TLR3_BOSTR
ID TLR3_BOSTR Reviewed; 904 AA.
AC Q0PV50;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Toll-like receptor 3;
DE AltName: CD_antigen=CD283;
DE Flags: Precursor;
GN Name=TLR3;
OS Boselaphus tragocamelus (Nilgai).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Boselaphus.
OX NCBI_TaxID=9917;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17119952; DOI=10.1007/s00251-006-0174-6;
RA Dhara A., Saini M., Das D.K., Swarup D., Sharma B., Kumar S., Gupta P.K.;
RT "Molecular characterization of coding sequences and analysis of Toll-like
RT receptor 3 mRNA expression in water buffalo (Bubalus bubalis) and nilgai
RT (Boselaphus tragocamelus).";
RL Immunogenetics 59:69-76(2007).
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, cytokine secretion and the inflammatory response
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer; dimerization is triggered by ligand-
CC binding and is required for TLR3 signaling. Interacts (via
CC transmembrane domain) with UNC93B1. Interacts with TICAM1 (via the TIR
CC domain) in response to poly(I:C) and this interaction is enhanced the
CC presence of WDFY1. Interacts with SRC; upon binding of double-stranded
CC RNA. The tyrosine-phosphorylated form (via TIR domain) interacts with
CC WDFY1 (via WD repeat 2) in response to poly(I:C).
CC {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 -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
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DR EMBL; DQ767878; ABG77523.1; -; mRNA.
DR AlphaFoldDB; Q0PV50; -.
DR SMR; Q0PV50; -.
DR PRIDE; Q0PV50; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
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: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; PF13855; LRR_8; 7.
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; Repeat; RNA-binding; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..904
FT /note="Toll-like receptor 3"
FT /id="PRO_0000253495"
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..196
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 414
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; 103766 MW; C2CFFEFF47034412 CRC64;
MSRPLPYHIY FFTGLLTCWI LCTSSAHKCT VRHEVADCSH LKLTQIPEDL PTNITVLNLT
HNQLRRLPPA NFTRYSRLTI LDGGFNSISK LEPELCQNLP WLEILNLQHN EISQLSDKTF
VFCMNLTELH LMSNSIQKIQ NDPFKNLKNL IKLDLSHNGL SSTKLGTQLQ LENLQELLLS
NNKISSLTPE ELDFLGNSSL ERLELSSNQI KEFSPGCFHA IGKLSGLSLN NAKLSPSLTE
KLCLELSNTS IENLSLSSNQ LDTISHTTFS GLKQTNLTTL DLSRSSLRVM DNDSFAWLPH
LEYLSLEYNN IEHLSSRSFY GLSNLRHLNL RWSFTRQSIS LTSLPKIDDF SFQWLKCLEY
LNMEDNNFPS IKRNTFTGLV RLKFLSLSNS FSSLRTLTNE TFLSLAGSPL LLLNLTKNKI
SKIQSGAFSW LGHLEVLDLG LNEIGQELTG QEWRGLDNIV EIYLSYNKYL ELTTNSFTSV
PSLQRLMLRR VALKNVACSP SPFRPLPNLV ILDLSNNNIA NVNDELLKGL EKLEILDLQH
NNLARLWKHA NPGGPVQFLK GLSHLRILNL GSNGFDEIPV EAFKDLRELK SIDLGMNNLN
ILPQSVFDNQ VSLKSLSLQK NLITSVQKTV FGPAFRNLSY LDMRFNPFDC TCESIAWFVN
WINSTHTNIS ELSNHYLCNT PPQYHGFPVM LFDVSPCKDS APFELLFMIN TNILLIFIFI
VLLIHFEGWR ISFYWNVSVH RVLGFKEIDR AEQFEYAAYI IHAYKDRDWV WKHFSPMEEE
DHTLRFCLEE RDFEAGVLKL EAIVNSIRRS RKIIFVITQN LLKDPLCKRF KVHRAVQQAI
EQNLDSIILI FLEEIPDYKL NHALCLRRGM FKSHCILNWP VQKERVNAFH HKLKVALGSR
NSAH
