ID G3X8Y8_MOUSE Unreviewed; 784 AA. AC G3X8Y8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Toll-like receptor 2 {ECO:0000256|ARBA:ARBA00017391, ECO:0000256|PIRNR:PIRNR037595}; GN Name=Tlr2 {ECO:0000313|Ensembl:ENSMUSP00000029623.10, GN ECO:0000313|MGI:MGI:1346060}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000029623.10, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000029623.10, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000029623.10, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000029623.10} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000029623.10}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- FUNCTION: Cooperates with LY96 to mediate the innate immune response to CC bacterial lipoproteins and other microbial cell wall components. CC Cooperates with TLR1 or TLR6 to mediate the innate immune response to CC bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, CC leading to NF-kappa-B activation, cytokine secretion and the CC inflammatory response. {ECO:0000256|PIRNR:PIRNR037595}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane CC {ECO:0000256|ARBA:ARBA00004596}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004596}. Membrane raft CC {ECO:0000256|ARBA:ARBA00004285}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the Toll-like receptor family. CC {ECO:0000256|ARBA:ARBA00009634, ECO:0000256|PIRNR:PIRNR037595}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; NP_036035.3; NM_011905.3. DR AlphaFoldDB; G3X8Y8; -. DR SMR; G3X8Y8; -. DR MaxQB; G3X8Y8; -. DR PeptideAtlas; G3X8Y8; -. DR ProteomicsDB; 336780; -. DR Antibodypedia; 16689; 1532 antibodies from 49 providers. DR DNASU; 24088; -. DR Ensembl; ENSMUST00000029623.11; ENSMUSP00000029623.10; ENSMUSG00000027995.11. DR GeneID; 24088; -. DR KEGG; mmu:24088; -. DR UCSC; uc008ppn.2; mouse. DR AGR; MGI:1346060; -. DR CTD; 7097; -. DR MGI; MGI:1346060; Tlr2. DR VEuPathDB; HostDB:ENSMUSG00000027995; -. DR GeneTree; ENSGT00940000156323; -. DR HOGENOM; CLU_006000_3_0_1; -. DR OMA; NRDICYD; -. DR OrthoDB; 21383at2759; -. DR PhylomeDB; G3X8Y8; -. DR TreeFam; TF351113; -. DR BioGRID-ORCS; 24088; 2 hits in 77 CRISPR screens. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; ENSMUSG00000027995; Expressed in granulocyte and 136 other cell types or tissues. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0042995; C:cell projection; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell. DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0035354; C:Toll-like receptor 1-Toll-like receptor 2 protein complex; IEA:Ensembl. DR GO; GO:0035355; C:Toll-like receptor 2-Toll-like receptor 6 protein complex; IEA:Ensembl. DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl. DR GO; GO:0038187; F:pattern recognition receptor activity; IEA:Ensembl. DR GO; GO:0042834; F:peptidoglycan binding; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0035325; F:Toll-like receptor binding; IEA:Ensembl. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro. DR GO; GO:0042497; F:triacyl lipopeptide binding; IEA:Ensembl. DR GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; IEA:Ensembl. DR GO; GO:0071223; P:cellular response to lipoteichoic acid; IEA:Ensembl. DR GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; IEA:Ensembl. DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl. DR GO; GO:0032289; P:central nervous system myelin formation; IEA:Ensembl. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl. DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl. DR GO; GO:0042496; P:detection of diacyl bacterial lipopeptide; IEA:Ensembl. DR GO; GO:0042495; P:detection of triacyl bacterial lipopeptide; IEA:Ensembl. DR GO; GO:0006691; P:leukotriene metabolic process; IEA:Ensembl. DR GO; GO:0001774; P:microglial cell activation; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0046209; P:nitric oxide metabolic process; IEA:Ensembl. DR GO; GO:1903974; P:positive regulation of cellular response to macrophage colony-stimulating factor stimulus; IEA:Ensembl. DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl. DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl. DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl. DR GO; GO:1904466; P:positive regulation of matrix metallopeptidase secretion; IEA:Ensembl. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl. DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0032680; P:regulation of tumor necrosis factor production; IEA:UniProt. DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IEA:Ensembl. DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; IEA:Ensembl. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 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; IPR017241; Toll-like_receptor. DR InterPro; IPR035897; Toll_tir_struct_dom_sf. DR PANTHER; PTHR24365; TOLL-LIKE RECEPTOR; 1. DR PANTHER; PTHR24365:SF17; TOLL-LIKE RECEPTOR 2; 1. DR Pfam; PF13516; LRR_6; 1. DR Pfam; PF13855; LRR_8; 2. DR Pfam; PF01582; TIR; 1. DR PIRSF; PIRSF037595; Toll-like_receptor; 1. DR PRINTS; PR01537; INTRLKN1R1F. DR PRINTS; PR00019; LEURICHRPT. DR SMART; SM00364; LRR_BAC; 5. DR SMART; SM00369; LRR_TYP; 7. DR SMART; SM00082; LRRCT; 1. DR SMART; SM00255; TIR; 1. DR SUPFAM; SSF52058; L domain-like; 1. DR SUPFAM; SSF52047; RNI-like; 1. DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1. DR PROSITE; PS51450; LRR; 2. DR PROSITE; PS50104; TIR; 1. PE 1: Evidence at protein level; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Immunity {ECO:0000256|ARBA:ARBA00022859, ECO:0000256|PIRNR:PIRNR037595}; KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198, KW ECO:0000256|PIRNR:PIRNR037595}; KW Innate immunity {ECO:0000256|ARBA:ARBA00022588, KW ECO:0000256|PIRNR:PIRNR037595}; KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0007829|MaxQB:G3X8Y8, KW ECO:0007829|PeptideAtlas:G3X8Y8}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR037595}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..784 FT /note="Toll-like receptor 2" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5015091847" FT TRANSMEM 589..612 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 639..782 FT /note="TIR" FT /evidence="ECO:0000259|PROSITE:PS50104" SQ SEQUENCE 784 AA; 89467 MW; BCBE96FCB988D858 CRC64; MLRALWLFWI LVAITVLFSK RCSAQESLSC DASGVCDGRS RSFTSIPSGL TAAMKSLDLS FNKITYIGHG DLRACANLQV LMLKSSRINT IEGDAFYSLG SLEHLDLSDN HLSSLSSSWF GPLSSLKYLN LMGNPYQTLG VTSLFPNLTN LQTLRIGNVE TFSEIRRIDF AGLTSLNELE IKALSLRNYQ SQSLKSIRDI HHLTLHLSES AFLLEIFADI LSSVRYLELR DTNLARFQFS PLPVDEVSSP MKKLAFRGSV LTDESFNELL KLLRYILELS EVEFDDCTLN GLGDFNPSES DVVSELGKVE TVTIRRLHIP QFYLFYDLST VYSLLEKVKR ITVENSKVFL VPCSFSQHLK SLEFLDLSEN LMVEEYLKNS ACKGAWPSLQ TLVLSQNHLR SMQKTGEILL TLKNLTSLDI SRNTFHPMPD SCQWPEKMRF LNLSSTGIRV VKTCIPQTLE VLDVSNNNLD SFSLFLPRLQ ELYISRNKLK TLPDASLFPV LLVMKIRENA VSTFSKDQLG SFPKLETLEA GDNHFVCSCE LLSFTMETPA LAQILVDWPD SYLCDSPPRL HGHRLQDARP SVLECHQAAL VSGVCCALLL LILLVGALCH HFHGLWYLRM MWAWLQAKRK PKKAPCRDVC YDAFVSYSEQ DSHWVENLMV QQLENSDPPF KLCLHKRDFV PGKWIIDNII DSIEKSHKTV FVLSENFVRS EWCKYELDFS HFRLFDENND AAILVLLEPI ERKAIPQRFC KLRKIMNTKT YLEWPLDEGQ QEVFWVNLRT AIKS //