TLR3_BOVIN
ID TLR3_BOVIN Reviewed; 904 AA.
AC Q5TJ59;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Toll-like receptor 3;
DE AltName: CD_antigen=CD283;
DE Flags: Precursor;
GN Name=TLR3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RA Yang W., Werling D., Goldammer T., Seyfert H.M.;
RT "Molecular characterization of the bovine TLR3-encoding gene reveals
RT expression from alternative promoters.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll-
CC like receptors) control host immune response against pathogens through
CC recognition of molecular patterns specific to microorganisms. TLR3 is a
CC nucleotide-sensing TLR which is activated by double-stranded RNA, a
CC sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to
CC NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion
CC and the inflammatory response (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer; dimerization is triggered by ligand-
CC binding, the signaling unit is composed of one ds-RNA of around 40 bp
CC and two TLR3 molecules, and lateral clustering of signaling units along
CC the length of the ds-RNA ligand is required for TLR3 signal
CC transduction. Interacts (via transmembrane domain) with UNC93B1; the
CC interaction is required for transport from the ER to the endosomes.
CC Interacts with TICAM1 (via the TIR domain) in response to poly(I:C) and
CC this interaction is enhanced in the presence of WDFY1. Interacts with
CC SRC; upon binding of double-stranded RNA. The tyrosine-phosphorylated
CC form (via TIR domain) interacts with WDFY1 (via WD repeat 2) in
CC response to poly(I:C). {ECO:0000250|UniProtKB:O15455}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein. Endosome membrane {ECO:0000250|UniProtKB:O15455}.
CC Early endosome {ECO:0000250|UniProtKB:O15455}.
CC -!- DOMAIN: ds-RNA binding is mediated by LRR 1 to 3, and LRR 17 to 18.
CC {ECO:0000250}.
CC -!- PTM: TLR3 signaling requires a proteolytic cleavage mediated by
CC cathepsins CTSB and CTSH, the cleavage occurs between amino acids 252
CC and 346. The cleaved form of TLR3 is the predominant form found in
CC endosomes (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
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DR EMBL; AJ812026; CAH19226.1; -; mRNA.
DR RefSeq; NP_001008664.1; NM_001008664.1.
DR AlphaFoldDB; Q5TJ59; -.
DR SMR; Q5TJ59; -.
DR STRING; 9913.ENSBTAP00000011445; -.
DR PaxDb; Q5TJ59; -.
DR PRIDE; Q5TJ59; -.
DR GeneID; 281535; -.
DR KEGG; bta:281535; -.
DR CTD; 7098; -.
DR eggNOG; KOG4641; Eukaryota.
DR InParanoid; Q5TJ59; -.
DR OrthoDB; 737804at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:InterPro.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
DR GO; GO:0043331; P:response to dsRNA; IBA:GO_Central.
DR GO; GO:0043330; P:response to exogenous dsRNA; IEA:InterPro.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IEA:InterPro.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR027173; TLR3.
DR InterPro; IPR041015; TLR3_TMD.
DR InterPro; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR PANTHER; PTHR24365:SF524; PTHR24365:SF524; 1.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 6.
DR Pfam; PF01582; TIR; 1.
DR Pfam; PF17968; Tlr3_TMD; 1.
DR SMART; SM00369; LRR_TYP; 16.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 20.
DR PROSITE; PS50104; TIR; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein; Immunity;
KW Inflammatory response; Innate immunity; Leucine-rich repeat; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; RNA-binding; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..904
FT /note="Toll-like receptor 3"
FT /id="PRO_0000253496"
FT TOPO_DOM 27..705
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 727..904
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..52
FT /note="LRRNT"
FT REPEAT 53..74
FT /note="LRR 1"
FT REPEAT 77..98
FT /note="LRR 2"
FT REPEAT 101..122
FT /note="LRR 3"
FT REPEAT 125..146
FT /note="LRR 4"
FT REPEAT 149..170
FT /note="LRR 5"
FT REPEAT 173..194
FT /note="LRR 6"
FT REPEAT 199..220
FT /note="LRR 7"
FT REPEAT 223..245
FT /note="LRR 8"
FT REPEAT 250..271
FT /note="LRR 9"
FT REPEAT 276..297
FT /note="LRR 10"
FT REPEAT 300..321
FT /note="LRR 11"
FT REPEAT 324..345
FT /note="LRR 12"
FT REPEAT 357..378
FT /note="LRR 13"
FT REPEAT 381..401
FT /note="LRR 14"
FT REPEAT 409..430
FT /note="LRR 15"
FT REPEAT 433..455
FT /note="LRR 16"
FT REPEAT 466..487
FT /note="LRR 17"
FT REPEAT 508..529
FT /note="LRR 18"
FT REPEAT 532..553
FT /note="LRR 19"
FT REPEAT 564..585
FT /note="LRR 20"
FT REPEAT 588..609
FT /note="LRR 21"
FT REPEAT 612..633
FT /note="LRR 22"
FT DOMAIN 646..699
FT /note="LRRCT"
FT DOMAIN 754..897
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT MOD_RES 759
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15455"
FT MOD_RES 858
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15455"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..38
FT /evidence="ECO:0000250"
FT DISULFID 96..123
FT /evidence="ECO:0000250"
FT DISULFID 650..678
FT /evidence="ECO:0000250"
FT DISULFID 652..697
FT /evidence="ECO:0000250"
SQ 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
