624LRR 6Add
    BLAST
    Repeati199 – 22022LRR 7Add
    BLAST
    Repeati250 – 27122LRR 8Add
    BLAST
    Repeati276 – 29722LRR 9Add
    BLAST
    Repeati300 – 32122LRR 10Add
    BLAST
    Repeati324 – 34522LRR 11Add
    BLAST
    Repeati357 – 37822LRR 12Add
    BLAST
    Repeati381 – 40121LRR 13Add
    BLAST
    Repeati409 – 43022LRR 14Add
    BLAST
    Repeati433 – 45422LRR 15Add
    BLAST
    Repeati458 – 47922LRR 16Add
    BLAST
    Repeati482 – 50221LRR 17Add
    BLAST
    Repeati508 – 52922LRR 18Add
    BLAST
    Repeati532 – 55322LRR 19Add
    BLAST
    Repeati564 – 58522LRR 20Add
    BLAST
    Repeati588 – 60922LRR 21Add
    BLAST
    Repeati612 – 63322LRR 22Add
    BLAST
    Domaini646 – 69954LRRCTAdd
    BLAST
    Domaini755 – 897143TIRPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to 18.

    Sequence similaritiesi

    Belongs to the Toll-like receptor family.Curated
    Contains 22 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 LRRNT domain.Curated
    Contains 1 TIR domain.PROSITE-ProRule annotation

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiNOG265249.
    GeneTreeiENSGT00750000117512.
    HOGENOMiHOG000251618.
    HOVERGENiHBG023181.
    InParanoidiQ99MB1.
    KOiK05401.
    OMAiIANINDD.
    OrthoDBiEOG79SDZG.
    PhylomeDBiQ99MB1.
    TreeFamiTF325595.

    Family and domain databases

    Gene3Di3.40.50.10140. 1 hit.
    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR000157. TIR_dom.
    IPR027173. TLR3.
    [Graphical view]
    PANTHERiPTHR24365:SF5. PTHR24365:SF5. 1 hit.
    PfamiPF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 6 hits.
    PF01582. TIR. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 4 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    SM00255. TIR. 1 hit.
    [Graphical view]
    SUPFAMiSSF52200. SSF52200. 1 hit.
    PROSITEiPS51450. LRR. 18 hits.
    PS50104. TIR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q99MB1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGCSSYLMY SFGGLLSLWI LLVSSTNQCT VRYNVADCSH LKLTHIPDDL    50
    PSNITVLNLT HNQLRRLPPT NFTRYSQLAI LDAGFNSISK LEPELCQILP 100
    LLKVLNLQHN ELSQISDQTF VFCTNLTELD LMSNSIHKIK SNPFKNQKNL 150
    IKLDLSHNGL SSTKLGTGVQ LENLQELLLA KNKILALRSE ELEFLGNSSL 200
    RKLDLSSNPL KEFSPGCFQT IGKLFALLLN NAQLNPHLTE KLCWELSNTS 250
    IQNLSLANNQ LLATSESTFS GLKWTNLTQL DLSYNNLHDV GNGSFSYLPS 300
    LRYLSLEYNN IQRLSPRSFY GLSNLRYLSL KRAFTKQSVS LASHPNIDDF 350
    SFQWLKYLEY LNMDDNNIPS TKSNTFTGLV SLKYLSLSKT FTSLQTLTNE 400
    TFVSLAHSPL LTLNLTKNHI SKIANGTFSW LGQLRILDLG LNEIEQKLSG 450
    QEWRGLRNIF EIYLSYNKYL QLSTSSFALV PSLQRLMLRR VALKNVDISP 500
    SPFRPLRNLT ILDLSNNNIA NINEDLLEGL ENLEILDFQH NNLARLWKRA 550
    NPGGPVNFLK GLSHLHILNL ESNGLDEIPV GVFKNLFELK SINLGLNNLN 600
    KLEPFIFDDQ TSLRSLNLQK NLITSVEKDV FGPPFQNLNS LDMRFNPFDC 650
    TCESISWFVN WINQTHTNIS ELSTHYLCNT PHHYYGFPLK LFDTSSCKDS 700
    APFELLFIIS TSMLLVFILV VLLIHIEGWR ISFYWNVSVH RILGFKEIDT 750
    QAEQFEYTAY IIHAHKDRDW VWEHFSPMEE QDQSLKFCLE ERDFEAGVLG 800
    LEAIVNSIKR SRKIIFVITH HLLKDPLCRR FKVHHAVQQA IEQNLDSIIL 850
    IFLQNIPDYK LNHALCLRRG MFKSHCILNW PVQKERINAF HHKLQVALGS 900
    RNSAH 905
    Length:905
    Mass (Da):103,671
    Last modified:January 31, 2002 - v2
    Checksum:i8EA6DBA9818E14B4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti670 – 6701S → F in AAK26117. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF420279 mRNA. Translation: AAL27007.1.
    AF355152 mRNA. Translation: AAK26117.1.
    AK083977 mRNA. Translation: BAC39082.1.
    CCDSiCCDS22278.1.
    RefSeqiNP_569054.2. NM_126166.4.
    XP_006509341.1. XM_006509278.1.
    XP_006509342.1. XM_006509279.1.
    XP_006509343.1. XM_006509280.1.
    XP_006509344.1. XM_006509281.1.
    XP_006509345.1. XM_006509282.1.
    XP_006509346.1. XM_006509283.1.
    UniGeneiMm.33874.

    Genome annotation databases

    EnsembliENSMUST00000034056; ENSMUSP00000034056; ENSMUSG00000031639.
    ENSMUST00000167106; ENSMUSP00000126556; ENSMUSG00000031639.
    GeneIDi142980.
    KEGGimmu:142980.
    UCSCiuc009loy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF420279 mRNA. Translation: AAL27007.1 .
    AF355152 mRNA. Translation: AAK26117.1 .
    AK083977 mRNA. Translation: BAC39082.1 .
    CCDSi CCDS22278.1.
    RefSeqi NP_569054.2. NM_126166.4.
    XP_006509341.1. XM_006509278.1.
    XP_006509342.1. XM_006509279.1.
    XP_006509343.1. XM_006509280.1.
    XP_006509344.1. XM_006509281.1.
    XP_006509345.1. XM_006509282.1.
    XP_006509346.1. XM_006509283.1.
    UniGenei Mm.33874.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CIG X-ray 2.66 A 28-704 [» ]
    3CIY X-ray 3.41 A/B 28-704 [» ]
    ProteinModelPortali Q99MB1.
    SMRi Q99MB1. Positions 28-698, 757-898.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q99MB1. 1 interaction.
    MINTi MINT-4138015.

    Chemistry

    ChEMBLi CHEMBL2146340.

    PTM databases

    PhosphoSitei Q99MB1.

    Proteomic databases

    MaxQBi Q99MB1.
    PaxDbi Q99MB1.
    PRIDEi Q99MB1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034056 ; ENSMUSP00000034056 ; ENSMUSG00000031639 .
    ENSMUST00000167106 ; ENSMUSP00000126556 ; ENSMUSG00000031639 .
    GeneIDi 142980.
    KEGGi mmu:142980.
    UCSCi uc009loy.1. mouse.

    Organism-specific databases

    CTDi 7098.
    MGIi MGI:2156367. Tlr3.

    Phylogenomic databases

    eggNOGi NOG265249.
    GeneTreei ENSGT00750000117512.
    HOGENOMi HOG000251618.
    HOVERGENi HBG023181.
    InParanoidi Q99MB1.
    KOi K05401.
    OMAi IANINDD.
    OrthoDBi EOG79SDZG.
    PhylomeDBi Q99MB1.
    TreeFami TF325595.

    Enzyme and pathway databases

    Reactomei REACT_196636. TRIF-mediated programmed cell death.
    REACT_198539. TRAF6 mediated induction of TAK1 complex.
    REACT_198976. Trafficking and processing of endosomal TLR.
    REACT_222971. RIP-mediated NFkB activation via ZBP1.
    REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_226192. IKK complex recruitment mediated by RIP1.

    Miscellaneous databases

    EvolutionaryTracei Q99MB1.
    NextBioi 370067.
    PROi Q99MB1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99MB1.
    Bgeei Q99MB1.
    CleanExi MM_TLR3.
    Genevestigatori Q99MB1.

    Family and domain databases

    Gene3Di 3.40.50.10140. 1 hit.
    InterProi IPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR000157. TIR_dom.
    IPR027173. TLR3.
    [Graphical view ]
    PANTHERi PTHR24365:SF5. PTHR24365:SF5. 1 hit.
    Pfami PF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 6 hits.
    PF01582. TIR. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 4 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    SM00255. TIR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52200. SSF52200. 1 hit.
    PROSITEi PS51450. LRR. 18 hits.
    PS50104. TIR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3."
      Alexopoulou L., Holt A.C., Medzhitov R., Flavell R.A.
      Nature 413:732-738(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129/Sv.
    2. "Molecular cloning of mouse Toll-like receptor 3 cDNA."
      Applequist S.E., Ljunggren H.G.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c X NIH.
      Tissue: Macrophage.
    3. "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].
      Strain: C57BL/6J.
      Tissue: Spinal ganglion.
    4. "Toll-like receptors 9 and 3 as essential components of innate immune defense against mouse cytomegalovirus infection."
      Tabeta K., Georgel P., Janssen E., Du X., Hoebe K., Crozat K., Mudd S., Shamel L., Sovath S., Goode J., Alexopoulou L., Flavell R.A., Beutler B.
      Proc. Natl. Acad. Sci. U.S.A. 101:3516-3521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CYTOMEGALOVIRUS INFECTION.
    5. "The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling."
      Brinkmann M.M., Spooner E., Hoebe K., Beutler B., Ploegh H.L., Kim Y.M.
      J. Cell Biol. 177:265-275(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH UNC93B1.
    6. "Structural basis of toll-like receptor 3 signaling with double-stranded RNA."
      Liu L., Botos I., Wang Y., Leonard J.N., Shiloach J., Segal D.M., Davies D.R.
      Science 320:379-381(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 28-704 IN COMPLEX WITH DS-RNA, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-71; ASN-197; ASN-253; ASN-276; ASN-292; ASN-399; ASN-414; ASN-425; ASN-508; ASN-663 AND ASN-668.

    Entry informationi

    Entry nameiTLR3_MOUSE
    AccessioniPrimary (citable) accession number: Q99MB1
    Secondary accession number(s): Q91ZM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: January 31, 2002
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 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