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Toll-like receptor 1 (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)

 TLR1_MOUSE              Reviewed;         795 AA.
Q9EPQ1; Q9EPW5;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 147.
RecName: Full=Toll-like receptor 1;
AltName: Full=Toll/interleukin-1 receptor-like protein;
Short=TIL;
AltName: CD_antigen=CD281;
Flags: Precursor;
Name=Tlr1;
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], AND SUBCELLULAR LOCATION.
STRAIN=BALB/cJ; TISSUE=Macrophage;
PubMed=11095740; DOI=10.1073/pnas.250476497;
Ozinsky A., Underhill D.M., Fontenot J.D., Hajjar A.M., Smith K.D.,
Wilson C.B., Schroeder L., Aderem A.;
"The repertoire for pattern recognition of pathogens by the innate
immune system is defined by cooperation between Toll-like receptors.";
Proc. Natl. Acad. Sci. U.S.A. 97:13766-13771(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Macrophage;
PubMed=11123271; DOI=10.4049/jimmunol.166.1.15;
Hajjar A.M., O'Mahony D.S., Ozinsky A., Underhill D.M., Aderem A.,
Klebanoff S.J., Wilson C.B.;
"Functional interactions between Toll-like receptor (TLR) 2 and TLR1
or TLR6 in response to phenol-soluble modulin.";
J. Immunol. 166:15-19(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Spleen;
Thomson D.P., Campbell C.C., Liew F.Y., Xu D.;
"Cloning of Mus musculus Toll-like receptor 1.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 681-692, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
INTERACTION WITH CNPY3, AND SUBCELLULAR LOCATION.
PubMed=17998391; DOI=10.1084/jem.20071132;
Takahashi K., Shibata T., Akashi-Takamura S., Kiyokawa T.,
Wakabayashi Y., Tanimura N., Kobayashi T., Matsumoto F., Fukui R.,
Kouro T., Nagai Y., Takatsu K., Saitoh S., Miyake K.;
"A protein associated with Toll-like receptor (TLR) 4 (PRAT4A) is
required for TLR-dependent immune responses.";
J. Exp. Med. 204:2963-2976(2007).
[6]
FUNCTION.
TISSUE=Macrophage;
PubMed=19362712; DOI=10.1016/j.cellimm.2009.03.008;
Drage M.G., Pecora N.D., Hise A.G., Febbraio M., Silverstein R.L.,
Golenbock D.T., Boom W.H., Harding C.V.;
"TLR2 and its co-receptors determine responses of macrophages and
dendritic cells to lipoproteins of Mycobacterium tuberculosis.";
Cell. Immunol. 258:29-37(2009).
-!- FUNCTION: Participates in the innate immune response to microbial
agents. Specifically recognizes diacylated and triacylated
lipopeptides. Cooperates with TLR2 to mediate the innate immune
response to bacterial lipoproteins or lipopeptides. Forms the
activation cluster TLR2:TLR1:CD14 in response to triacylated
lipopeptides, this cluster triggers signaling from the cell
surface and subsequently is targeted to the Golgi in a lipid-raft
dependent pathway. Acts via MYD88 and TRAF6, leading to NF-kappa-B
activation, cytokine secretion and the inflammatory response (By
similarity). Acts as a coreceptor for M.tuberculosis lipoproteins
LprG, LpqH and PhoS1 (pstS1), in conjunction with TLR2 and for
some but not all lipoproteins CD14 and/or CD36. The lipoproteins
act as agonists to modulate antigen presenting cell functions in
response to the pathogen (PubMed:19362712).
{ECO:0000250|UniProtKB:Q15399, ECO:0000269|PubMed:19362712}.
-!- SUBUNIT: Interacts (via extracellular domain) with TLR2. TLR2
seems to exist in heterodimers with either TLR1 or TLR6 before
stimulation by the ligand. The heterodimers form bigger oligomers
in response to their corresponding ligands as well as further
heterotypic associations with other receptors such as CD14 and/or
CD36 (By similarity). Binds MYD88 (via TIR domain). Interacts with
CNPY3 (PubMed:17998391). {ECO:0000250|UniProtKB:Q15399,
ECO:0000269|PubMed:17998391}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11095740,
ECO:0000269|PubMed:17998391}; Single-pass type I membrane protein
{ECO:0000255}. Cytoplasmic vesicle, phagosome membrane
{ECO:0000269|PubMed:11095740}; Single-pass type I membrane protein
{ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:Q15399}. Golgi
apparatus {ECO:0000250|UniProtKB:Q15399}. Note=Does not reside in
lipid rafts before stimulation but accumulates increasingly in the
raft upon the presence of the microbial ligand. In response to
triacylated lipoproteins, TLR2:TLR1 heterodimers are recruited in
lipid rafts, this recruitment determine the intracellular
targeting to the Golgi apparatus. {ECO:0000250|UniProtKB:Q15399}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY009154; AAG37302.1; -; mRNA.
EMBL; AF316985; AAG35062.1; -; mRNA.
CCDS; CCDS19302.1; -.
RefSeq; NP_001263374.1; NM_001276445.1.
RefSeq; NP_109607.1; NM_030682.2.
RefSeq; XP_006503914.1; XM_006503851.2.
RefSeq; XP_006503915.1; XM_006503852.3.
RefSeq; XP_006503916.1; XM_006503853.1.
RefSeq; XP_006503917.1; XM_006503854.1.
RefSeq; XP_006503919.1; XM_006503856.1.
RefSeq; XP_011239022.1; XM_011240720.2.
UniGene; Mm.273024; -.
ProteinModelPortal; Q9EPQ1; -.
SMR; Q9EPQ1; -.
IntAct; Q9EPQ1; 6.
STRING; 10090.ENSMUSP00000060793; -.
ChEMBL; CHEMBL2146338; -.
iPTMnet; Q9EPQ1; -.
PhosphoSitePlus; Q9EPQ1; -.
MaxQB; Q9EPQ1; -.
PaxDb; Q9EPQ1; -.
PRIDE; Q9EPQ1; -.
Ensembl; ENSMUST00000059349; ENSMUSP00000060793; ENSMUSG00000044827.
Ensembl; ENSMUST00000197315; ENSMUSP00000142500; ENSMUSG00000044827.
GeneID; 21897; -.
KEGG; mmu:21897; -.
UCSC; uc008xmw.2; mouse.
CTD; 7096; -.
MGI; MGI:1341295; Tlr1.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000008676; -.
HOVERGEN; HBG023180; -.
InParanoid; Q9EPQ1; -.
KO; K05398; -.
OMA; NNIETTW; -.
OrthoDB; EOG091G0356; -.
PhylomeDB; Q9EPQ1; -.
TreeFam; TF351113; -.
Reactome; R-MMU-1461957; Beta defensins.
Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
PRO; PR:Q9EPQ1; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000044827; Expressed in 115 organ(s), highest expression level in lymph node.
CleanEx; MM_TLR1; -.
ExpressionAtlas; Q9EPQ1; baseline and differential.
Genevisible; Q9EPQ1; MM.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; NAS:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0035354; C:Toll-like receptor 1-Toll-like receptor 2 protein complex; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0071723; F:lipopeptide binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0035663; F:Toll-like receptor 2 binding; ISO:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
GO; GO:0042497; F:triacyl lipopeptide binding; NAS:UniProtKB.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; NAS:UniProtKB.
GO; GO:0001775; P:cell activation; ISO:MGI.
GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; ISS:UniProtKB.
GO; GO:0006952; P:defense response; IMP:MGI.
GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
GO; GO:0042495; P:detection of triacyl bacterial lipopeptide; ISO:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0042116; P:macrophage activation; NAS:UniProtKB.
GO; GO:0001774; P:microglial cell activation; ISO:MGI.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
GO; GO:0045410; P:positive regulation of interleukin-6 biosynthetic process; IMP:UniProtKB.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; ISO:MGI.
GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; ISO:MGI.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IMP:UniProtKB.
GO; GO:0032493; P:response to bacterial lipoprotein; ISO:MGI.
GO; GO:0034130; P:toll-like receptor 1 signaling pathway; IEA:InterPro.
GO; GO:0002224; P:toll-like receptor signaling pathway; ISO:MGI.
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; IPR025875; Leu-rich_rpt_4.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027190; TLR1.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR24365:SF261; PTHR24365:SF261; 1.
Pfam; PF12799; LRR_4; 1.
Pfam; PF13855; LRR_8; 1.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 6.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 10.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasmic vesicle;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Golgi apparatus; Immunity; Inflammatory response; Innate immunity;
Leucine-rich repeat; Membrane; Receptor; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 795 Toll-like receptor 1.
/FTId=PRO_0000034706.
TOPO_DOM 26 582 Extracellular. {ECO:0000255}.
TRANSMEM 583 603 Helical. {ECO:0000255}.
TOPO_DOM 604 795 Cytoplasmic. {ECO:0000255}.
REPEAT 54 77 LRR 1.
REPEAT 78 101 LRR 2.
REPEAT 102 125 LRR 3.
REPEAT 126 150 LRR 4.
REPEAT 151 175 LRR 5.
REPEAT 176 199 LRR 6.
REPEAT 200 223 LRR 7.
REPEAT 224 250 LRR 8.
REPEAT 251 278 LRR 9.
REPEAT 279 308 LRR 10.
REPEAT 309 337 LRR 11.
REPEAT 338 361 LRR 12.
REPEAT 362 388 LRR 13.
REPEAT 389 414 LRR 14.
REPEAT 415 437 LRR 15.
REPEAT 438 457 LRR 16.
REPEAT 458 478 LRR 17.
REPEAT 479 500 LRR 18.
REPEAT 501 524 LRR 19.
DOMAIN 524 579 LRRCT.
DOMAIN 638 782 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
REGION 316 319 Interaction with bacterial lipopeptide.
{ECO:0000250}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 432 432 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 113 135 {ECO:0000250}.
DISULFID 226 233 {ECO:0000250}.
DISULFID 346 371 {ECO:0000250}.
DISULFID 422 445 {ECO:0000250}.
CONFLICT 88 88 N -> D (in Ref. 3; AAG35062).
{ECO:0000305}.
SEQUENCE 795 AA; 90673 MW; 855356429872D232 CRC64;
MTKPNSLIFY CIIVLGLTLM KIQLSEECEL IIKRPNANLT RVPKDLPLQT TTLDLSQNNI
SELQTSDILS LSKLRVLIMS YNRLQYLNIS VFKFNTELEY LDLSHNELKV ILCHPTVSLK
HLDLSFNAFD ALPICKEFGN MSQLQFLGLS GSRVQSSSVQ LIAHLNISKV LLVLGDAYGE
KEDPESLRHV STETLHIVFP SKREFRFLLD VSVSTTIGLE LSNIKCVLED QGCSYFLRAL
SKLGKNLKLS NLTLNNVETT WNSFINILQI VWHTPVKYFS ISNVKLQGQL AFRMFNYSDT
SLKALSIHQV VTDVFSFPQS YIYSIFANMN IQNFTMSGTH MVHMLCPSQV SPFLHVDFTD
NLLTDMVFKD CRNLVRLKTL SLQKNQLKNL ENIILTSAKM TSLQKLDISQ NSLRYSDGGI
PCAWTQSLLV LNLSSNMLTG SVFRCLPPKV KVLDLHNNRI MSIPKDVTHL QALQELNVAS
NSLTDLPGCG AFSSLSVLVI DHNSVSHPSE DFFQSCQNIR SLTAGNNPFQ CTCELRDFVK
NIGWVAREVV EGWPDSYRCD YPESSRGTAL RDFHMSPLSC DTVLLTVTIG ATMLVLAVTG
AFLCLYFDLP WYVRMLCQWT QTRHRARHIP LEELQRNLQF HAFVSYSGHD SAWVKNELLP
NLEKDDIQIC LHERNFVPGK SIVENIINFI EKSYKSIFVL SPHFIQSEWC HYELYFAHHN
LFHEGSDNLI LILLAPIPQY SIPTNYHKLK TLMSRRTYLE WPTEKNKHGL FWANLRASIN
VKLVNQAEGT CYTQQ


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