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Q9QUN7 (TLR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Toll-like receptor 2
Alternative name(s):
CD_antigen=CD282
Gene names
Name:Tlr2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 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. May also promote apoptosis in response to lipoproteins By similarity. Ref.9

Subunit structure

Interacts with ATG16L1 By similarity. Interacts with LY96, TLR1 and TLR6 (via extracellular domain). Binds MYD88 (via TIR domain). Interacts with TICAM1. Ligand binding induces the formation of a heterodimer with TLR1 or TLR6. Interacts with CNPY3. Ref.7 Ref.9

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesiclephagosome membrane; Single-pass type I membrane protein.

Tissue specificity

Detected in a macrophage cell line, smooth muscle, lung, spleen, thymus, brain and adipose tissue.

Domain

Ester-bound lipid substrates are bound through a crevice formed between the LRR 11 and LRR 12.

The ATG16L1-binding motif mediates interaction with ATG16L1 By similarity.

Post-translational modification

Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2 By similarity.

Sequence similarities

Belongs to the Toll-like receptor family.

Contains 19 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 TIR domain.

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentCell membrane
Cytoplasmic vesicle
Membrane
   DomainLeucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processMyD88-dependent toll-like receptor signaling pathway

Inferred from genetic interaction PubMed 12719478. Source: MGI

cell surface pattern recognition receptor signaling pathway

Inferred from mutant phenotype PubMed 12719478. Source: MGI

cellular response to bacterial lipopeptide

Traceable author statement PubMed 15356140. Source: BHF-UCL

cellular response to lipoteichoic acid

Inferred from mutant phenotype PubMed 15690042. Source: MGI

cellular response to peptidoglycan

Inferred from mutant phenotype PubMed 16949315. Source: MGI

chloramphenicol transport

Inferred from mutant phenotype PubMed 12091878. Source: MGI

defense response to Gram-positive bacterium

Inferred from mutant phenotype PubMed 11067888PubMed 15690042PubMed 19139201. Source: MGI

induction by symbiont of defense-related host nitric oxide production

Inferred from mutant phenotype PubMed 16239543. Source: MGI

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement PubMed 15356140. Source: BHF-UCL

negative regulation of growth of symbiont in host

Inferred from mutant phenotype PubMed 11067888PubMed 15690042. Source: MGI

negative regulation of interleukin-12 production

Inferred from mutant phenotype PubMed 16949315. Source: MGI

negative regulation of interleukin-17 production

Inferred from mutant phenotype PubMed 16239543. Source: MGI

positive regulation of chemokine production

Inferred from mutant phenotype PubMed 16239543. Source: MGI

positive regulation of cytokine secretion

Inferred from genetic interaction PubMed 19770268. Source: MGI

positive regulation of inflammatory response

Inferred from electronic annotation. Source: InterPro

positive regulation of interferon-beta production

Inferred from direct assay PubMed 15356140. Source: BHF-UCL

positive regulation of interleukin-12 production

Inferred from direct assay PubMed 15356140. Source: BHF-UCL

positive regulation of interleukin-18 production

Inferred from direct assay PubMed 15356140. Source: BHF-UCL

positive regulation of interleukin-6 production

Inferred from direct assay PubMed 15356140. Source: BHF-UCL

positive regulation of leukocyte migration

Inferred from mutant phenotype PubMed 17114491. Source: MGI

positive regulation of macrophage cytokine production

Inferred from mutant phenotype PubMed 10549626. Source: MGI

positive regulation of nitric oxide biosynthetic process

Inferred from mutant phenotype PubMed 10549626PubMed 16239543. Source: MGI

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from direct assay PubMed 15356140. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15356140. Source: BHF-UCL

positive regulation of tumor necrosis factor biosynthetic process

Inferred from mutant phenotype PubMed 16239543. Source: MGI

positive regulation of tumor necrosis factor production

Inferred from direct assay PubMed 15356140. Source: BHF-UCL

response to bacterium

Inferred from mutant phenotype PubMed 17114491. Source: MGI

response to molecule of fungal origin

Inferred from mutant phenotype PubMed 12719478. Source: MGI

response to peptidoglycan

Inferred from mutant phenotype PubMed 10549626PubMed 17114491. Source: MGI

toll-like receptor 2 signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentToll-like receptor 1-Toll-like receptor 2 protein complex

Inferred from sequence orthology Ref.8. Source: MGI

Toll-like receptor 2-Toll-like receptor 6 protein complex

Inferred from physical interaction Ref.9. Source: MGI

external side of plasma membrane

Inferred from direct assay PubMed 15220916. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

phagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 12719478. Source: MGI

   Molecular_functiondiacyl lipopeptide binding

Inferred from direct assay Ref.8Ref.9. Source: MGI

lipoteichoic acid binding

Inferred from direct assay Ref.9. Source: MGI

protein heterodimerization activity

Inferred from physical interaction Ref.9. Source: MGI

transmembrane signaling receptor activity

Inferred from electronic annotation. Source: InterPro

triacyl lipopeptide binding

Inferred from direct assay Ref.8. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 784760Toll-like receptor 2
PRO_0000034712

Regions

Topological domain25 – 587563Extracellular Potential
Transmembrane588 – 60821Helical; Potential
Topological domain609 – 784176Cytoplasmic Potential
Repeat54 – 7724LRR 1
Repeat78 – 10124LRR 2
Repeat102 – 12524LRR 3
Repeat126 – 15025LRR 4
Repeat151 – 17525LRR 5
Repeat176 – 19924LRR 6
Repeat200 – 22324LRR 7
Repeat224 – 25027LRR 8
Repeat251 – 27828LRR 9
Repeat279 – 30830LRR 10
Repeat309 – 33729LRR 11
Repeat338 – 36124LRR 12
Repeat362 – 38827LRR 13
Repeat389 – 41426LRR 14
Repeat415 – 43723LRR 15
Repeat438 – 45720LRR 16
Repeat458 – 47821LRR 17
Repeat479 – 50022LRR 18
Repeat501 – 52424LRR 19
Domain525 – 57652LRRCT
Domain639 – 784146TIR
Motif761 – 77818ATG16L1-binding motif

Sites

Site3491Interaction with bacterial lipopeptide By similarity

Amino acid modifications

Glycosylation1471N-linked (GlcNAc...) Ref.8 Ref.9
Glycosylation4141N-linked (GlcNAc...) Ref.8 Ref.9
Glycosylation4421N-linked (GlcNAc...) Ref.8 Ref.9
Disulfide bond30 ↔ 36 Ref.8 Ref.9
Disulfide bond353 ↔ 382 Ref.8 Ref.9
Disulfide bond432 ↔ 454 Ref.8 Ref.9

Experimental info

Mutagenesis6811P → H: Abolishes MYD88-binding and response to microbial cell wall components. Ref.1
Sequence conflict591L → P in BAB23770. Ref.5
Sequence conflict821I → M in BAB23770. Ref.5

Secondary structure

..................................................................................... 784
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9QUN7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 606D56BF85F320A2

FASTA78489,449
        10         20         30         40         50         60 
MLRALWLFWI LVAITVLFSK RCSAQESLSC DASGVCDGRS RSFTSIPSGL TAAMKSLDLS 

        70         80         90        100        110        120 
FNKITYIGHG DLRACANLQV LILKSSRINT IEGDAFYSLG SLEHLDLSDN HLSSLSSSWF 

       130        140        150        160        170        180 
GPLSSLKYLN LMGNPYQTLG VTSLFPNLTN LQTLRIGNVE TFSEIRRIDF AGLTSLNELE 

       190        200        210        220        230        240 
IKALSLRNYQ SQSLKSIRDI HHLTLHLSES AFLLEIFADI LSSVRYLELR DTNLARFQFS 

       250        260        270        280        290        300 
PLPVDEVSSP MKKLAFRGSV LTDESFNELL KLLRYILELS EVEFDDCTLN GLGDFNPSES 

       310        320        330        340        350        360 
DVVSELGKVE TVTIRRLHIP QFYLFYDLST VYSLLEKVKR ITVENSKVFL VPCSFSQHLK 

       370        380        390        400        410        420 
SLEFLDLSEN LMVEEYLKNS ACKGAWPSLQ TLVLSQNHLR SMQKTGEILL TLKNLTSLDI 

       430        440        450        460        470        480 
SRNTFHPMPD SCQWPEKMRF LNLSSTGIRV VKTCIPQTLE VLDVSNNNLD SFSLFLPRLQ 

       490        500        510        520        530        540 
ELYISRNKLK TLPDASLFPV LLVMKIRENA VSTFSKDQLG SFPKLETLEA GDNHFVCSCE 

       550        560        570        580        590        600 
LLSFTMETPA LAQILVDWPD SYLCDSPPRL HGHRLQDARP SVLECHQAAL VSGVCCALLL 

       610        620        630        640        650        660 
LILLVGALCH HFHGLWYLRM MWAWLQAKRK PKKAPCRDVC YDAFVSYSEQ DSHWVENLMV 

       670        680        690        700        710        720 
QQLENSDPPF KLCLHKRDFV PGKWIIDNII DSIEKSHKTV FVLSENFVRS EWCKYELDFS 

       730        740        750        760        770        780 
HFRLFDENND AAILVLLEPI ERKAIPQRFC KLRKIMNTKT YLEWPLDEGQ QEVFWVNLRT 


AIKS 

« Hide

References

« Hide 'large scale' references
[1]"The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens."
Underhill D.M., Ozinsky A., Hajjar A.M., Stevens A., Wilson C.B., Bassetti M., Aderem A.
Nature 401:811-815(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF PRO-681.
[2]"Cells that carry a null allele for Toll-like receptor 2 are capable of responding to endotoxin."
Heine H., Kirschning C.J., Lien E., Monks B.G., Rothe M., Golenbock D.T.
J. Immunol. 162:6971-6975(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Macrophage.
[3]"Gene expressions of lipopolysaccharide receptors, Toll-like receptors 2 and 4, are differently regulated in mouse T lymphocytes."
Matsuguchi T., Takagi K., Musikacharoen T., Yoshikai Y.
Blood 95:1378-1385(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Macrophage.
[4]"The lipopolysaccharide-activated Toll-like receptor (TLR)-4 induces synthesis of the closely related receptor TLR-2 in adipocytes."
Lin Y., Lee H., Berg A.H., Lisanti M.P., Shapiro L., Scherer P.E.
J. Biol. Chem. 275:24255-24263(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Adipocyte.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Liver.
[6]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 405-413 AND 754-759, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[7]"A single base mutation in the PRAT4A gene reveals differential interaction of PRAT4A with Toll-like receptors."
Kiyokawa T., Akashi-Takamura S., Shibata T., Matsumoto F., Nishitani C., Kuroki Y., Seto Y., Miyake K.
Int. Immunol. 20:1407-1415(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CNPY3.
[8]"Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide."
Jin M.S., Kim S.E., Heo J.Y., Lee M.E., Kim H.M., Paik S.-G., Lee H., Lee J.-O.
Cell 130:1071-1082(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-506, DISULFIDE BONDS, GLYCOSYLATION AT ASN-147; ASN-414 AND ASN-442.
[9]"Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer."
Kang J.Y., Nan X., Jin M.S., Youn S.J., Ryu Y.H., Mah S., Han S.H., Lee H., Paik S.G., Lee J.O.
Immunity 31:873-884(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-506 IN COMPLEX WITH TLR6 AND LIPOPEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-147; ASN-414 AND ASN-442, FUNCTION, LRR REPEATS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF185284 mRNA. Translation: AAF04277.1.
AF124741 mRNA. Translation: AAD46481.1.
AF216289 mRNA. Translation: AAF28345.1.
AF165189 mRNA. Translation: AAD49335.1.
AK005043 mRNA. Translation: BAB23770.1.
AK154504 mRNA. Translation: BAE32635.1.
RefSeqNP_036035.3. NM_011905.3.
UniGeneMm.87596.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z81X-ray1.80A27-506[»]
2Z82X-ray2.60A27-506[»]
3A79X-ray2.90A1-506[»]
3A7BX-ray2.53A1-506[»]
3A7CX-ray2.40A1-506[»]
ProteinModelPortalQ9QUN7.
SMRQ9QUN7. Positions 27-784.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9QUN7. 1 interaction.
STRING10090.ENSMUSP00000029623.

Chemistry

ChEMBLCHEMBL1075106.

PTM databases

PhosphoSiteQ9QUN7.

Proteomic databases

PRIDEQ9QUN7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24088.
KEGGmmu:24088.

Organism-specific databases

CTD7097.
MGIMGI:1346060. Tlr2.

Phylogenomic databases

eggNOGNOG251801.
HOGENOMHOG000110611.
HOVERGENHBG108574.
InParanoidQ9QUN7.
KOK10159.
PhylomeDBQ9QUN7.

Gene expression databases

CleanExMM_TLR2.
GenevestigatorQ9QUN7.

Family and domain databases

Gene3D3.40.50.10140. 1 hit.
InterProIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027185. TLR2.
IPR017241. Toll-like_receptor.
[Graphical view]
PANTHERPTHR24365:SF17. PTHR24365:SF17. 1 hit.
PfamPF01582. TIR. 1 hit.
[Graphical view]
PIRSFPIRSF037595. Toll-like_receptor. 1 hit.
SMARTSM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMSSF52200. SSF52200. 1 hit.
PROSITEPS51450. LRR. 9 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9QUN7.
NextBio304101.
PROQ9QUN7.
SOURCESearch...

Entry information

Entry nameTLR2_MOUSE
AccessionPrimary (citable) accession number: Q9QUN7
Secondary accession number(s): Q3U400, Q9DBC4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot