LOCUS       NP_569054                905 aa            linear   ROD 28-JAN-2025
DEFINITION  toll-like receptor 3 precursor [Mus musculus].
ACCESSION   NP_569054
VERSION     NP_569054.2
DBSOURCE    REFSEQ: accession NM_126166.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 905)
  AUTHORS   Chung,K.Y., Kim,S., Yoon,H.T., Kwon,S.H., Park,H.S., Im,J.P.,
            Kim,J.S., Kim,J.W., Han,Y.M. and Koh,S.J.
  TITLE     Toll-like receptor 3 signaling attenuated colitis-associated cancer
            development in mice
  JOURNAL   Sci Rep 14 (1), 30308 (2024)
   PUBMED   39639064
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 905)
  AUTHORS   Zhang,R.R., Yang,X.Y., Yang,Y.L., Guo,T.K., Huang,J.S., Yang,Y.S.,
            Shi,C.W., Yang,G.L., Huang,H.B., Wang,J.Z., Jiang,Y.L., Cao,X.,
            Wang,N., Zeng,Y., Yang,W.T. and Wang,C.F.
  TITLE     TLR3/TRIF and MAVS Signaling Is Essential in Regulating Mucosal T
            Cell Responses during Rotavirus Infection
  JOURNAL   J Immunol 213 (7), 1008-1022 (2024)
   PUBMED   39194407
  REMARK    GeneRIF: TLR3/TRIF and MAVS Signaling Is Essential in Regulating
            Mucosal T Cell Responses during Rotavirus Infection.
REFERENCE   3  (residues 1 to 905)
  AUTHORS   Li,N., Kumar,S.R.P., Cao,D., Munoz-Melero,M., Arisa,S., Brian,B.A.,
            Greenwood,C.M., Yamada,K., Duan,D. and Herzog,R.W.
  TITLE     Redundancy in Innate Immune Pathways That Promote CD8+ T-Cell
            Responses in AAV1 Muscle Gene Transfer
  JOURNAL   Viruses 16 (10), 1507 (2024)
   PUBMED   39459842
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 905)
  AUTHORS   Lopez,D.A., Griffin,A., Aguilar,L.M., Deering-Rice,C., Myers,E.J.,
            Warren,K.J., Welner,R.S. and Beaudin,A.E.
  TITLE     Prenatal inflammation remodels lung immunity and function by
            programming ILC2 hyperactivation
  JOURNAL   Cell Rep 43 (7), 114365 (2024)
   PUBMED   38909363
REFERENCE   5  (residues 1 to 905)
  AUTHORS   Suvieri,C., Mondanelli,G., Orabona,C., Pallotta,M.T., Panfili,E.,
            Rossini,S., Volpi,C. and Belladonna,M.L.
  TITLE     Sensing of an HIV-1-Derived Single-Stranded RNA-Oligonucleotide
            Induces Arginase 1-Mediated Tolerance
  JOURNAL   Cells 13 (13), 1088 (2024)
   PUBMED   38994942
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 905)
  AUTHORS   Takami,M., Kim,N., Rho,J. and Choi,Y.
  TITLE     Stimulation by toll-like receptors inhibits osteoclast
            differentiation
  JOURNAL   J Immunol 169 (3), 1516-1523 (2002)
   PUBMED   12133979
REFERENCE   7  (residues 1 to 905)
  AUTHORS   Matsumoto,M., Kikkawa,S., Kohase,M., Miyake,K. and Seya,T.
  TITLE     Establishment of a monoclonal antibody against human Toll-like
            receptor 3 that blocks double-stranded RNA-mediated signaling
  JOURNAL   Biochem Biophys Res Commun 293 (5), 1364-1369 (2002)
   PUBMED   12054664
REFERENCE   8  (residues 1 to 905)
  AUTHORS   Suzuki,N., Suzuki,S., Duncan,G.S., Millar,D.G., Wada,T.,
            Mirtsos,C., Takada,H., Wakeham,A., Itie,A., Li,S., Penninger,J.M.,
            Wesche,H., Ohashi,P.S., Mak,T.W. and Yeh,W.C.
  TITLE     Severe impairment of interleukin-1 and Toll-like receptor
            signalling in mice lacking IRAK-4
  JOURNAL   Nature 416 (6882), 750-756 (2002)
   PUBMED   11923871
  REMARK    GeneRIF: Severe impairment of interleukin-1 and Toll-like receptor
            signalling in mice lacking IRAK-4.
REFERENCE   9  (residues 1 to 905)
  AUTHORS   Alexopoulou,L., Holt,A.C., Medzhitov,R. and Flavell,R.A.
  TITLE     Recognition of double-stranded RNA and activation of NF-kappaB by
            Toll-like receptor 3
  JOURNAL   Nature 413 (6857), 732-738 (2001)
   PUBMED   11607032
REFERENCE   10 (residues 1 to 905)
  AUTHORS   Bogerd,A.M., Franklin,A., Rice,D.A., Schimmer,B.P. and Parker,K.L.
  TITLE     Identification and characterization of two upstream elements that
            regulate adrenocortical expression of steroid 11 beta-hydroxylase
  JOURNAL   Mol Endocrinol 4 (6), 845-850 (1990)
   PUBMED   2233742
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY770706.1, AK083977.1 and BC099937.1.
            
            On Jun 9, 2003 this sequence version replaced NP_569054.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK083977.1, BC099937.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..905
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="8"
                     /map="8 25.31 cM"
     Protein         1..905
                     /product="toll-like receptor 3 precursor"
                     /calculated_mol_wt=100933
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2756
     mat_peptide     26..905
                     /product="Toll-like receptor 3. /id=PRO_0000034716"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
                     /calculated_mol_wt=100933
     Region          37..53
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          53..74
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          54..77
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          70..>543
                     /region_name="PLN00113"
                     /note="leucine-rich repeat receptor-like protein kinase;
                     Provisional"
                     /db_xref="CDD:215061"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          77..98
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          78..101
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          101..122
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          102..125
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          125..146
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          126..149
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          149..170
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          150..199
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          173..196
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          199..220
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          200..250
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            248
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          250..271
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          251..276
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          276..297
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          277..300
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          300..321
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          301..324
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          324..345
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          325..381
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          357..378
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          381..401
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          382..433
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            399
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          409..430
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Site            414
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Site            425
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          433..454
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          434..458
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          458..479
                     /region_name="LRR 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          459..482
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          482..502
                     /region_name="LRR 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          483..508
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          503..>649
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          508..529
                     /region_name="LRR 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Site            508
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          509..532
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          532..553
                     /region_name="LRR 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          533..564
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          564..585
                     /region_name="LRR 20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          565..586
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          588..609
                     /region_name="LRR 21"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          589..610
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          612..633
                     /region_name="LRR 22"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          613..637
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          646..698
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Site            663
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Site            668
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18420935; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          699..731
                     /region_name="Tlr3_TMD"
                     /note="Toll-like receptor 3 trans-membrane domain;
                     pfam17968"
                     /db_xref="CDD:465595"
     Site            706..726
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99MB1.2)"
     Region          756..901
                     /region_name="TIR"
                     /note="Toll - interleukin 1 - resistance; smart00255"
                     /db_xref="CDD:214587"
     Site            760
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O15455; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O15455; propagated from
                     UniProtKB/Swiss-Prot (Q99MB1.2)"
     CDS             1..905
                     /gene="Tlr3"
                     /coded_by="NM_126166.5:442..3159"
                     /db_xref="CCDS:CCDS22278.1"
                     /db_xref="GeneID:142980"
                     /db_xref="MGI:MGI:2156367"
ORIGIN      
        1 mkgcssylmy sfggllslwi llvsstnqct vrynvadcsh lklthipddl psnitvlnlt
       61 hnqlrrlppt nftrysqlai ldagfnsisk lepelcqilp llkvlnlqhn elsqisdqtf
      121 vfctnlteld lmsnsihkik snpfknqknl ikldlshngl sstklgtgvq lenlqellla
      181 knkilalrse eleflgnssl rkldlssnpl kefspgcfqt igklfallln naqlnphlte
      241 klcwelsnts iqnlslannq llatsestfs glkwtnltql dlsynnlhdv gngsfsylps
      301 lrylsleynn iqrlsprsfy glsnlrylsl kraftkqsvs lashpniddf sfqwlkyley
      361 lnmddnnips tksntftglv slkylslskt ftslqtltne tfvslahspl ltlnltknhi
      421 skiangtfsw lgqlrildlg lneieqklsg qewrglrnif eiylsynkyl qlstssfalv
      481 pslqrlmlrr valknvdisp spfrplrnlt ildlsnnnia ninedllegl enleildfqh
      541 nnlarlwkra npggpvnflk glshlhilnl esngldeipv gvfknlfelk sinlglnnln
      601 klepfifddq tslrslnlqk nlitsvekdv fgppfqnlns ldmrfnpfdc tcesiswfvn
      661 winqthtnis elsthylcnt phhyygfplk lfdtssckds apfellfiis tsmllvfilv
      721 vllihiegwr isfywnvsvh rilgfkeidt qaeqfeytay iihahkdrdw vwehfspmee
      781 qdqslkfcle erdfeagvlg leaivnsikr srkiifvith hllkdplcrr fkvhhavqqa
      841 ieqnldsiil iflqnipdyk lnhalclrrg mfkshcilnw pvqkerinaf hhklqvalgs
      901 rnsah
//
