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Toll-like receptor 8 (CD antigen CD288)

 TLR8_MOUSE              Reviewed;        1032 AA.
P58682; A2AHI9; Q91XI7;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
05-DEC-2018, entry version 149.
RecName: Full=Toll-like receptor 8;
AltName: CD_antigen=CD288;
Flags: Precursor;
Name=Tlr8;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Spleen;
Heil F.J., Lipford G.B., Wagner H., Bauer S.M.;
"Molecular cloning of murine Toll-like receptor 8.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH UNC93B1.
PubMed=19451267; DOI=10.1084/jem.20082316;
Fukui R., Saitoh S., Matsumoto F., Kozuka-Hata H., Oyama M.,
Tabeta K., Beutler B., Miyake K.;
"Unc93B1 biases Toll-like receptor responses to nucleic acid in
dendritic cells toward DNA- but against RNA-sensing.";
J. Exp. Med. 206:1339-1350(2009).
[5]
INTERACTION WITH SMPDL3B.
PubMed=26095358; DOI=10.1016/j.celrep.2015.05.006;
Heinz L.X., Baumann C.L., Koeberlin M.S., Snijder B., Gawish R.,
Shui G., Sharif O., Aspalter I.M., Mueller A.C., Kandasamy R.K.,
Breitwieser F.P., Pichlmair A., Bruckner M., Rebsamen M., Blueml S.,
Karonitsch T., Fauster A., Colinge J., Bennett K.L., Knapp S.,
Wenk M.R., Superti-Furga G.;
"The lipid-modifying enzyme SMPDL3B negatively regulates innate
immunity.";
Cell Rep. 11:1919-1928(2015).
-!- 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. Acts via MYD88 and TRAF6, leading to NF-kappa-B.
activation, cytokine secretion and the inflammatory response (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with MYD88 via their respective TIR
domains (By similarity). Interacts with BTK (By similarity).
Interacts with UNC93B1. Interacts with SMPDL3B (PubMed:26095358).
{ECO:0000250|UniProtKB:Q9NR97, ECO:0000269|PubMed:19451267,
ECO:0000269|PubMed:26095358}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AY035890; AAK62677.1; -; mRNA.
EMBL; AL731735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC132054; AAI32055.1; -; mRNA.
CCDS; CCDS41209.1; -.
RefSeq; NP_001300689.1; NM_001313760.1.
RefSeq; NP_001300690.1; NM_001313761.1.
RefSeq; NP_573475.2; NM_133212.3.
UniGene; Mm.196676; -.
ProteinModelPortal; P58682; -.
SMR; P58682; -.
IntAct; P58682; 2.
STRING; 10090.ENSMUSP00000036762; -.
ChEMBL; CHEMBL3137280; -.
iPTMnet; P58682; -.
PhosphoSitePlus; P58682; -.
MaxQB; P58682; -.
PaxDb; P58682; -.
PeptideAtlas; P58682; -.
PRIDE; P58682; -.
Ensembl; ENSMUST00000049023; ENSMUSP00000036762; ENSMUSG00000040522.
Ensembl; ENSMUST00000112170; ENSMUSP00000107793; ENSMUSG00000040522.
GeneID; 170744; -.
KEGG; mmu:170744; -.
UCSC; uc009uwy.1; mouse.
CTD; 51311; -.
MGI; MGI:2176887; Tlr8.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00940000160879; -.
HOGENOM; HOG000230468; -.
HOVERGEN; HBG018601; -.
InParanoid; P58682; -.
KO; K10170; -.
OMA; FDCTCDI; -.
OrthoDB; EOG091G014D; -.
TreeFam; TF351113; -.
Reactome; R-MMU-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-MMU-168181; Toll Like Receptor 7/8 (TLR7/8) Cascade.
Reactome; R-MMU-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-MMU-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
Reactome; R-MMU-975155; MyD88 dependent cascade initiated on endosome.
PRO; PR:P58682; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000040522; Expressed in 25 organ(s), highest expression level in bone marrow macrophage.
CleanEx; MM_TLR8; -.
ExpressionAtlas; P58682; baseline and differential.
Genevisible; P58682; MM.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008329; F:signaling pattern recognition receptor activity; IBA:GO_Central.
GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0001774; P:microglial cell activation; ISO:MGI.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
GO; GO:2001183; P:negative regulation of interleukin-12 secretion; ISO:MGI.
GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB.
GO; GO:0045356; P:positive regulation of interferon-alpha biosynthetic process; ISS:UniProtKB.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; ISS:UniProtKB.
GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; ISS:UniProtKB.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; ISO:MGI.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IBA:GO_Central.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISO:MGI.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; ISS:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; IGI:MGI.
GO; GO:0009615; P:response to virus; ISO:MGI.
GO; GO:0034158; P:toll-like receptor 8 signaling pathway; ISO:MGI.
GO; GO:0002224; P:toll-like receptor signaling pathway; ISO:MGI.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR026906; LRR_5.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027175; TLR8.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR44312:SF2; PTHR44312:SF2; 1.
Pfam; PF13306; LRR_5; 1.
Pfam; PF13855; LRR_8; 4.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 13.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 22.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Leucine-rich repeat; Membrane;
Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 1032 Toll-like receptor 8.
/FTId=PRO_0000034736.
TOPO_DOM 24 818 Extracellular. {ECO:0000255}.
TRANSMEM 819 839 Helical. {ECO:0000255}.
TOPO_DOM 840 1032 Cytoplasmic. {ECO:0000255}.
REPEAT 41 61 LRR 1.
REPEAT 62 85 LRR 2.
REPEAT 87 109 LRR 3.
REPEAT 120 143 LRR 4.
REPEAT 145 165 LRR 5.
REPEAT 166 194 LRR 6.
REPEAT 195 218 LRR 7.
REPEAT 220 239 LRR 8.
REPEAT 240 267 LRR 9.
REPEAT 281 304 LRR 10.
REPEAT 306 329 LRR 11.
REPEAT 331 360 LRR 12.
REPEAT 361 384 LRR 13.
REPEAT 388 411 LRR 14.
REPEAT 413 436 LRR 15.
REPEAT 471 494 LRR 16.
REPEAT 520 543 LRR 17.
REPEAT 545 572 LRR 18.
REPEAT 574 598 LRR 19.
REPEAT 600 621 LRR 20.
REPEAT 629 652 LRR 21.
REPEAT 654 677 LRR 22.
REPEAT 678 701 LRR 23.
REPEAT 702 725 LRR 24.
REPEAT 727 749 LRR 25.
REPEAT 752 776 LRR 26.
DOMAIN 869 1016 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 357 357 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 411 411 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 502 502 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 581 581 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 671 671 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 743 743 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 754 754 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 783 783 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 49 {ECO:0000250}.
DISULFID 177 181 {ECO:0000250}.
DISULFID 252 265 {ECO:0000250}.
DISULFID 255 262 {ECO:0000250}.
DISULFID 470 500 {ECO:0000250}.
CONFLICT 613 613 R -> H (in Ref. 1; AAK62677).
{ECO:0000305}.
SEQUENCE 1032 AA; 119358 MW; CA192552F08E33EA CRC64;
MENMPPQSWI LTCFCLLSSG TSAIFHKANY SRSYPCDEIR HNSLVIAECN HRQLHEVPQT
IGKYVTNIDL SDNAITHITK ESFQKLQNLT KIDLNHNAKQ QHPNENKNGM NITEGALLSL
RNLTVLLLED NQLYTIPAGL PESLKELSLI QNNIFQVTKN NTFGLRNLER LYLGWNCYFK
CNQTFKVEDG AFKNLIHLKV LSLSFNNLFY VPPKLPSSLR KLFLSNAKIM NITQEDFKGL
ENLTLLDLSG NCPRCYNAPF PCTPCKENSS IHIHPLAFQS LTQLLYLNLS STSLRTIPST
WFENLSNLKE LHLEFNYLVQ EIASGAFLTK LPSLQILDLS FNFQYKEYLQ FINISSNFSK
LRSLKKLHLR GYVFRELKKK HFEHLQSLPN LATINLGINF IEKIDFKAFQ NFSKLDVIYL
SGNRIASVLD GTDYSSWRNR LRKPLSTDDD EFDPHVNFYH STKPLIKPQC TAYGKALDLS
LNNIFIIGKS QFEGFQDIAC LNLSFNANTQ VFNGTEFSSM PHIKYLDLTN NRLDFDDNNA
FSDLHDLEVL DLSHNAHYFS IAGVTHRLGF IQNLINLRVL NLSHNGIYTL TEESELKSIS
LKELVFSGNR LDRLWNANDG KYWSIFKSLQ NLIRLDLSYN NLQQIPNGAF LNLPQSLQEL
LISGNKLRFF NWTLLQYFPH LHLLDLSRNE LYFLPNCLSK FAHSLETLLL SHNHFSHLPS
GFLSEARNLV HLDLSFNTIK MINKSSLQTK MKTNLSILEL HGNYFDCTCD ISDFRSWLDE
NLNITIPKLV NVICSNPGDQ KSKSIMSLDL TTCVSDTTAA VLFFLTFLTT SMVMLAALVH
HLFYWDVWFI YHMCSAKLKG YRTSSTSQTF YDAYISYDTK DASVTDWVIN ELRYHLEESE
DKSVLLCLEE RDWDPGLPII DNLMQSINQS KKTIFVLTKK YAKSWNFKTA FYLALQRLMD
ENMDVIIFIL LEPVLQYSQY LRLRQRICKS SILQWPNNPK AENLFWQSLK NVVLTENDSR
YDDLYIDSIR QY


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