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Toll-like receptor 2 (CD antigen CD282)

 TLR2_CAPHI              Reviewed;         784 AA.
Q0GC71;
10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 1.
05-JUL-2017, entry version 69.
RecName: Full=Toll-like receptor 2;
AltName: CD_antigen=CD282;
Flags: Precursor;
Name=TLR2;
Capra hircus (Goat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Capra.
NCBI_TaxID=9925;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Das D.K., Saini M., Dhara A., Swarup D., Sharma B., Gupta P.K.;
"Full-length cDNA cloning and characterization of Toll-like receptor 2
(TLR2) from goat (Capra hiscus).";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
-!- 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 (By similarity). May also
promote apoptosis in response to lipoproteins. 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 (By similarity).
{ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}.
-!- SUBUNIT: Interacts with LY96, TLR1 and TLR6 (via extracellular
domain). 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. Binds MYD88 (via TIR domain). Interacts with
TICAM1 (By similarity). Interacts with CNPY3 (By similarity).
Interacts with ATG16L1 (By similarity).
{ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}.
-!- 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:0000250|UniProtKB:O60603}. 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 determine the intracellular
targeting to the Golgi apparatus. Triacylated lipoproteins induce
the same mechanism for TLR2:TLR1 heterodimers.
{ECO:0000250|UniProtKB:O60603}.
-!- 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:0000250}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DQ872435; ABI31733.1; -; mRNA.
RefSeq; NP_001272532.1; NM_001285603.1.
UniGene; Chi.13427; -.
ProteinModelPortal; Q0GC71; -.
SMR; Q0GC71; -.
GeneID; 100860747; -.
KEGG; chx:100860747; -.
CTD; 7097; -.
HOVERGEN; HBG108574; -.
KO; K10159; -.
OrthoDB; EOG091G05L8; -.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
GO; GO:0050707; P:regulation of cytokine secretion; IEA:InterPro.
GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IEA:InterPro.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027185; TLR2.
PANTHER; PTHR24365:SF487; PTHR24365:SF487; 1.
Pfam; PF13855; LRR_8; 2.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 6.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 10.
PROSITE; PS50104; TIR; 1.
2: Evidence at transcript level;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Leucine-rich repeat; Membrane;
Receptor; Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 784 Toll-like receptor 2.
/FTId=PRO_0000363775.
TOPO_DOM 21 587 Extracellular. {ECO:0000255}.
TRANSMEM 588 608 Helical. {ECO:0000255}.
TOPO_DOM 609 784 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.
{ECO:0000250}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 248 248 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 442 442 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 36 {ECO:0000250}.
DISULFID 353 382 {ECO:0000250}.
DISULFID 432 454 {ECO:0000250}.
SEQUENCE 784 AA; 90067 MW; C3434B760BB92E6A CRC64;
MPRALWTAWV WAVIILSMEG ASHQASSLSC DPTGVCDGHS RSLNSIPSGL TDGVKSLDLS
NNEITYVSNR DLQRCVNLKT LRLGANEIHT VEEDSFFHLR NLEYLDLSYN RLSNLSSSWF
RSLYALKFLN LLGNVYKTLG ETSLFSHLPN LRTLKVGNSN SFTEIHEKDF TGLIFLEELE
ISAQNLQIYV PKSLKSIQNI SHLILHLKQP VLLVDILVDI VSSLDCLELR DTNLHTFHFS
EASISEMNTS VKKLIFRNVQ FTDESFVEVV KLFNYVSGIL EVEFDDCTHD GIGDFRALSL
DRIRHLGNVE TLTIRKLHIP QFFLFHDLSS IYPLTGKVKR VTIESSKVFL VPCLLSQHLK
SLEYLDLSEN LMSEETLKNS ACKDAWPFLQ TLVLRQNRLK SLEKTGELLL TLKNLNNLDI
SKNNFLSMPE TCQWPGKMKQ LNLSSTRIHS LTQCLPQTLE ILDVSNNNLD SFSLILPQLK
ELYISRNKLK TLPDASFLPV LSVMRISGNI INTFSKEQLD SFPQLKALEA GGNNFICSCD
FLSFTQGQQA LARVLVDWPD GYRCDAPSHV RGQRVQDARL SLSECHRAAV VSAVCCALFL
LLLLTGVLCH RFHGLWYMKM MWAWLQAKRK PRKAPRRDLC YDAFVSYSEQ DSYWVENLMV
QELEHFNPPF KLCLHKRDFV PGKWIIDNII DSIEKSRKTI FVLSENFVRS EWCKYELDFS
HFRLFDENND AAILILLEPI DKKAIPQRFC KLRKIMNTKT YLEWPTDETQ QEAFWLNLRA
AIRS


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