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Q99MB1

- TLR3_MOUSE

UniProt

Q99MB1 - TLR3_MOUSE

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Protein
Toll-like receptor 3
Gene
Tlr3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. 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.1 Publication

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. I-kappaB phosphorylation Source: Ensembl
  2. MyD88-independent toll-like receptor signaling pathway Source: InterPro
  3. cellular response to drug Source: Ensembl
  4. cellular response to exogenous dsRNA Source: Ensembl
  5. cellular response to interferon-beta Source: Ensembl
  6. cellular response to interferon-gamma Source: Ensembl
  7. cellular response to mechanical stimulus Source: Ensembl
  8. defense response Source: MGI
  9. defense response to virus Source: BHF-UCL
  10. extrinsic apoptotic signaling pathway Source: Ensembl
  11. inflammatory response Source: UniProtKB-KW
  12. innate immune response Source: BHF-UCL
  13. male gonad development Source: Ensembl
  14. microglial cell activation involved in immune response Source: Ensembl
  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 I-kappaB kinase/NF-kappaB signaling Source: MGI
  18. positive regulation of JNK cascade Source: MGI
  19. positive regulation of NF-kappaB import into nucleus Source: Ensembl
  20. positive regulation of NF-kappaB transcription factor activity Source: MGI
  21. positive regulation of apoptotic process Source: Ensembl
  22. positive regulation of chemokine biosynthetic process Source: MGI
  23. positive regulation of chemokine production Source: InterPro
  24. positive regulation of inflammatory response Source: InterPro
  25. positive regulation of interferon-alpha biosynthetic process Source: UniProtKB
  26. positive regulation of interferon-beta biosynthetic process Source: UniProtKB
  27. positive regulation of interferon-beta production Source: BHF-UCL
  28. positive regulation of interferon-gamma biosynthetic process Source: UniProtKB
  29. positive regulation of interleukin-12 production Source: BHF-UCL
  30. positive regulation of interleukin-6 production Source: BHF-UCL
  31. positive regulation of interleukin-8 production Source: Ensembl
  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 I interferon production Source: MGI
  37. positive regulation of type III 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 705680Lumenal Reviewed prediction
Add
BLAST
Transmembranei706 – 72621Helical; Reviewed prediction
Add
BLAST
Topological domaini727 – 905179Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 381 Publication
Glycosylationi53 – 531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi58 – 581N-linked (GlcNAc...) Reviewed prediction
Glycosylationi71 – 711N-linked (GlcNAc...)1 Publication
Disulfide bondi96 ↔ 1231 Publication
Glycosylationi125 – 1251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi197 – 1971N-linked (GlcNAc...)1 Publication
Glycosylationi248 – 2481N-linked (GlcNAc...) Reviewed prediction
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 – 7601Phosphotyrosine By similarity
Modified residuei859 – 8591Phosphotyrosine By 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.

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.2 Publications

Protein-protein interaction databases

IntActiQ99MB1. 1 interaction.
MINTiMINT-4138015.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ99MB1.

Family & Domainsi

Domains and Repeats

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

Domaini

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

Sequence similaritiesi

Contains 1 LRRCT domain.
Contains 1 LRRNT domain.
Contains 1 TIR domain.

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

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 129 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

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