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Database: UniProt
Entry: E0ZNJ3_CHINI
LinkDB: E0ZNJ3_CHINI
Original site: E0ZNJ3_CHINI 
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
//
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