ID E0ZNJ3_CHINI Unreviewed; 783 AA.
AC E0ZNJ3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Toll-like receptor 2 {ECO:0000256|ARBA:ARBA00017391, ECO:0000256|PIRNR:PIRNR037595};
GN Name=TLR2 {ECO:0000313|EMBL:ADM52306.1};
OS Chionomys nivalis (European snow vole) (Microtus nivalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Arvicolinae; Chionomys.
OX NCBI_TaxID=269649 {ECO:0000313|EMBL:ADM52306.1};
RN [1] {ECO:0000313|EMBL:ADM52306.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21418116; DOI=10.1111/j.1420-9101.2011.02254.x;
RA Tschirren B., Raberg L., Westerdahl H.;
RT "Signatures of selection acting on the innate immunity gene Toll-like
RT receptor 2 (TLR2) during the evolutionary history of rodents.";
RL J. Evol. Biol. 24:1232-1240(2011).
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. {ECO:0000256|PIRNR:PIRNR037595}.
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; HM215595; ADM52306.1; -; Genomic_DNA.
DR GO; GO:0016020; C: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:0001819; P:positive regulation of cytokine production; IEA:UniProt.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; IEA:UniProt.
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; IPR026906; LRR_5.
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; PF13306; LRR_5; 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; 4.
DR SMART; SM00369; LRR_TYP; 6.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..783
FT /note="Toll-like receptor 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003143410"
FT TRANSMEM 588..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 638..781
FT /note="TIR"
FT /evidence="ECO:0000259|PROSITE:PS50104"
SQ SEQUENCE 783 AA; 89633 MW; 48A284485B7A03BF CRC64;
MLRVLWTLWI LVAMKDLQRE GCSAQAPLSC DAGVCDGRSR SFTSIPSGLS TAMKSLDLSN
NKITSIGHGD LRGCVNLRAL MLQSXRINRI EEGAFSSLRS LEHLDLSDNQ LSDLSFXWFR
PLSSLKYLNL LGNRYRILGE TSLFYNLTNL QTLRVGNIDT FSGIRRIDFA GLTSLDELEI
KALSLQTYDS QSLKSIQNIH HLTLHLSQSD FLLAIFADIL SSVGYLELRD IGVASFRFSE
LSADEINSPM KKLAFRNADL TDESFNELLK LLRYIPELLE VEFDDCTLDG VGDFQPSESD
IMRELGKVET LIIRRLQIPR FYSVSDLSAV YHLLEKVKHI TVENSKVFLV PCAFSKRLKS
LEFLDLSENL MVEEYLRNSA CEDAWPSLQT LILRQNYLKS LERTGEILLT LKNLTALDIS
RNSFRPMPAT CQWPPKMLFL NLSSTGIQAV KTCIPQTLEV LDVSNNNLNS FSLFLPRLRE
LYISRNKLKT LPDASLFPVL LVMKIRENAI NTFSKDQLSS FPKLVTLEAG DNHFVCSCEF
LSFTLGQPAL SQVLPDWPDS YLCDSPXRLR GQKVQEARPS VLECHQALLV SGVCCALLLL
ILLIGGLCHH FHGLWYLRMM WAWLRAKRKP KKAPCRDICY DVFVSYSEQD SYWVENLMVQ
QLENSDPPFK LCLHKRDFVP GKWIIDNIID SIEKSHKTVF VLSENFVRSE WCKYELDFSH
FRLFDENNDA CILVLLEPIE KKAIPQRFCK LRKIMNTKTY LEWPLDEAQX EVFWANLRTA
IKS
//