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Protein

Toll-like receptor 1

Gene

Tlr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity).By similarity

GO - Molecular functioni

  1. protein heterodimerization activity Source: MGI
  2. transmembrane signaling receptor activity Source: UniProtKB
  3. triacyl lipopeptide binding Source: UniProtKB

GO - Biological processi

  1. activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  2. cellular response to triacyl bacterial lipopeptide Source: MGI
  3. defense response Source: MGI
  4. detection of triacyl bacterial lipopeptide Source: UniProtKB
  5. inflammatory response Source: UniProtKB-KW
  6. innate immune response Source: UniProtKB-KW
  7. macrophage activation Source: UniProtKB
  8. MyD88-dependent toll-like receptor signaling pathway Source: InterPro
  9. positive regulation of interleukin-6 biosynthetic process Source: UniProtKB
  10. positive regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  11. regulation of cytokine secretion Source: InterPro
  12. toll-like receptor 1 signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-like receptor 1
Alternative name(s):
Toll/interleukin-1 receptor-like protein
Short name:
TIL
CD_antigen: CD281
Gene namesi
Name:Tlr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1341295. Tlr1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 582557ExtracellularSequence AnalysisAdd
BLAST
Transmembranei583 – 60321HelicalSequence AnalysisAdd
BLAST
Topological domaini604 – 795192CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane Source: UniProtKB
  3. phagocytic vesicle Source: UniProtKB
  4. phagocytic vesicle membrane Source: UniProtKB-SubCell
  5. Toll-like receptor 1-Toll-like receptor 2 protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 795770Toll-like receptor 1PRO_0000034706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi113 ↔ 135By similarity
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi226 ↔ 233By similarity
Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi346 ↔ 371By similarity
Disulfide bondi422 ↔ 445By similarity
Glycosylationi432 – 4321N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9EPQ1.

PTM databases

PhosphoSiteiQ9EPQ1.

Expressioni

Gene expression databases

BgeeiQ9EPQ1.
CleanExiMM_TLR1.
ExpressionAtlasiQ9EPQ1. baseline and differential.
GenevestigatoriQ9EPQ1.

Interactioni

Subunit structurei

Binds MYD88 (via TIR domains) (By similarity). Interacts (via extracellular domain) with TLR2. Ligand binding induces the formation of a heterodimer with TLR2 (By similarity). Interacts with CNPY3.By similarity1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9EPQ1.
SMRiQ9EPQ1. Positions 29-576, 628-788.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati54 – 7724LRR 1Add
BLAST
Repeati78 – 10124LRR 2Add
BLAST
Repeati102 – 12524LRR 3Add
BLAST
Repeati126 – 15025LRR 4Add
BLAST
Repeati151 – 17525LRR 5Add
BLAST
Repeati176 – 19924LRR 6Add
BLAST
Repeati200 – 22324LRR 7Add
BLAST
Repeati224 – 25027LRR 8Add
BLAST
Repeati251 – 27828LRR 9Add
BLAST
Repeati279 – 30830LRR 10Add
BLAST
Repeati309 – 33729LRR 11Add
BLAST
Repeati338 – 36124LRR 12Add
BLAST
Repeati362 – 38827LRR 13Add
BLAST
Repeati389 – 41426LRR 14Add
BLAST
Repeati415 – 43723LRR 15Add
BLAST
Repeati438 – 45720LRR 16Add
BLAST
Repeati458 – 47821LRR 17Add
BLAST
Repeati479 – 50022LRR 18Add
BLAST
Repeati501 – 52424LRR 19Add
BLAST
Domaini524 – 57956LRRCTAdd
BLAST
Domaini638 – 782145TIRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni316 – 3194Interaction with bacterial lipopeptideBy similarity

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated
Contains 19 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG272762.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000008676.
HOVERGENiHBG023180.
InParanoidiQ9EPQ1.
KOiK05398.
OMAiKISCHPT.
OrthoDBiEOG7GN2M5.
PhylomeDBiQ9EPQ1.
TreeFamiTF351113.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR000157. TIR_dom.
IPR027190. TLR1.
IPR017241. Toll-like_receptor.
[Graphical view]
PANTHERiPTHR24365:SF261. PTHR24365:SF261. 1 hit.
PfamiPF12799. LRR_4. 1 hit.
PF13855. LRR_8. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
PIRSFiPIRSF037595. Toll-like_receptor. 1 hit.
SMARTiSM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 10 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9EPQ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKPNSLIFY CIIVLGLTLM KIQLSEECEL IIKRPNANLT RVPKDLPLQT
60 70 80 90 100
TTLDLSQNNI SELQTSDILS LSKLRVLIMS YNRLQYLNIS VFKFNTELEY
110 120 130 140 150
LDLSHNELKV ILCHPTVSLK HLDLSFNAFD ALPICKEFGN MSQLQFLGLS
160 170 180 190 200
GSRVQSSSVQ LIAHLNISKV LLVLGDAYGE KEDPESLRHV STETLHIVFP
210 220 230 240 250
SKREFRFLLD VSVSTTIGLE LSNIKCVLED QGCSYFLRAL SKLGKNLKLS
260 270 280 290 300
NLTLNNVETT WNSFINILQI VWHTPVKYFS ISNVKLQGQL AFRMFNYSDT
310 320 330 340 350
SLKALSIHQV VTDVFSFPQS YIYSIFANMN IQNFTMSGTH MVHMLCPSQV
360 370 380 390 400
SPFLHVDFTD NLLTDMVFKD CRNLVRLKTL SLQKNQLKNL ENIILTSAKM
410 420 430 440 450
TSLQKLDISQ NSLRYSDGGI PCAWTQSLLV LNLSSNMLTG SVFRCLPPKV
460 470 480 490 500
KVLDLHNNRI MSIPKDVTHL QALQELNVAS NSLTDLPGCG AFSSLSVLVI
510 520 530 540 550
DHNSVSHPSE DFFQSCQNIR SLTAGNNPFQ CTCELRDFVK NIGWVAREVV
560 570 580 590 600
EGWPDSYRCD YPESSRGTAL RDFHMSPLSC DTVLLTVTIG ATMLVLAVTG
610 620 630 640 650
AFLCLYFDLP WYVRMLCQWT QTRHRARHIP LEELQRNLQF HAFVSYSGHD
660 670 680 690 700
SAWVKNELLP NLEKDDIQIC LHERNFVPGK SIVENIINFI EKSYKSIFVL
710 720 730 740 750
SPHFIQSEWC HYELYFAHHN LFHEGSDNLI LILLAPIPQY SIPTNYHKLK
760 770 780 790
TLMSRRTYLE WPTEKNKHGL FWANLRASIN VKLVNQAEGT CYTQQ
Length:795
Mass (Da):90,673
Last modified:March 1, 2001 - v1
Checksum:i855356429872D232
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881N → D in AAG35062 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY009154 mRNA. Translation: AAG37302.1.
AF316985 mRNA. Translation: AAG35062.1.
CCDSiCCDS19302.1.
RefSeqiNP_001263374.1. NM_001276445.1.
NP_109607.1. NM_030682.2.
XP_006503913.1. XM_006503850.1.
XP_006503914.1. XM_006503851.1.
XP_006503915.1. XM_006503852.1.
XP_006503916.1. XM_006503853.1.
XP_006503917.1. XM_006503854.1.
XP_006503918.1. XM_006503855.1.
XP_006503919.1. XM_006503856.1.
UniGeneiMm.273024.

Genome annotation databases

EnsembliENSMUST00000059349; ENSMUSP00000060793; ENSMUSG00000044827.
GeneIDi21897.
KEGGimmu:21897.
UCSCiuc008xmv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY009154 mRNA. Translation: AAG37302.1.
AF316985 mRNA. Translation: AAG35062.1.
CCDSiCCDS19302.1.
RefSeqiNP_001263374.1. NM_001276445.1.
NP_109607.1. NM_030682.2.
XP_006503913.1. XM_006503850.1.
XP_006503914.1. XM_006503851.1.
XP_006503915.1. XM_006503852.1.
XP_006503916.1. XM_006503853.1.
XP_006503917.1. XM_006503854.1.
XP_006503918.1. XM_006503855.1.
XP_006503919.1. XM_006503856.1.
UniGeneiMm.273024.

3D structure databases

ProteinModelPortaliQ9EPQ1.
SMRiQ9EPQ1. Positions 29-576, 628-788.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9EPQ1.

Proteomic databases

PRIDEiQ9EPQ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059349; ENSMUSP00000060793; ENSMUSG00000044827.
GeneIDi21897.
KEGGimmu:21897.
UCSCiuc008xmv.1. mouse.

Organism-specific databases

CTDi7096.
MGIiMGI:1341295. Tlr1.

Phylogenomic databases

eggNOGiNOG272762.
GeneTreeiENSGT00760000119006.
HOGENOMiHOG000008676.
HOVERGENiHBG023180.
InParanoidiQ9EPQ1.
KOiK05398.
OMAiKISCHPT.
OrthoDBiEOG7GN2M5.
PhylomeDBiQ9EPQ1.
TreeFamiTF351113.

Miscellaneous databases

NextBioi301432.
PROiQ9EPQ1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EPQ1.
CleanExiMM_TLR1.
ExpressionAtlasiQ9EPQ1. baseline and differential.
GenevestigatoriQ9EPQ1.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR000157. TIR_dom.
IPR027190. TLR1.
IPR017241. Toll-like_receptor.
[Graphical view]
PANTHERiPTHR24365:SF261. PTHR24365:SF261. 1 hit.
PfamiPF12799. LRR_4. 1 hit.
PF13855. LRR_8. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
PIRSFiPIRSF037595. Toll-like_receptor. 1 hit.
SMARTiSM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMiSSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 10 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between Toll-like receptors."
    Ozinsky A., Underhill D.M., Fontenot J.D., Hajjar A.M., Smith K.D., Wilson C.B., Schroeder L., Aderem A.
    Proc. Natl. Acad. Sci. U.S.A. 97:13766-13771(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Macrophage.
  2. "Functional interactions between Toll-like receptor (TLR) 2 and TLR1 or TLR6 in response to phenol-soluble modulin."
    Hajjar A.M., O'Mahony D.S., Ozinsky A., Underhill D.M., Aderem A., Klebanoff S.J., Wilson C.B.
    J. Immunol. 166:15-19(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage.
  3. "Cloning of Mus musculus Toll-like receptor 1."
    Thomson D.P., Campbell C.C., Liew F.Y., Xu D.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Spleen.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 681-692, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "A protein associated with Toll-like receptor (TLR) 4 (PRAT4A) is required for TLR-dependent immune responses."
    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.
    J. Exp. Med. 204:2963-2976(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNPY3.

Entry informationi

Entry nameiTLR1_MOUSE
AccessioniPrimary (citable) accession number: Q9EPQ1
Secondary accession number(s): Q9EPW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: March 1, 2001
Last modified: February 4, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.