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Toll-like receptor 3 (CD antigen CD283)

 TLR3_BOVIN              Reviewed;         904 AA.
Q5TJ59;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
23-MAY-2018, entry version 85.
RecName: Full=Toll-like receptor 3;
AltName: CD_antigen=CD283;
Flags: Precursor;
Name=TLR3;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
Yang W., Werling D., Goldammer T., Seyfert H.M.;
"Molecular characterization of the bovine TLR3-encoding gene reveals
expression from alternative promoters.";
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: 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). {ECO:0000250}.
-!- SUBUNIT: 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) in
response to poly(I:C) and this interaction is enhanced in the
presence of WDFY1. Interacts with SRC; upon binding of double-
stranded RNA. The tyrosine-phosphorylated form (via TIR domain)
interacts with WDFY1 (via WD repeat 2) in response to poly(I:C).
{ECO:0000250|UniProtKB:O15455}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
type I membrane protein. Endosome membrane
{ECO:0000250|UniProtKB:O15455}. Early endosome
{ECO:0000250|UniProtKB:O15455}.
-!- DOMAIN: ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to
18. {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AJ812026; CAH19226.1; -; mRNA.
RefSeq; NP_001008664.1; NM_001008664.1.
UniGene; Bt.12298; -.
ProteinModelPortal; Q5TJ59; -.
SMR; Q5TJ59; -.
STRING; 9913.ENSBTAP00000011445; -.
PaxDb; Q5TJ59; -.
PRIDE; Q5TJ59; -.
GeneID; 281535; -.
KEGG; bta:281535; -.
CTD; 7098; -.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
HOVERGEN; HBG023181; -.
InParanoid; Q5TJ59; -.
KO; K05401; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; IEA:InterPro.
GO; GO:0032722; P:positive regulation of chemokine production; IEA:InterPro.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
GO; GO:0043331; P:response to dsRNA; IBA:GO_Central.
GO; GO:0043330; P:response to exogenous dsRNA; IEA:InterPro.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IEA:InterPro.
GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027173; TLR3.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR44599; PTHR44599; 1.
Pfam; PF13516; LRR_6; 1.
Pfam; PF13855; LRR_8; 6.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 16.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 20.
PROSITE; PS50104; TIR; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Endoplasmic reticulum; Endosome;
Glycoprotein; Immunity; Inflammatory response; Innate immunity;
Leucine-rich repeat; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; RNA-binding; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 904 Toll-like receptor 3.
/FTId=PRO_0000253496.
TOPO_DOM 27 705 Lumenal. {ECO:0000255}.
TRANSMEM 706 726 Helical. {ECO:0000255}.
TOPO_DOM 727 904 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 52 LRRNT.
REPEAT 53 74 LRR 1.
REPEAT 77 98 LRR 2.
REPEAT 101 122 LRR 3.
REPEAT 125 146 LRR 4.
REPEAT 149 170 LRR 5.
REPEAT 173 194 LRR 6.
REPEAT 199 220 LRR 7.
REPEAT 223 245 LRR 8.
REPEAT 250 271 LRR 9.
REPEAT 276 297 LRR 10.
REPEAT 300 321 LRR 11.
REPEAT 324 345 LRR 12.
REPEAT 357 378 LRR 13.
REPEAT 381 401 LRR 14.
REPEAT 409 430 LRR 15.
REPEAT 433 455 LRR 16.
REPEAT 466 487 LRR 17.
REPEAT 508 529 LRR 18.
REPEAT 532 553 LRR 19.
REPEAT 564 585 LRR 20.
REPEAT 588 609 LRR 21.
REPEAT 612 633 LRR 22.
DOMAIN 646 699 LRRCT.
DOMAIN 754 896 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
MOD_RES 759 759 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15455}.
MOD_RES 858 858 Phosphotyrosine.
{ECO:0000250|UniProtKB:O15455}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 248 248 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 637 637 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 663 663 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 668 668 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 29 38 {ECO:0000250}.
DISULFID 96 123 {ECO:0000250}.
DISULFID 650 678 {ECO:0000250}.
DISULFID 652 697 {ECO:0000250}.
SEQUENCE 904 AA; 103658 MW; 609CD7BEDA5C6C2A CRC64;
MSRPLPYHIH FFSGLLTCWI LCTSSAHKCT VRHEVADCSH LKLTQIPDDL PTNITVLNLT
HNQLRRLPPA NFTRYSQLTT LDGGFNSISK LEPELCQSLP WLEILNLQHN EISQLSDKTF
IFCMNLTELH LMSNSIQKIK NDPFKNLKNL IKLDLSHNGL SSTKLGTQLQ LENLQELLLS
NNKISSLTPG EFDFLGNSSL KRLELSSNQI KEFSPGCFHT LGELSGLSLN NAKLSPSLTE
KLCLELSNTS IENLSLSSNQ LDTISHTTFD GLKQTNLTTL DLSRNSLRVM GNDSFAWLPH
LEYLSLEYNN IEHLSSRSFY GLSNLRRLDL RRSFTRQSIS LTSLPKIDDF SFQWLKCLEY
LNMDDNNFPG IKRNTFTGLV RLKFLSLSNS FSSLRTLTNE TFLSLAGCPL LLLDLTKNKI
SKIQSGAFSW LGHLEVLDLG LNEIGQELTG QEWRGLDNIV EIYLSYNKYL ELTTNSFTSV
PSLQRLMLRR VALKNVDCSP SPFRPLPNLV ILDLSNNNIA NINDELLKGL EKLEILDLQH
NNLARLWKHA NPGGPVQFLK GLFHLHILNL GSNGFDEIPV EAFKDLRELK SIDLGMNNLN
ILPQSVFDNQ VSLKSLSLQK NLITSVQKTV FGPAFRNLSY LDMRFNPFDC TCESIAWFVN
WINITHTNIS ELSNHYLCNT PPQYHGYPVM LFDVSPCKDS APFELLFMIN INILLIFIFI
VLLIHFEGWR ISFYWNVSVH RVLGFKEIDR AEQFEYAAYI IHAYKDRDWV WKHSSPMEDE
DHTLRFCLEE RDFEAGVLEL EAIVNSIRRS RKIIFVVTQN LLKDPLCKRF KVHHAVQQAI
EQNLDSIILI FLEEIPDYKL NHALCLRRGM FKSHCILNWP VQKERVNAFH HKLKVALGSR
NSAH


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