ID L5L252_PTEAL Unreviewed; 566 AA.
AC L5L252;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Toll-like receptor 2 {ECO:0000256|ARBA:ARBA00017391};
GN ORFNames=PAL_GLEAN10016583 {ECO:0000313|EMBL:ELK17490.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK17490.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 -!- 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}.
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DR EMBL; KB030405; ELK17490.1; -; Genomic_DNA.
DR AlphaFoldDB; L5L252; -.
DR STRING; 9402.L5L252; -.
DR eggNOG; KOG4641; Eukaryota.
DR InParanoid; L5L252; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:InterPro.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01537; INTRLKN1R1F.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS50104; TIR; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:ELK17490.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..566
FT /note="Toll-like receptor 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003969796"
FT TRANSMEM 371..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 421..564
FT /note="TIR"
FT /evidence="ECO:0000259|PROSITE:PS50104"
SQ SEQUENCE 566 AA; 65070 MW; 377FA980DDD4B588 CRC64;
MPRVLWTVWV LGAAISLLEK GALDQASSVN CDSTGVCDGH SKSLNFIPSG LPATVKSLDL
SNNKITYVSS SDLRACVNLQ ALRLGSNRIN AIQEDSFLSL GSLEHLDLSY NHLNNLSSSW
FRPLSSLKFL NLLGNPYKTL GKTSLFSHLT NLRILKVGNN YFTEIREKDF AGLTFLQELE
IDASNLQRYE PKSLKSIQNV SCLILHIKQP VFLQKIFVDI LSSLEYLELI DTHLNTFHFS
EVSINKTNTL IKKFTFRNVE ITDEGFNELV KLLPYASEAL DVEFEDCTLN GIGDFDISEQ
LDSFKKLKTL EAGGNNFICS CEFLRFTQEQ QALAQILIDW PGNYLCDSPS HVRGHRVQDT
HLSISECHRT ALVSALCCAL FLFILLTVVL CHHFHGLWYM KMMWAWLQAK RKPKKAPHRD
ICYDAFVSYS ERDSHWVENL MVQELEHFDP PFKLCLHKRD FVPGKWIIDN IIDSIEKSHK
TVFVLSENFV KSEWCKYELD FSHFRLFDEN NDAAILILLE PIEKKTIPQR FCKLRKMMNT
KTYLEWPTDE AQQEGFWLNL RTAIKS
//
