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Toll-like receptor 2 (Toll/interleukin-1 receptor-like protein 4) (CD antigen CD282)

 TLR2_HUMAN              Reviewed;         784 AA.
O60603; B3Y612; D1CS45; D1CS48; D1CS49; O15454; Q8NI00;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
22-NOV-2017, entry version 195.
RecName: Full=Toll-like receptor 2;
AltName: Full=Toll/interleukin-1 receptor-like protein 4;
AltName: CD_antigen=CD282;
Flags: Precursor;
Name=TLR2; Synonyms=TIL4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Leukocyte, and Prostate;
PubMed=9596645;
Chaudhary P.M., Ferguson C., Nguyen V., Nguyen O., Massa H.F., Eby M.,
Jasmin A., Trask B.J., Hood L., Nelson P.S.;
"Cloning and characterization of two Toll/Interleukin-1 receptor-like
genes TIL3 and TIL4: evidence for a multi-gene receptor family in
humans.";
Blood 91:4020-4027(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9435236; DOI=10.1073/pnas.95.2.588;
Rock F.L., Hardiman G., Timans J.C., Kastelein R.A., Bazan J.F.;
"A family of human receptors structurally related to Drosophila
Toll.";
Proc. Natl. Acad. Sci. U.S.A. 95:588-593(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND RESPONSE TO LIPOPOLYSACCHARIDE.
TISSUE=Fetal lung;
PubMed=9751057; DOI=10.1038/26239;
Yang R.-B., Mark M.R., Gray A.M., Huang A., Xie M.-H., Zhang M.,
Goddard A.D., Wood W.I., Gurney A.L., Godowski P.J.;
"Toll-like receptor-2 mediates lipopolysaccharide-induced cellular
signalling.";
Nature 395:284-288(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T.,
Kimura A.;
"Natural selection in the TLR-related genes in the course of primate
evolution.";
Immunogenetics 60:727-735(2008).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIS-631 AND GLN-753.
PubMed=19924287; DOI=10.1371/journal.pone.0007803;
Georgel P., Macquin C., Bahram S.;
"The heterogeneous allelic repertoire of human Toll-Like receptor
(TLR) genes.";
PLoS ONE 4:E7803-E7803(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-586.
Zhang L., Yu W.B., Ma Y.Y.;
"Cloning and sequencing of extracellular domain and its N-terminal and
C-terminal fragments of Toll-like receptor 2.";
Di 4 Jun Yi Da Xue Xue Bao 23:1085-1089(2002).
[9]
FUNCTION.
TISSUE=T-cell;
PubMed=10426995; DOI=10.1126/science.285.5428.732;
Brightbill H.D., Libraty D.H., Krutzik S.R., Yang R.B., Belisle J.T.,
Bleharski J.R., Maitland M., Norgard M.V., Plevy S.E., Smale S.T.,
Brennan P.J., Bloom B.R., Godowski P.J., Modlin R.L.;
"Host defense mechanisms triggered by microbial lipoproteins through
Toll-like receptors.";
Science 285:732-736(1999).
[10]
FUNCTION.
PubMed=10426996; DOI=10.1126/science.285.5428.736;
Aliprantis A.O., Yang R.-B., Mark M.R., Suggett S., Devaux B.,
Radolf J.D., Klimpel G.R., Godowski P.J., Zychlinsky A.;
"Cell activation and apoptosis by bacterial lipoproteins through Toll-
like receptor-2.";
Science 285:736-739(1999).
[11]
FUNCTION.
PubMed=11441107; DOI=10.4049/jimmunol.167.2.987;
Bulut Y., Faure E., Thomas L., Equils O., Arditi M.;
"Cooperation of Toll-like receptor 2 and 6 for cellular activation by
soluble tuberculosis factor and Borrelia burgdorferi outer surface
protein A lipoprotein: role of Toll-interacting protein and IL-1
receptor signaling molecules in Toll-like receptor 2 signaling.";
J. Immunol. 167:987-994(2001).
[12]
INTERACTION WITH TICAM1.
PubMed=12471095; DOI=10.4049/jimmunol.169.12.6668;
Yamamoto M., Sato S., Mori K., Hoshino K., Takeuchi O., Takeda K.,
Akira S.;
"A novel Toll/IL-1 receptor domain-containing adapter that
preferentially activates the IFN-beta promoter in the Toll-like
receptor signaling.";
J. Immunol. 169:6668-6672(2002).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CD14; CD36; TLR1
AND TLR6.
PubMed=16880211; DOI=10.1074/jbc.M602794200;
Triantafilou M., Gamper F.G., Haston R.M., Mouratis M.A., Morath S.,
Hartung T., Triantafilou K.;
"Membrane sorting of toll-like receptor (TLR)-2/6 and TLR2/1
heterodimers at the cell surface determines heterotypic associations
with CD36 and intracellular targeting.";
J. Biol. Chem. 281:31002-31011(2006).
[14]
GLYCOSYLATION AT ASN-114; ASN-199 AND ASN-442, AND MUTAGENESIS OF
ASN-114; ASN-199; THR-416 AND ASN-442.
PubMed=15173186; DOI=10.1074/jbc.M403830200;
Weber A.N., Morse M.A., Gay N.J.;
"Four N-linked glycosylation sites in human toll-like receptor 2
cooperate to direct efficient biosynthesis and secretion.";
J. Biol. Chem. 279:34589-34594(2004).
[15]
FUNCTION.
PubMed=15809303; DOI=10.1074/jbc.M411379200;
Bulut Y., Michelsen K.S., Hayrapetian L., Naiki Y., Spallek R.,
Singh M., Arditi M.;
"Mycobacterium tuberculosis heat shock proteins use diverse Toll-like
receptor pathways to activate pro-inflammatory signals.";
J. Biol. Chem. 280:20961-20967(2005).
[16]
FUNCTION.
TISSUE=Monocyte;
PubMed=16622205; DOI=10.1128/IAI.74.5.2686-2696.2006;
Jung S.B., Yang C.S., Lee J.S., Shin A.R., Jung S.S., Son J.W.,
Harding C.V., Kim H.J., Park J.K., Paik T.H., Song C.H., Jo E.K.;
"The mycobacterial 38-kilodalton glycolipoprotein antigen activates
the mitogen-activated protein kinase pathway and release of
proinflammatory cytokines through Toll-like receptors 2 and 4 in human
monocytes.";
Infect. Immun. 74:2686-2696(2006).
[17]
FUNCTION.
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).
[18]
FUNCTION, AND INTERACTION WITH M.BOVIS MPB83 AND M.TUBERCULOSIS ESXA.
PubMed=20800577; DOI=10.1016/j.bbrc.2010.08.085;
Chambers M.A., Whelan A.O., Spallek R., Singh M., Coddeville B.,
Guerardel Y., Elass E.;
"Non-acylated Mycobacterium bovis glycoprotein MPB83 binds to TLR1/2
and stimulates production of matrix metalloproteinase 9.";
Biochem. Biophys. Res. Commun. 400:403-408(2010).
[19]
FUNCTION.
TISSUE=T-cell;
PubMed=21078852; DOI=10.1128/IAI.00806-10;
Lancioni C.L., Li Q., Thomas J.J., Ding X., Thiel B., Drage M.G.,
Pecora N.D., Ziady A.G., Shank S., Harding C.V., Boom W.H.,
Rojas R.E.;
"Mycobacterium tuberculosis lipoproteins directly regulate human
memory CD4(+) T cell activation via Toll-like receptors 1 and 2.";
Infect. Immun. 79:663-673(2011).
[20]
INTERACTION WITH ATG16L1.
PubMed=23376921; DOI=10.1038/emboj.2013.8;
Boada-Romero E., Letek M., Fleischer A., Pallauf K., Ramon-Barros C.,
Pimentel-Muinos F.X.;
"TMEM59 defines a novel ATG16L1-binding motif that promotes local
activation of LC3.";
EMBO J. 32:566-582(2013).
[21]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 639-784, AND MUTAGENESIS.
PubMed=11081518; DOI=10.1038/35040600;
Xu Y., Tao X., Shen B., Horng T., Medzhitov R., Manley J.L., Tong L.;
"Structural basis for signal transduction by the Toll/interleukin-1
receptor domains.";
Nature 408:111-115(2000).
[22]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-509 IN COMPLEX WITH TLR1
AND BACTERIAL LIPOPEPTIDE ANALOG, DISULFIDE BONDS, GLYCOSYLATION AT
ASN-114; ASN-199; ASN-414 AND ASN-442, AND FUNCTION.
PubMed=17889651; DOI=10.1016/j.cell.2007.09.008;
Jin M.S., Kim S.E., Heo J.Y., Lee M.E., Kim H.M., Paik S.-G., Lee H.,
Lee J.-O.;
"Crystal structure of the TLR1-TLR2 heterodimer induced by binding of
a tri-acylated lipopeptide.";
Cell 130:1071-1082(2007).
[23]
VARIANT TRP-677, AND ASSOCIATION WITH LEPROSIS.
PubMed=11476982; DOI=10.1111/j.1574-695X.2001.tb01586.x;
Kang T.-J., Chae G.-T.;
"Detection of Toll-like receptor 2 (TLR2) mutation in the lepromatous
leprosy patients.";
FEMS Immunol. Med. Microbiol. 31:53-58(2001).
[24]
VARIANT TRP-677, AND ASSOCIATION WITH LEPROSIS.
PubMed=12646604; DOI=10.4049/jimmunol.170.7.3451;
Bochud P.-Y., Hawn T.R., Aderem A.;
"A Toll-like receptor 2 polymorphism that is associated with
lepromatous leprosy is unable to mediate mycobacterial signaling.";
J. Immunol. 170:3451-3454(2003).
[25]
VARIANTS ASP-89; ILE-411; HIS-571; HIS-631; ARG-636 AND GLN-753, AND
CHARACTERIZATION OF VARIANTS ILE-411; HIS-631 AND GLN-753.
PubMed=21618349; DOI=10.1002/humu.21486;
Ben-Ali M., Corre B., Manry J., Barreiro L.B., Quach H., Boniotto M.,
Pellegrini S., Quintana-Murci L.;
"Functional characterization of naturally occurring genetic variants
in the human TLR1-2-6 gene family.";
Hum. Mutat. 32:643-652(2011).
-!- 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
(PubMed:21078852, PubMed:17889651). Acts via MYD88 and TRAF6,
leading to NF-kappa-B activation, cytokine secretion and the
inflammatory response. May also activate immune cells and promote
apoptosis in response to the lipid moiety of lipoproteins
(PubMed:10426995, PubMed:10426996). Recognizes mycoplasmal
macrophage-activating lipopeptide-2kD (MALP-2), soluble
tuberculosis factor (STF), phenol-soluble modulin (PSM) and
B.burgdorferi outer surface protein A lipoprotein (OspA-L)
cooperatively with TLR6 (PubMed:11441107). Stimulation of
monocytes in vitro with M.tuberculosis PstS1 induces p38 MAPK and
ERK1/2 activation primarily via this receptor, but also partially
via TLR4 (PubMed:16622205). MAPK activation in response to
bacterial peptidoglycan also occurs via this receptor
(PubMed:16622205). Acts as a receptor for M.tuberculosis
lipoproteins LprA, LprG, LpqH and PstS1, some lipoproteins are
dependent on other coreceptors (TLR1, CD14 and/or CD36); the
lipoproteins act as agonists to modulate antigen presenting cell
functions in response to the pathogen (PubMed:19362712).
M.tuberculosis HSP70 (dnaK) but not HSP65 (groEL-2) acts via this
protein to stimulate NF-kappa-B expression (PubMed:15809303).
Recognizes M.tuberculosis major T-antigen EsxA (ESAT-6) which
inhibits downstream MYD88-dependent signaling (shown in mouse) (By
similarity). Forms activation clusters composed of several
receptors depending on the ligand, these clusters trigger
signaling from the cell surface and subsequently are targeted to
the Golgi in a lipid-raft dependent pathway. Forms the cluster
TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and
TLR2:TLR1:CD14 in response to triacylated lipopeptides
(PubMed:16880211). Required for normal uptake of M.tuberculosis, a
process that is inhibited by M.tuberculosis LppM (By similarity).
{ECO:0000250|UniProtKB:Q9QUN7, ECO:0000269|PubMed:10426995,
ECO:0000269|PubMed:10426996, ECO:0000269|PubMed:11441107,
ECO:0000269|PubMed:15809303, ECO:0000269|PubMed:16622205,
ECO:0000269|PubMed:16880211, ECO:0000269|PubMed:17889651,
ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:21078852}.
-!- SUBUNIT: Interacts with LY96, TLR1 and TLR6 (via extracellular
domain) (PubMed:17889651). 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 (PubMed:16880211).
Binds MYD88 (via TIR domain). Interacts with TICAM1
(PubMed:12471095). Interacts with CNPY3 (By similarity). Interacts
with ATG16L1 (PubMed:23376921). {ECO:0000250|UniProtKB:Q9QUN7,
ECO:0000269|PubMed:12471095, ECO:0000269|PubMed:16880211,
ECO:0000269|PubMed:17889651, ECO:0000269|PubMed:23376921}.
-!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis EsxA
(PubMed:20800577). Interacts with M.bovis MPB83 (PubMed:20800577).
{ECO:0000269|PubMed:20800577}.
-!- INTERACTION:
P61073:CXCR4; NbExp=3; IntAct=EBI-973722, EBI-489411;
P00533:EGFR; NbExp=2; IntAct=EBI-973722, EBI-297353;
C3PTT6:PAUF; NbExp=3; IntAct=EBI-973722, EBI-3505892;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7};
Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic
vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7};
Single-pass type I membrane protein {ECO:0000255}. Membrane raft
{ECO:0000269|PubMed:16880211}. 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 diacylated
lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts,
this recruitment determines the intracellular targeting to the
Golgi apparatus. Triacylated lipoproteins induce the same
mechanism for TLR2:TLR1 heterodimers.
{ECO:0000269|PubMed:16880211}.
-!- TISSUE SPECIFICITY: Highly expressed in peripheral blood
leukocytes, in particular in monocytes, in bone marrow, lymph node
and in spleen. Also detected in lung and in fetal liver. Levels
are low in other tissues.
-!- DOMAIN: Ester-bound lipid substrates are bound through a crevice
formed between the LRR 11 and LRR 12. {ECO:0000250}.
-!- DOMAIN: The ATG16L1-binding motif mediates interaction with
ATG16L1. {ECO:0000269|PubMed:23376921}.
-!- PTM: Glycosylation of Asn-442 is critical for secretion of the N-
terminal ectodomain of TLR2. {ECO:0000269|PubMed:15173186,
ECO:0000269|PubMed:17889651}.
-!- POLYMORPHISM: Genetic variations in TLR2 are associated with
susceptibility to leprosy [MIM:246300]. Leprosy is a chronic
disease associated with depressed cellular (but not humoral)
immunity, the bacterium requires a lower temperature than 37
degrees Celsius and thrives particularly in peripheral Schwann
cells and macrophages. The Trp-677 polymorphism in the
intracellular domain of TLR2 has a role in susceptibility to
lepromatous leprosy. Wild-type TLR2 mediates CD14-enhanced
Mycobacterium leprae-dependent activation of NFKB1, but TLR2
containing the Trp-677 polymorphism did not. The impaired function
of the Trp-677 polymorphism provides a molecular mechanism for the
poor cellular immune response associated with lepromatous leprosy.
{ECO:0000269|PubMed:11476982, ECO:0000269|PubMed:12646604}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
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EMBL; AF051152; AAC34377.1; -; mRNA.
EMBL; U88878; AAC34133.1; -; mRNA.
EMBL; AB445624; BAG55021.1; -; mRNA.
EMBL; DQ012265; AAY85644.1; -; mRNA.
EMBL; DQ012266; AAY85645.1; -; mRNA.
EMBL; DQ012267; AAY85646.1; -; mRNA.
EMBL; DQ012268; AAY85647.1; -; mRNA.
EMBL; DQ012269; AAY85648.1; -; mRNA.
EMBL; DQ012270; AAY85649.1; -; mRNA.
EMBL; DQ012271; AAY85650.1; -; mRNA.
EMBL; CH471056; EAX04952.1; -; Genomic_DNA.
EMBL; CH471056; EAX04953.1; -; Genomic_DNA.
EMBL; BC033756; AAH33756.1; -; mRNA.
EMBL; AF502291; AAM23001.1; -; mRNA.
CCDS; CCDS3784.1; -.
RefSeq; NP_001305716.1; NM_001318787.1.
RefSeq; NP_001305718.1; NM_001318789.1.
RefSeq; NP_001305719.1; NM_001318790.1.
RefSeq; NP_001305720.1; NM_001318791.1.
RefSeq; NP_001305722.1; NM_001318793.1.
RefSeq; NP_001305724.1; NM_001318795.1.
RefSeq; NP_001305725.1; NM_001318796.1.
RefSeq; NP_003255.2; NM_003264.4.
RefSeq; XP_011530517.1; XM_011532215.2.
RefSeq; XP_011530518.1; XM_011532216.2.
RefSeq; XP_016864062.1; XM_017008573.1.
RefSeq; XP_016864063.1; XM_017008574.1.
RefSeq; XP_016864064.1; XM_017008575.1.
RefSeq; XP_016864065.1; XM_017008576.1.
UniGene; Hs.519033; -.
PDB; 1FYW; X-ray; 3.00 A; A=636-784.
PDB; 1FYX; X-ray; 2.80 A; A=636-784.
PDB; 1O77; X-ray; 3.20 A; A/B/C/D/E=639-784.
PDB; 2Z7X; X-ray; 2.10 A; A=27-506.
PDB; 2Z80; X-ray; 1.80 A; A/B=1-284.
PDBsum; 1FYW; -.
PDBsum; 1FYX; -.
PDBsum; 1O77; -.
PDBsum; 2Z7X; -.
PDBsum; 2Z80; -.
ProteinModelPortal; O60603; -.
SMR; O60603; -.
BioGrid; 112952; 27.
DIP; DIP-35138N; -.
IntAct; O60603; 23.
MINT; MINT-3000106; -.
STRING; 9606.ENSP00000260010; -.
BindingDB; O60603; -.
ChEMBL; CHEMBL4163; -.
DrugBank; DB00045; OspA lipoprotein.
DrugBank; DB03963; S-(Dimethylarsenic)Cysteine.
DrugBank; DB05475; SCV-07.
GuidetoPHARMACOLOGY; 1752; -.
iPTMnet; O60603; -.
PhosphoSitePlus; O60603; -.
SwissPalm; O60603; -.
BioMuta; TLR2; -.
PaxDb; O60603; -.
PeptideAtlas; O60603; -.
PRIDE; O60603; -.
DNASU; 7097; -.
Ensembl; ENST00000260010; ENSP00000260010; ENSG00000137462.
GeneID; 7097; -.
KEGG; hsa:7097; -.
UCSC; uc063aif.1; human.
CTD; 7097; -.
DisGeNET; 7097; -.
EuPathDB; HostDB:ENSG00000137462.6; -.
GeneCards; TLR2; -.
HGNC; HGNC:11848; TLR2.
HPA; HPA060231; -.
HPA; HPA071546; -.
MalaCards; TLR2; -.
MIM; 246300; phenotype.
MIM; 603028; gene.
neXtProt; NX_O60603; -.
OpenTargets; ENSG00000137462; -.
PharmGKB; PA36550; -.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000110611; -.
HOVERGEN; HBG108574; -.
InParanoid; O60603; -.
KO; K10159; -.
OMA; IPQRFCK; -.
OrthoDB; EOG091G05L8; -.
PhylomeDB; O60603; -.
TreeFam; TF351113; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1461957; Beta defensins.
Reactome; R-HSA-166058; MyD88:Mal cascade initiated on plasma membrane.
Reactome; R-HSA-168179; Toll Like Receptor TLR1:TLR2 Cascade.
Reactome; R-HSA-168188; Toll Like Receptor TLR6:TLR2 Cascade.
Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; O60603; -.
EvolutionaryTrace; O60603; -.
GeneWiki; TLR_2; -.
GenomeRNAi; 7097; -.
PRO; PR:O60603; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000137462; -.
CleanEx; HS_TLR2; -.
ExpressionAtlas; O60603; baseline and differential.
Genevisible; O60603; HS.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0042995; C:cell projection; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0035354; C:Toll-like receptor 1-Toll-like receptor 2 protein complex; IDA:MGI.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
GO; GO:0001875; F:lipopolysaccharide receptor activity; TAS:UniProtKB.
GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IPI:ARUK-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
GO; GO:0008329; F:signaling pattern recognition receptor activity; IDA:UniProtKB.
GO; GO:0035325; F:Toll-like receptor binding; IPI:UniProtKB.
GO; GO:0042497; F:triacyl lipopeptide binding; IDA:MGI.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0001775; P:cell activation; IDA:AgBase.
GO; GO:0071221; P:cellular response to bacterial lipopeptide; TAS:BHF-UCL.
GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; IDA:UniProtKB.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IDA:MGI.
GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; IDA:UniProtKB.
GO; GO:0032289; P:central nervous system myelin formation; IEA:Ensembl.
GO; GO:0002374; P:cytokine secretion involved in immune response; IMP:CACAO.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0042496; P:detection of diacyl bacterial lipopeptide; IDA:MGI.
GO; GO:0042495; P:detection of triacyl bacterial lipopeptide; IDA:MGI.
GO; GO:0007252; P:I-kappaB phosphorylation; IDA:BHF-UCL.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
GO; GO:0032613; P:interleukin-10 production; IDA:CACAO.
GO; GO:0007612; P:learning; ISS:ARUK-UCL.
GO; GO:0006691; P:leukotriene metabolic process; IEA:Ensembl.
GO; GO:0014005; P:microglia development; ISS:ARUK-UCL.
GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0050765; P:negative regulation of phagocytosis; ISS:ARUK-UCL.
GO; GO:0051964; P:negative regulation of synapse assembly; ISS:ARUK-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0046209; P:nitric oxide metabolic process; IEA:Ensembl.
GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:BHF-UCL.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
GO; GO:0032741; P:positive regulation of interleukin-18 production; ISS:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IGI:ARUK-UCL.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IDA:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISS:BHF-UCL.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0034123; P:positive regulation of toll-like receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:BHF-UCL.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IEA:InterPro.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome.
GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome.
GO; GO:0032640; P:tumor necrosis factor production; ISS:ARUK-UCL.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027185; TLR2.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR24365:SF17; PTHR24365:SF17; 1.
Pfam; PF13855; LRR_8; 2.
Pfam; PF01463; LRRCT; 1.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 7.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 11.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasmic vesicle; Disulfide bond;
Glycoprotein; Immunity; Inflammatory response; Innate immunity;
Leucine-rich repeat; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 784 Toll-like receptor 2.
/FTId=PRO_0000034710.
TOPO_DOM 21 588 Extracellular. {ECO:0000255}.
TRANSMEM 589 609 Helical. {ECO:0000255}.
TOPO_DOM 610 784 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 525 579 LRRCT.
DOMAIN 639 784 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
MOTIF 761 778 ATG16L1-binding motif.
SITE 349 349 Interaction with bacterial lipopeptide.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15173186,
ECO:0000269|PubMed:17889651}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15173186,
ECO:0000269|PubMed:17889651}.
CARBOHYD 414 414 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17889651}.
CARBOHYD 442 442 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15173186,
ECO:0000269|PubMed:17889651}.
DISULFID 30 36 {ECO:0000269|PubMed:17889651}.
DISULFID 353 382 {ECO:0000269|PubMed:17889651}.
DISULFID 432 454 {ECO:0000269|PubMed:17889651}.
VARIANT 89 89 N -> D (in dbSNP:rs137853176).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066349.
VARIANT 411 411 T -> I (reduces TLR2-mediated NF-kappa-B
activation; dbSNP:rs5743699).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_026765.
VARIANT 571 571 R -> H (in dbSNP:rs61735277).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066350.
VARIANT 579 579 R -> H (in dbSNP:rs5743703).
/FTId=VAR_026766.
VARIANT 631 631 P -> H (reduces TLR2-mediated NF-kappa-B
activation; dbSNP:rs5743704).
{ECO:0000269|PubMed:19924287,
ECO:0000269|PubMed:21618349}.
/FTId=VAR_024663.
VARIANT 636 636 S -> R (in dbSNP:rs137853177).
{ECO:0000269|PubMed:21618349}.
/FTId=VAR_066351.
VARIANT 677 677 R -> W (in dbSNP:rs121917864).
{ECO:0000269|PubMed:11476982,
ECO:0000269|PubMed:12646604}.
/FTId=VAR_031236.
VARIANT 715 715 Y -> N (in dbSNP:rs5743706).
/FTId=VAR_052360.
VARIANT 753 753 R -> Q (reduces TLR2-mediated NF-kappa-B
activation; dbSNP:rs5743708).
{ECO:0000269|PubMed:19924287,
ECO:0000269|PubMed:21618349}.
/FTId=VAR_031237.
MUTAGEN 114 114 N->S: Prevents addition of N-glycans.
Reduces secretion of the N-terminal
ectodomain.
{ECO:0000269|PubMed:15173186}.
MUTAGEN 199 199 N->D: Prevents addition of N-glycans.
Reduces secretion of the N-terminal
ectodomain.
{ECO:0000269|PubMed:15173186}.
MUTAGEN 416 416 T->A: Prevents addition of N-glycans.
Reduces secretion of the N-terminal
ectodomain.
{ECO:0000269|PubMed:15173186}.
MUTAGEN 442 442 N->D: Prevents addition of N-glycans.
Prevents secretion of the N-terminal
ectodomain.
{ECO:0000269|PubMed:15173186}.
MUTAGEN 681 681 P->F: Abolishes the interaction with
MYD88. No effect on oligomerization or on
the structure of the TIR domain.
{ECO:0000269|PubMed:11081518}.
CONFLICT 59 59 L -> Q (in Ref. 8; AAM23001).
{ECO:0000305}.
CONFLICT 68 68 S -> C (in Ref. 8; AAM23001).
{ECO:0000305}.
CONFLICT 726 726 D -> E (in Ref. 2; AAC34133).
{ECO:0000305}.
STRAND 34 37 {ECO:0000244|PDB:2Z80}.
STRAND 56 58 {ECO:0000244|PDB:2Z80}.
TURN 69 74 {ECO:0000244|PDB:2Z80}.
STRAND 80 82 {ECO:0000244|PDB:2Z80}.
TURN 93 98 {ECO:0000244|PDB:2Z80}.
STRAND 104 106 {ECO:0000244|PDB:2Z80}.
HELIX 117 120 {ECO:0000244|PDB:2Z80}.
STRAND 127 130 {ECO:0000244|PDB:2Z80}.
STRAND 137 139 {ECO:0000244|PDB:2Z80}.
STRAND 153 161 {ECO:0000244|PDB:2Z80}.
TURN 167 172 {ECO:0000244|PDB:2Z80}.
STRAND 175 183 {ECO:0000244|PDB:2Z80}.
TURN 191 196 {ECO:0000244|PDB:2Z80}.
STRAND 198 206 {ECO:0000244|PDB:2Z80}.
HELIX 213 220 {ECO:0000244|PDB:2Z80}.
TURN 221 223 {ECO:0000244|PDB:2Z80}.
STRAND 224 231 {ECO:0000244|PDB:2Z80}.
STRAND 253 258 {ECO:0000244|PDB:2Z80}.
STRAND 260 262 {ECO:0000244|PDB:2Z7X}.
HELIX 263 274 {ECO:0000244|PDB:2Z80}.
STRAND 281 283 {ECO:0000244|PDB:2Z80}.
STRAND 288 291 {ECO:0000244|PDB:2Z7X}.
STRAND 311 316 {ECO:0000244|PDB:2Z7X}.
HELIX 322 324 {ECO:0000244|PDB:2Z7X}.
HELIX 329 334 {ECO:0000244|PDB:2Z7X}.
STRAND 340 346 {ECO:0000244|PDB:2Z7X}.
HELIX 353 358 {ECO:0000244|PDB:2Z7X}.
STRAND 364 366 {ECO:0000244|PDB:2Z7X}.
HELIX 374 380 {ECO:0000244|PDB:2Z7X}.
STRAND 391 393 {ECO:0000244|PDB:2Z7X}.
HELIX 402 408 {ECO:0000244|PDB:2Z7X}.
HELIX 409 411 {ECO:0000244|PDB:2Z7X}.
STRAND 417 419 {ECO:0000244|PDB:2Z7X}.
STRAND 440 442 {ECO:0000244|PDB:2Z7X}.
STRAND 460 463 {ECO:0000244|PDB:2Z7X}.
STRAND 481 483 {ECO:0000244|PDB:2Z7X}.
HELIX 495 497 {ECO:0000244|PDB:2Z7X}.
STRAND 503 505 {ECO:0000244|PDB:2Z7X}.
HELIX 518 520 {ECO:0000244|PDB:2Z7X}.
STRAND 527 529 {ECO:0000244|PDB:2Z7X}.
HELIX 539 544 {ECO:0000244|PDB:2Z7X}.
TURN 545 547 {ECO:0000244|PDB:2Z7X}.
STRAND 548 550 {ECO:0000244|PDB:2Z7X}.
STRAND 641 646 {ECO:0000244|PDB:1FYX}.
HELIX 649 651 {ECO:0000244|PDB:1FYX}.
HELIX 652 656 {ECO:0000244|PDB:1FYX}.
HELIX 658 663 {ECO:0000244|PDB:1FYX}.
STRAND 666 668 {ECO:0000244|PDB:1FYX}.
STRAND 672 674 {ECO:0000244|PDB:1FYX}.
HELIX 675 678 {ECO:0000244|PDB:1FYX}.
STRAND 681 683 {ECO:0000244|PDB:1FYX}.
HELIX 685 695 {ECO:0000244|PDB:1FYX}.
STRAND 696 703 {ECO:0000244|PDB:1FYX}.
HELIX 705 711 {ECO:0000244|PDB:1FYX}.
HELIX 713 716 {ECO:0000244|PDB:1FYX}.
TURN 717 719 {ECO:0000244|PDB:1O77}.
HELIX 720 722 {ECO:0000244|PDB:1O77}.
TURN 723 725 {ECO:0000244|PDB:1FYW}.
HELIX 726 728 {ECO:0000244|PDB:1FYX}.
STRAND 733 738 {ECO:0000244|PDB:1FYX}.
TURN 742 744 {ECO:0000244|PDB:1FYX}.
HELIX 750 758 {ECO:0000244|PDB:1FYX}.
STRAND 761 763 {ECO:0000244|PDB:1FYX}.
HELIX 768 770 {ECO:0000244|PDB:1FYX}.
HELIX 771 783 {ECO:0000244|PDB:1FYX}.
SEQUENCE 784 AA; 89838 MW; 7DBE6B24CF1FAF8B CRC64;
MPHTLWMVWV LGVIISLSKE ESSNQASLSC DRNGICKGSS GSLNSIPSGL TEAVKSLDLS
NNRITYISNS DLQRCVNLQA LVLTSNGINT IEEDSFSSLG SLEHLDLSYN YLSNLSSSWF
KPLSSLTFLN LLGNPYKTLG ETSLFSHLTK LQILRVGNMD TFTKIQRKDF AGLTFLEELE
IDASDLQSYE PKSLKSIQNV SHLILHMKQH ILLLEIFVDV TSSVECLELR DTDLDTFHFS
ELSTGETNSL IKKFTFRNVK ITDESLFQVM KLLNQISGLL ELEFDDCTLN GVGNFRASDN
DRVIDPGKVE TLTIRRLHIP RFYLFYDLST LYSLTERVKR ITVENSKVFL VPCLLSQHLK
SLEYLDLSEN LMVEEYLKNS ACEDAWPSLQ TLILRQNHLA SLEKTGETLL TLKNLTNIDI
SKNSFHSMPE TCQWPEKMKY LNLSSTRIHS VTGCIPKTLE ILDVSNNNLN LFSLNLPQLK
ELYISRNKLM TLPDASLLPM LLVLKISRNA ITTFSKEQLD SFHTLKTLEA GGNNFICSCE
FLSFTQEQQA LAKVLIDWPA NYLCDSPSHV RGQQVQDVRL SVSECHRTAL VSGMCCALFL
LILLTGVLCH RFHGLWYMKM MWAWLQAKRK PRKAPSRNIC YDAFVSYSER DAYWVENLMV
QELENFNPPF KLCLHKRDFI PGKWIIDNII DSIEKSHKTV FVLSENFVKS EWCKYELDFS
HFRLFDENND AAILILLEPI EKKAIPQRFC KLRKIMNTKT YLEWPMDEAQ REGFWVNLRA
AIKS


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