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Database: UniProt
Entry: Q6YGU2_RAT
LinkDB: Q6YGU2_RAT
Original site: Q6YGU2_RAT 
ID   Q6YGU2_RAT              Unreviewed;       784 AA.
AC   Q6YGU2; A6J5V7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=Toll-like receptor 2 {ECO:0000256|ARBA:ARBA00017391, ECO:0000256|PIRNR:PIRNR037595};
GN   Name=Tlr2 {ECO:0000313|EMBL:QQJ42674.1, ECO:0000313|RGD:735138};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:QQJ42674.1};
RN   [1] {ECO:0000313|EMBL:AAN86525.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wistar {ECO:0000313|EMBL:AAN86525.1};
RC   TISSUE=Spleen {ECO:0000313|EMBL:AAN86525.1};
RA   Li Y., Ji A., Schafer M.K.;
RT   "Molecular cloning and regulation of toll-like receptor 2 mRNA in rat
RT   spleen.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QQJ42674.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GZRn34 {ECO:0000313|EMBL:QQJ42674.1};
RA   Su Q., Chen Y., He H.;
RL   Submitted (JUL-2020) 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. {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; AY151256; AAN86525.1; -; mRNA.
DR   EMBL; MT730141; QQJ42674.1; -; mRNA.
DR   RefSeq; NP_942064.1; NM_198769.2.
DR   GeneID; 310553; -.
DR   KEGG; rno:310553; -.
DR   UCSC; RGD:735138; rat.
DR   AGR; RGD:735138; -.
DR   CTD; 7097; -.
DR   RGD; 735138; Tlr2.
DR   OrthoDB; 21383at2759; -.
DR   GO; GO:0044297; C:cell body; IDA:RGD.
DR   GO; GO:0042995; C:cell projection; IDA:RGD.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0045121; C:membrane raft; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0043235; C:receptor complex; ISO:RGD.
DR   GO; GO:0035354; C:Toll-like receptor 1-Toll-like receptor 2 protein complex; ISO:RGD.
DR   GO; GO:0035355; C:Toll-like receptor 2-Toll-like receptor 6 protein complex; ISO:RGD.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR   GO; GO:0042498; F:diacyl lipopeptide binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0071723; F:lipopeptide binding; IMP:RGD.
DR   GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR   GO; GO:0070891; F:lipoteichoic acid binding; ISO:RGD.
DR   GO; GO:0038187; F:pattern recognition receptor activity; ISO:RGD.
DR   GO; GO:0042834; F:peptidoglycan binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0035325; F:Toll-like receptor binding; ISO:RGD.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0042497; F:triacyl lipopeptide binding; ISO:RGD.
DR   GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; ISO:RGD.
DR   GO; GO:0071221; P:cellular response to bacterial lipopeptide; ISO:RGD.
DR   GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISO:RGD.
DR   GO; GO:0071223; P:cellular response to lipoteichoic acid; ISO:RGD.
DR   GO; GO:0071224; P:cellular response to peptidoglycan; ISO:RGD.
DR   GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; ISO:RGD.
DR   GO; GO:0071346; P:cellular response to type II interferon; ISO:RGD.
DR   GO; GO:0032289; P:central nervous system myelin formation; IDA:RGD.
DR   GO; GO:0006952; P:defense response; ISO:RGD.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR   GO; GO:0042496; P:detection of diacyl bacterial lipopeptide; ISO:RGD.
DR   GO; GO:0042495; P:detection of triacyl bacterial lipopeptide; ISO:RGD.
DR   GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD.
DR   GO; GO:0006955; P:immune response; NAS:RGD.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0007612; P:learning; ISO:RGD.
DR   GO; GO:0050900; P:leukocyte migration; ISO:RGD.
DR   GO; GO:0006691; P:leukotriene metabolic process; IDA:RGD.
DR   GO; GO:0014005; P:microglia development; ISO:RGD.
DR   GO; GO:0001774; P:microglial cell activation; IDA:RGD.
DR   GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; ISO:RGD.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
DR   GO; GO:0032695; P:negative regulation of interleukin-12 production; ISO:RGD.
DR   GO; GO:0032700; P:negative regulation of interleukin-17 production; ISO:RGD.
DR   GO; GO:0050765; P:negative regulation of phagocytosis; ISO:RGD.
DR   GO; GO:0051964; P:negative regulation of synapse assembly; ISO:RGD.
DR   GO; GO:1990266; P:neutrophil migration; ISO:RGD.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; ISO:RGD.
DR   GO; GO:0046209; P:nitric oxide metabolic process; IDA:RGD.
DR   GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; ISO:RGD.
DR   GO; GO:1903974; P:positive regulation of cellular response to macrophage colony-stimulating factor stimulus; ISO:RGD.
DR   GO; GO:0032722; P:positive regulation of chemokine production; ISO:RGD.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR   GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:RGD.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:RGD.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:RGD.
DR   GO; GO:0032735; P:positive regulation of interleukin-12 production; ISO:RGD.
DR   GO; GO:0032741; P:positive regulation of interleukin-18 production; ISO:RGD.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
DR   GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:RGD.
DR   GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISO:RGD.
DR   GO; GO:1904466; P:positive regulation of matrix metallopeptidase secretion; ISO:RGD.
DR   GO; GO:1902624; P:positive regulation of neutrophil migration; ISO:RGD.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:RGD.
DR   GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:RGD.
DR   GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; ISO:RGD.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IDA:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
DR   GO; GO:1904417; P:positive regulation of xenophagy; ISO:RGD.
DR   GO; GO:0002730; P:regulation of dendritic cell cytokine production; ISO:RGD.
DR   GO; GO:0032493; P:response to bacterial lipoprotein; IDA:RGD.
DR   GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR   GO; GO:0070542; P:response to fatty acid; IDA:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0032868; P:response to insulin; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0002238; P:response to molecule of fungal origin; ISO:RGD.
DR   GO; GO:0032494; P:response to peptidoglycan; ISO:RGD.
DR   GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR   GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR   GO; GO:0034134; P:toll-like receptor 2 signaling pathway; ISO:RGD.
DR   GO; GO:0002224; P:toll-like receptor signaling pathway; IDA:RGD.
DR   GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; ISO:RGD.
DR   GO; GO:0098792; P:xenophagy; ISO:RGD.
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; SM00369; LRR_TYP; 8.
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; 1.
DR   PROSITE; PS50104; TIR; 1.
PE   2: Evidence at transcript level;
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..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..784
FT                   /note="Toll-like receptor 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013533491"
FT   TRANSMEM        589..618
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;  89413 MW;  B2D22A8998EB77F8 CRC64;
     MLQALWLFWI LMAVIGLSRE GHSAQASLSC DAAGVCDGSS RSFTSIPSGL TANTKKLDLS
     FNKITYIGHG DLRACVNLRV LTLESSGINT IEGDAFYSLG SLEHLDLSNN HLSSLSSSWF
     RPLSSLKYLN LMGNPYRTLG ETSLFSNLTN LQTLRVGNVD TFSEIRRIDF AGLTSLNELE
     IQVLSLGNYE SRSLQSIRDI YHLTLHLSES AFLLGIFADI LSSVRYLELR DTNLARFQFS
     ELSVDEINSP MKKLAFRNAD LTDKSFNELL KLLRYILELM EVEFDHCTLN GVGNFNPSES
     DVVRELGKVE TVTIRSLHIP QFYLFYDLST VYSLLEKVKR ITVENSKVFL VPCSFSQHLK
     SLEFLDLSEN LMVEEYLKNS ACEGGWPSLQ SLVLSQNHLR SIRKTAEILL TLKNLTALDI
     SKNSFQPMPD SCQWPGKMRF LNLSSTGIQA VKTCIPQTLE VLDVSNNNLD SFSLFLPRLQ
     ELYISRNKLK TLPEASLFPV LQVMKIRENA ISTFSKDQLG SFPKLETLEA GDNHFICSCE
     LLSFILERPA LVHVLVDWPD SYLCDSPPRL HGQRLQDARP SVLECHQAAL VSGVCCALLL
     LILLLGALCY HFHGLWYLRM MWAWLRAKRK PKKAPCRDLC YDAFVSYSEQ DSYWVENLMV
     QQLENSDPPF KLCLHKRDFV PGKWIIDNII DSIEKSHKTV FVLSENFVRS EWCKYELDFS
     HFRLFDENND AAILVLLEPI EKKAIPQRFC KLRKIMNTKT YLEWPLDEGQ REVFWANLRT
     AIKS
//
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