ID G9BH51_BOVIN Unreviewed; 784 AA.
AC G9BH51;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Toll-like receptor 2 {ECO:0000256|ARBA:ARBA00017391, ECO:0000256|PIRNR:PIRNR037595};
GN Name=TLR2 {ECO:0000313|EMBL:ADW79406.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:ADW79406.1};
RN [1] {ECO:0000313|EMBL:ADW79406.1}
RP NUCLEOTIDE SEQUENCE.
RA Liu M.;
RT "Association of Toll-like Receptor 2 Polymorphisms with Somatic Cell Score
RT in Xinjiang Brown Cattle.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). May also promote apoptosis in
CC response to lipoproteins. Forms activation clusters composed of several
CC receptors depending on the ligand, these clusters trigger signaling
CC from the cell surface and subsequently are targeted to the Golgi in a
CC lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in
CC response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to
CC triacylated lipopeptides. {ECO:0000256|ARBA:ARBA00025293}.
CC -!- SUBUNIT: Interacts with LY96, TLR1 and TLR6 (via extracellular domain).
CC TLR2 seems to exist in heterodimers with either TLR1 or TLR6 before
CC stimulation by the ligand. The heterodimers form bigger oligomers in
CC response to their corresponding ligands as well as further heterotypic
CC associations with other receptors such as CD14 and/or CD36. Binds MYD88
CC (via TIR domain). Interacts with TICAM1. Interacts with CNPY3.
CC Interacts with ATG16L1. Interacts with PPP1R11. Interacts with TICAM2.
CC Interacts with TIRAP. {ECO:0000256|ARBA:ARBA00038692}.
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}.
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DR EMBL; HQ540579; ADW79406.1; -; mRNA.
DR AlphaFoldDB; G9BH51; -.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-UniRule.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-UniRule.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:UniProtKB-UniRule.
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; 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; SM00365; LRR_SD22; 6.
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 2: Evidence at transcript 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 Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR037595};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..784
FT /note="Toll-like receptor 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003520076"
FT TRANSMEM 588..609
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; 90113 MW; CC944D52536F2121 CRC64;
MPRALWTAWV WAVIILSTEG ASDQASSLSC DPTGVCDGHS RSLNSIPSGL AAGVKSLDLS
NNEITYVSNR DLQRCVNLKT LRLGANEIHT VEEDSFFHLR NLEYLDLSYN RLSNLSSSWF
RSLYVLKFLN LLGNLYKTLG ETSLFSHLPN LRTLKVGNSN SFTEIHEKDF TGLTFLEELE
ISAQNLQIYV PKSLKSIQNI SHLILHLKQP VLLVDILVDI VSSLDCFELR DTNLHTFHFS
EASISEMSTS VKKLIFRNVQ FTDESFVEVV KLFNYVSGIL EVEFDDCTHD GIGDFRALSL
DRIRHLGNVE TLTIRKLHIP QFFLFQDLSS IYPLTGKVKR VTIENSKVFL VPCLLSQHLK
SLEYLDLSEN LMSEETLKNS ACKDAWPFLQ TLVLRQNRLK SLEKTGELLL TLENLNSLDI
SKNNFLSMPE TCQWPGKMKQ LNLSSTRIHS LTQCLPQTLE ILDVSNNNLD SFSLILPQLK
ELYISRNKLK TLPDASFLPV LSVMRISRNI INTFSKEQLD SFQQLKTLEA GGNNFICSCD
FLSFTQGQQA LGRVLVDWPD DYHCDSPSHV RGQRVQDARL SLSECHRAAV VSAACCALFL
LLLLTGVLCH RFHGLWYMKM MWAWLQAKRK PRKAPRRDIC YDAFVSYSER DSYWVENLMV
QELEQFNPPF KLCLHKRDFI PGKWIIDNII DSIEKSHKTI FVLSENFVKS EWCKYELDFS
HFRLFDENND AAILILLEPI DKKAIPQRFC KLRKIMNTKT YLEWPVDETQ QEGFWLNLRA
AIRS
//
