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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.
26-FEB-2020, entry version 215.
RecName: Full=Toll-like receptor 2;
EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
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
(MICROBIAL INFECTION).
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 STAPHYLOCOCCUS AUREUS SUPERANTIGEN-LIKE PROTEIN 3
(MICROBIAL INFECTION).
PubMed=22665377; DOI=10.1128/iai.00399-12;
Yokoyama R., Itoh S., Kamoshida G., Takii T., Fujii S., Tsuji T.,
Onozaki K.;
"Staphylococcal superantigen-like protein 3 binds to the Toll-like receptor
2 extracellular domain and inhibits cytokine production induced by
Staphylococcus aureus, cell wall component, or lipopeptides in murine
macrophages.";
Infect. Immun. 80:2816-2825(2012).
[21]
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).
[22]
INTERACTION WITH TICAM2.
PubMed=25385819; DOI=10.4049/jimmunol.1401605;
Stack J., Doyle S.L., Connolly D.J., Reinert L.S., O'Keeffe K.M.,
McLoughlin R.M., Paludan S.R., Bowie A.G.;
"TRAM is required for TLR2 endosomal signaling to type I IFN induction.";
J. Immunol. 193:6090-6102(2014).
[23]
UBIQUITINATION AT LYS-754, AND MUTAGENESIS OF LYS-709; LYS-714;
742-LYS--LYS-743; LYS-751 AND LYS-754.
PubMed=27805901; DOI=10.7554/elife.18496;
McKelvey A.C., Lear T.B., Dunn S.R., Evankovich J., Londino J.D.,
Bednash J.S., Zhang Y., McVerry B.J., Liu Y., Chen B.B.;
"RING finger E3 ligase PPP1R11 regulates TLR2 signaling and innate
immunity.";
Elife 5:0-0(2016).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
-!- 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). Interacts with PPP1R11 (By similarity).
Interacts with TICAM2 (PubMed:25385819). {ECO:0000250|UniProtKB:Q9QUN7,
ECO:0000269|PubMed:12471095, ECO:0000269|PubMed:16880211,
ECO:0000269|PubMed:17889651, ECO:0000269|PubMed:23376921,
ECO:0000269|PubMed:25385819}.
-!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis EsxA.
{ECO:0000269|PubMed:20800577}.
-!- SUBUNIT: (Microbial infection) Interacts with M.bovis MPB83.
{ECO:0000269|PubMed:20800577}.
-!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
protein SSL5. {ECO:0000269|PubMed:22665377}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-973722, EBI-973722;
P61073:CXCR4; NbExp=3; IntAct=EBI-973722, EBI-489411;
P00533:EGFR; NbExp=2; IntAct=EBI-973722, EBI-297353;
Q99836:MYD88; NbExp=4; IntAct=EBI-973722, EBI-447677;
C3PTT6:PAUF; NbExp=3; IntAct=EBI-973722, EBI-3505892;
Q15399:TLR1; NbExp=3; IntAct=EBI-973722, EBI-9009517;
Q9BXR5:TLR10; NbExp=3; IntAct=EBI-973722, EBI-16825459;
Q9Y2C9:TLR6; NbExp=4; IntAct=EBI-973722, EBI-13940779;
-!- 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}.
-!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
Self-association of TIR domains is required for NADase activity.
{ECO:0000255|PROSITE-ProRule:PRU00204}.
-!- PTM: Glycosylation of Asn-442 is critical for secretion of the N-
terminal ectodomain of TLR2. {ECO:0000269|PubMed:15173186,
ECO:0000269|PubMed:17889651}.
-!- PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation
(PubMed:27805901). Deubiquitinated by USP2 (By similarity).
{ECO:0000250|UniProtKB:Q9QUN7, ECO:0000269|PubMed:27805901}.
-!- 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.
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.
PDB; 6NIG; X-ray; 2.35 A; A/B/C/D=1-507.
PDBsum; 1FYW; -.
PDBsum; 1FYX; -.
PDBsum; 1O77; -.
PDBsum; 2Z7X; -.
PDBsum; 2Z80; -.
PDBsum; 6NIG; -.
SMR; O60603; -.
BioGrid; 112952; 28.
CORUM; O60603; -.
DIP; DIP-35138N; -.
IntAct; O60603; 38.
MINT; O60603; -.
STRING; 9606.ENSP00000260010; -.
BindingDB; O60603; -.
ChEMBL; CHEMBL4163; -.
DrugBank; DB05475; Golotimod.
DrugBank; DB00045; Lyme disease vaccine (recombinant OspA).
DrugBank; DB03963; S-(Dimethylarsenic)Cysteine.
DrugBank; DB11601; Tuberculin Purified Protein Derivative.
GuidetoPHARMACOLOGY; 1752; -.
GlyConnect; 1816; -.
iPTMnet; O60603; -.
PhosphoSitePlus; O60603; -.
SwissPalm; O60603; -.
BioMuta; TLR2; -.
EPD; O60603; -.
jPOST; O60603; -.
MassIVE; O60603; -.
PaxDb; O60603; -.
PeptideAtlas; O60603; -.
PRIDE; O60603; -.
ProteomicsDB; 49481; -.
ABCD; O60603; -.
DNASU; 7097; -.
Ensembl; ENST00000260010; ENSP00000260010; ENSG00000137462.
Ensembl; ENST00000642580; ENSP00000495339; ENSG00000137462.
Ensembl; ENST00000642700; ENSP00000494425; ENSG00000137462.
GeneID; 7097; -.
KEGG; hsa:7097; -.
UCSC; uc063aif.1; human.
CTD; 7097; -.
DisGeNET; 7097; -.
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; ENSGT00940000156323; -.
HOGENOM; CLU_006000_3_0_1; -.
InParanoid; O60603; -.
KO; K10159; -.
OMA; DSYWVEN; -.
OrthoDB; 282372at2759; -.
PhylomeDB; O60603; -.
TreeFam; TF351113; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1461957; Beta defensins.
Reactome; R-HSA-166058; MyD88:MAL(TIRAP) 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; -.
Pharos; O60603; Tchem.
PRO; PR:O60603; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; O60603; protein.
Bgee; ENSG00000137462; Expressed in blood and 157 other tissues.
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; IDA:ARUK-UCL.
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:0001540; F:amyloid-beta binding; IDA:ARUK-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
GO; GO:0001875; F:lipopolysaccharide immune receptor activity; TAS:UniProtKB.
GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB.
GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
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:0071346; P:cellular response to interferon-gamma; 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; IBA:GO_Central.
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 population 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:1903974; P:positive regulation of cellular response to macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
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; IGI:ARUK-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:2000778; P:positive regulation of interleukin-6 secretion; IGI:ARUK-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:1904466; P:positive regulation of matrix metallopeptidase secretion; IGI:ARUK-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:BHF-UCL.
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 by RNA polymerase II; 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; IBA:GO_Central.
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; -; 1.
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; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 11.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
Immunity; Inflammatory response; Innate immunity; Isopeptide bond;
Leucine-rich repeat; Membrane; NAD; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
Ubl conjugation.
SIGNAL 1..20
/evidence="ECO:0000255"
CHAIN 21..784
/note="Toll-like receptor 2"
/id="PRO_0000034710"
TOPO_DOM 21..588
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 589..609
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 610..784
/note="Cytoplasmic"
/evidence="ECO:0000255"
REPEAT 54..77
/note="LRR 1"
REPEAT 78..101
/note="LRR 2"
REPEAT 102..125
/note="LRR 3"
REPEAT 126..150
/note="LRR 4"
REPEAT 151..175
/note="LRR 5"
REPEAT 176..199
/note="LRR 6"
REPEAT 200..223
/note="LRR 7"
REPEAT 224..250
/note="LRR 8"
REPEAT 251..278
/note="LRR 9"
REPEAT 279..308
/note="LRR 10"
REPEAT 309..337
/note="LRR 11"
REPEAT 338..361
/note="LRR 12"
REPEAT 362..388
/note="LRR 13"
REPEAT 389..414
/note="LRR 14"
REPEAT 415..437
/note="LRR 15"
REPEAT 438..457
/note="LRR 16"
REPEAT 458..478
/note="LRR 17"
REPEAT 479..500
/note="LRR 18"
REPEAT 501..524
/note="LRR 19"
DOMAIN 525..579
/note="LRRCT"
DOMAIN 639..782
/note="TIR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
MOTIF 761..778
/note="ATG16L1-binding motif"
ACT_SITE 716
/evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SITE 349
/note="Interaction with bacterial lipopeptide"
CARBOHYD 114
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15173186,
ECO:0000269|PubMed:17889651"
CARBOHYD 199
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15173186,
ECO:0000269|PubMed:17889651"
CARBOHYD 414
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:17889651"
CARBOHYD 442
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:15173186,
ECO:0000269|PubMed:17889651"
DISULFID 30..36
/evidence="ECO:0000269|PubMed:17889651"
DISULFID 353..382
/evidence="ECO:0000269|PubMed:17889651"
DISULFID 432..454
/evidence="ECO:0000269|PubMed:17889651"
CROSSLNK 754
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:27805901"
VARIANT 89
/note="N -> D (in dbSNP:rs137853176)"
/evidence="ECO:0000269|PubMed:21618349"
/id="VAR_066349"
VARIANT 411
/note="T -> I (reduces TLR2-mediated NF-kappa-B activation;
dbSNP:rs5743699)"
/evidence="ECO:0000269|PubMed:21618349"
/id="VAR_026765"
VARIANT 571
/note="R -> H (in dbSNP:rs61735277)"
/evidence="ECO:0000269|PubMed:21618349"
/id="VAR_066350"
VARIANT 579
/note="R -> H (in dbSNP:rs5743703)"
/id="VAR_026766"
VARIANT 631
/note="P -> H (reduces TLR2-mediated NF-kappa-B activation;
dbSNP:rs5743704)"
/evidence="ECO:0000269|PubMed:19924287,
ECO:0000269|PubMed:21618349"
/id="VAR_024663"
VARIANT 636
/note="S -> R (in dbSNP:rs137853177)"
/evidence="ECO:0000269|PubMed:21618349"
/id="VAR_066351"
VARIANT 677
/note="R -> W (in dbSNP:rs121917864)"
/evidence="ECO:0000269|PubMed:11476982,
ECO:0000269|PubMed:12646604"
/id="VAR_031236"
VARIANT 715
/note="Y -> N (in dbSNP:rs5743706)"
/id="VAR_052360"
VARIANT 753
/note="R -> Q (reduces TLR2-mediated NF-kappa-B activation;
dbSNP:rs5743708)"
/evidence="ECO:0000269|PubMed:19924287,
ECO:0000269|PubMed:21618349"
/id="VAR_031237"
MUTAGEN 114
/note="N->S: Prevents addition of N-glycans. Reduces
secretion of the N-terminal ectodomain."
/evidence="ECO:0000269|PubMed:15173186"
MUTAGEN 199
/note="N->D: Prevents addition of N-glycans. Reduces
secretion of the N-terminal ectodomain."
/evidence="ECO:0000269|PubMed:15173186"
MUTAGEN 416
/note="T->A: Prevents addition of N-glycans. Reduces
secretion of the N-terminal ectodomain."
/evidence="ECO:0000269|PubMed:15173186"
MUTAGEN 442
/note="N->D: Prevents addition of N-glycans. Prevents
secretion of the N-terminal ectodomain."
/evidence="ECO:0000269|PubMed:15173186"
MUTAGEN 681
/note="P->F: Abolishes the interaction with MYD88. No
effect on oligomerization or on the structure of the TIR
domain."
/evidence="ECO:0000269|PubMed:11081518"
MUTAGEN 709
/note="K->R: Reduced protein stability."
/evidence="ECO:0000269|PubMed:27805901"
MUTAGEN 714
/note="K->R: Reduced protein stability."
/evidence="ECO:0000269|PubMed:27805901"
MUTAGEN 742..743
/note="KK->RR: Reduced protein stability."
/evidence="ECO:0000269|PubMed:27805901"
MUTAGEN 751
/note="K->R: Reduced protein stability."
/evidence="ECO:0000269|PubMed:27805901"
MUTAGEN 754
/note="K->R: Loss of PPP1R11-mediated ubiquitination and
degradation."
/evidence="ECO:0000269|PubMed:27805901"
CONFLICT 59
/note="L -> Q (in Ref. 8; AAM23001)"
/evidence="ECO:0000305"
CONFLICT 68
/note="S -> C (in Ref. 8; AAM23001)"
/evidence="ECO:0000305"
CONFLICT 726
/note="D -> E (in Ref. 2; AAC34133)"
/evidence="ECO:0000305"
STRAND 34..37
/evidence="ECO:0000244|PDB:2Z80"
STRAND 56..58
/evidence="ECO:0000244|PDB:2Z80"
TURN 69..74
/evidence="ECO:0000244|PDB:2Z80"
STRAND 80..82
/evidence="ECO:0000244|PDB:2Z80"
TURN 93..98
/evidence="ECO:0000244|PDB:2Z80"
STRAND 104..106
/evidence="ECO:0000244|PDB:2Z80"
HELIX 117..120
/evidence="ECO:0000244|PDB:2Z80"
STRAND 127..130
/evidence="ECO:0000244|PDB:2Z80"
STRAND 137..139
/evidence="ECO:0000244|PDB:2Z80"
STRAND 153..161
/evidence="ECO:0000244|PDB:2Z80"
TURN 167..172
/evidence="ECO:0000244|PDB:2Z80"
STRAND 175..183
/evidence="ECO:0000244|PDB:2Z80"
TURN 191..196
/evidence="ECO:0000244|PDB:2Z80"
STRAND 198..206
/evidence="ECO:0000244|PDB:2Z80"
STRAND 208..210
/evidence="ECO:0000244|PDB:6NIG"
HELIX 213..220
/evidence="ECO:0000244|PDB:2Z80"
TURN 221..223
/evidence="ECO:0000244|PDB:2Z80"
STRAND 224..231
/evidence="ECO:0000244|PDB:2Z80"
STRAND 253..258
/evidence="ECO:0000244|PDB:2Z80"
STRAND 260..262
/evidence="ECO:0000244|PDB:2Z7X"
HELIX 263..274
/evidence="ECO:0000244|PDB:2Z80"
STRAND 281..283
/evidence="ECO:0000244|PDB:2Z80"
STRAND 288..291
/evidence="ECO:0000244|PDB:2Z7X"
TURN 300..302
/evidence="ECO:0000244|PDB:6NIG"
STRAND 311..316
/evidence="ECO:0000244|PDB:2Z7X"
HELIX 322..324
/evidence="ECO:0000244|PDB:2Z7X"
HELIX 329..334
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 340..346
/evidence="ECO:0000244|PDB:2Z7X"
HELIX 353..358
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 364..366
/evidence="ECO:0000244|PDB:2Z7X"
HELIX 374..380
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 391..393
/evidence="ECO:0000244|PDB:2Z7X"
HELIX 402..408
/evidence="ECO:0000244|PDB:2Z7X"
HELIX 409..411
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 417..419
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 440..442
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 460..463
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 481..483
/evidence="ECO:0000244|PDB:2Z7X"
HELIX 495..497
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 503..505
/evidence="ECO:0000244|PDB:2Z7X"
HELIX 518..520
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 527..529
/evidence="ECO:0000244|PDB:2Z7X"
HELIX 539..544
/evidence="ECO:0000244|PDB:2Z7X"
TURN 545..547
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 548..550
/evidence="ECO:0000244|PDB:2Z7X"
STRAND 641..646
/evidence="ECO:0000244|PDB:1FYX"
HELIX 649..651
/evidence="ECO:0000244|PDB:1FYX"
HELIX 652..656
/evidence="ECO:0000244|PDB:1FYX"
HELIX 658..663
/evidence="ECO:0000244|PDB:1FYX"
STRAND 666..668
/evidence="ECO:0000244|PDB:1FYX"
STRAND 672..674
/evidence="ECO:0000244|PDB:1FYX"
HELIX 675..678
/evidence="ECO:0000244|PDB:1FYX"
STRAND 681..683
/evidence="ECO:0000244|PDB:1FYX"
HELIX 685..695
/evidence="ECO:0000244|PDB:1FYX"
STRAND 696..703
/evidence="ECO:0000244|PDB:1FYX"
HELIX 705..711
/evidence="ECO:0000244|PDB:1FYX"
HELIX 713..716
/evidence="ECO:0000244|PDB:1FYX"
TURN 717..719
/evidence="ECO:0000244|PDB:1O77"
HELIX 720..722
/evidence="ECO:0000244|PDB:1O77"
TURN 723..725
/evidence="ECO:0000244|PDB:1FYW"
HELIX 726..728
/evidence="ECO:0000244|PDB:1FYX"
STRAND 733..738
/evidence="ECO:0000244|PDB:1FYX"
TURN 742..744
/evidence="ECO:0000244|PDB:1FYX"
HELIX 750..758
/evidence="ECO:0000244|PDB:1FYX"
STRAND 761..763
/evidence="ECO:0000244|PDB:1FYX"
HELIX 768..770
/evidence="ECO:0000244|PDB:1FYX"
HELIX 771..783
/evidence="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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20-321-175143 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.1 mg
20-321-175146 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.1 mg
15-288-22787 Toll-like receptor 2 - Toll_interleukin 1 receptor-like protein 4; CD282 antigen Polyclonal 0.1 mg
15-288-22787 Toll-like receptor 2 - Toll_interleukin 1 receptor-like protein 4; CD282 antigen Polyclonal 0.05 mg
18-661-15147 Toll-like receptor 2 - Toll_interleukin 1 receptor-like protein 4; CD282 antigen Polyclonal 0.1 mg
20-321-175062 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - FITC CONJUGATED MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) Monoclonal 0.1 mg
20-321-175058 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - BIOTINYLATED MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) Monoclonal 0.05 mg
20-321-175063 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - BIOTINYLATED MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) Monoclonal 0.05 mg
20-321-175079 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - BIOTINYLATED MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) Monoclonal 0.05 mg
20-321-175061 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) Monoclonal 0.1 mg
20-321-175050 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) Monoclonal 0.1 mg
20-321-175056 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) Monoclonal 0.1 mg
20-321-175078 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) Monoclonal 0.1 mg
LF-PA41656 anti-Toll-interleukin 1 Receptor, Rabbit polyclonal to Toll-interleukin 1 Receptor, Isotype IgG, Host Rabbit 100 ul
20-321-175057 FITC CONJUGATED TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - FITC CONJUGATED MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) Monoclonal 0.1 mg
20-321-175164 TOLL-LIKE RECEPTOR 1 (TLR1. CD281) - FITC CONJUGATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 1 (TLR1. CD281); Toll_interleukin-1 receptor-like protein; TIL; CD281 antigen Monoclonal 0.1 mg
20-321-175165 TOLL-LIKE RECEPTOR 1 (TLR1. CD281) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 1 (TLR1. CD281); Toll_interleukin-1 receptor-like protein; TIL; CD281 antigen Monoclonal 0.05 mg
20-321-175163 TOLL-LIKE RECEPTOR 1 (TLR1. CD281) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 1 (TLR1. CD281); Toll_interleukin-1 receptor-like protein; TIL; CD281 antigen Monoclonal 0.1 mg
20-321-175051 MONOCLONAL ANTIBODY TOMOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - BIOTINYLATED MONOCLONAL ANTIBODY TOMOUSE TOLL-LIKE RECEPTOR 2 (TLR2. CD282) Monoclonal 0.05 mg
GWB-8796A3 TOLL-LIKE RECEPTOR 2 (TLR2. CD282), Antibody
GWB-756CDD TOLL-LIKE RECEPTOR 2 (TLR2. CD282), Antibody
Pathways :
WP2272: Pathogenic Escherichia coli infection
WP1183: Toll-like receptor signaling pathway
WP1309: Toll-like receptor signaling pathway
WP829: Toll-like receptor signaling pathway
WP1384: Toll-like receptor signaling pathway
WP1449: Regulation of toll-like receptor signaling pathway
WP88: Toll Like Receptor signaling
WP949: Toll-like receptor signaling pathway
WP1271: Toll-like receptor signaling pathway
WP1067: Toll-like receptor signaling pathway
WP75: Toll-like receptor signaling pathway
WP2328: Allograft rejection
WP2292: Chemokine signaling pathway
WP780: T Cell Receptor Signaling Pathway
WP474: Endochondral Ossification
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1004: Kit Receptor Signaling Pathway
WP1025: B Cell Receptor Signaling Pathway
WP147: Kit Receptor Signaling Pathway
WP252: Androgen Receptor Signaling Pathway
WP809: TGF-beta Receptor Signaling Pathway
WP1249: EPO Receptor Signaling
WP566: canonical wnt - zebrafish
WP2197: Endothelin
WP590: Cardiovascular Signaling

Related Genes :
[TLR2 TIL4] Toll-like receptor 2 (EC 3.2.2.6) (Toll/interleukin-1 receptor-like protein 4) (CD antigen CD282)
[Tlr2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[TLR2] Toll-like receptor 2 (EC 3.2.2.6) (CD antigen CD282)
[Tlr1] Toll-like receptor 1 (EC 3.2.2.6) (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)
[TLR1 KIAA0012] Toll-like receptor 1 (EC 3.2.2.6) (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281)
[TICAM2 TIRAP3 TIRP TRAM] TIR domain-containing adapter molecule 2 (TICAM-2) (Putative NF-kappa-B-activating protein 502) (TRIF-related adapter molecule) (Toll-like receptor adaptor protein 3) (Toll/interleukin-1 receptor domain-containing protein) (MyD88-4)
[TLR4] Toll-like receptor 4 (EC 3.2.2.6) (hToll) (CD antigen CD284)
[Tlr4] Toll-like receptor 4 (Toll4) (EC 3.2.2.6) (CD antigen CD284)
[TLR5 TIL3] Toll-like receptor 5 (Toll/interleukin-1 receptor-like protein 3)
[Tlr4 Lps] Toll-like receptor 4 (EC 3.2.2.6) (CD antigen CD284)
[TLR4] Toll-like receptor 4 (EC 3.2.2.6) (CD antigen CD284)
[Ticam2 Tirp Tram] TIR domain-containing adapter molecule 2 (TICAM-2) (TRIF-related adapter molecule) (Toll/interleukin-1 receptor domain-containing protein)
[TIRAP MAL] Toll/interleukin-1 receptor domain-containing adapter protein (TIR domain-containing adapter protein) (Adaptor protein Wyatt) (MyD88 adapter-like protein) (MyD88-2)
[TLR6] Toll-like receptor 6 (EC 3.2.2.6) (CD antigen CD286)

Bibliography :