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Database: UniProt
Entry: B3Y615
LinkDB: B3Y615
Original site: B3Y615 
ID   TLR2_GORGO              Reviewed;         784 AA.
AC   B3Y615;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   01-OCT-2014, entry version 38.
DE   RecName: Full=Toll-like receptor 2;
DE   AltName: CD_antigen=CD282;
DE   Flags: Precursor;
GN   Name=TLR2;
OS   Gorilla gorilla gorilla (Lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T.,
RA   Kimura A.;
RT   "Molecular evolution of the Toll-like receptor-related genes in
RT   primates.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cooperates with LY96 to mediate the innate immune
CC       response to bacterial lipoproteins and other microbial cell wall
CC       components. Cooperates with TLR1 or TLR6 to mediate the innate
CC       immune response to bacterial lipoproteins or lipopeptides. Acts
CC       via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine
CC       secretion and the inflammatory response. May also promote
CC       apoptosis in response to lipoproteins (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with LY96, TLR1 and TLR6 (via extracellular
CC       domain). Binds MYD88 (via TIR domain). Interacts with TICAM1.
CC       Ligand binding induces the formation of a heterodimer with TLR1 or
CC       TLR6. Interacts with CNPY3. Interacts with ATG16L1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: Ester-bound lipid substrates are bound through a crevice
CC       formed between the LRR 11 and LRR 12. {ECO:0000250}.
CC   -!- DOMAIN: The ATG16L1-binding motif mediates interaction with
CC       ATG16L1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Toll-like receptor family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 19 LRR (leucine-rich) repeats. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 LRRCT domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 TIR domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00204}.
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DR   EMBL; AB445627; BAG55024.1; -; mRNA.
DR   RefSeq; NP_001266693.1; NM_001279764.1.
DR   ProteinModelPortal; B3Y615; -.
DR   GeneID; 101128447; -.
DR   CTD; 7097; -.
DR   HOVERGEN; HBG108574; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
DR   GO; GO:0050707; P:regulation of cytokine secretion; IEA:InterPro.
DR   GO; GO:0002237; P:response to molecule of bacterial origin; IEA:InterPro.
DR   GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IEA:InterPro.
DR   Gene3D; 3.40.50.10140; -; 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; IPR000157; TIR_dom.
DR   InterPro; IPR027185; TLR2.
DR   InterPro; IPR017241; Toll-like_receptor.
DR   PANTHER; PTHR24365:SF17; PTHR24365:SF17; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF01582; TIR; 1.
DR   PIRSF; PIRSF037595; Toll-like_receptor; 1.
DR   SMART; SM00369; LRR_TYP; 2.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF52200; SSF52200; 1.
DR   PROSITE; PS51450; LRR; 11.
DR   PROSITE; PS50104; TIR; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; Glycoprotein; Immunity;
KW   Inflammatory response; Innate immunity; Leucine-rich repeat; Membrane;
KW   Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    784       Toll-like receptor 2.
FT                                /FTId=PRO_0000363774.
FT   TOPO_DOM     21    587       Extracellular. {ECO:0000255}.
FT   TRANSMEM    588    608       Helical. {ECO:0000255}.
FT   TOPO_DOM    609    784       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       54     77       LRR 1.
FT   REPEAT       78    101       LRR 2.
FT   REPEAT      102    125       LRR 3.
FT   REPEAT      126    150       LRR 4.
FT   REPEAT      151    175       LRR 5.
FT   REPEAT      176    199       LRR 6.
FT   REPEAT      200    223       LRR 7.
FT   REPEAT      224    250       LRR 8.
FT   REPEAT      251    278       LRR 9.
FT   REPEAT      279    308       LRR 10.
FT   REPEAT      309    337       LRR 11.
FT   REPEAT      338    361       LRR 12.
FT   REPEAT      362    388       LRR 13.
FT   REPEAT      389    414       LRR 14.
FT   REPEAT      415    437       LRR 15.
FT   REPEAT      438    457       LRR 16.
FT   REPEAT      458    478       LRR 17.
FT   REPEAT      479    500       LRR 18.
FT   REPEAT      501    524       LRR 19.
FT   DOMAIN      525    579       LRRCT.
FT   DOMAIN      639    784       TIR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00204}.
FT   MOTIF       761    778       ATG16L1-binding motif.
FT   SITE        349    349       Interaction with bacterial lipopeptide.
FT                                {ECO:0000250}.
FT   CARBOHYD    114    114       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    199    199       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    414    414       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    442    442       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     30     36       {ECO:0000250}.
FT   DISULFID    353    382       {ECO:0000250}.
FT   DISULFID    432    454       {ECO:0000250}.
SQ   SEQUENCE   784 AA;  89824 MW;  1465031E6825069C CRC64;
     MPHTLWMVWV LGVIISLSKE ESSNQASLSC DRNGICKGSS GSLNSIPSGL TEAVKSLDLS
     NNRITYISNS DLQRCVNLQA LVLTSNGINT IEEDSFSSLG SLEHLDLSYN YLSNLSSSWF
     KPLSSLTFLN LLGNPYKTLG ETSLFSHLTK LQILRVGNMD TFTKIQRKDF AGLTFLEELE
     IDASDLQSYE PKSLKSIQNV SHLILHMKQH ILLLEIFVDV TSSVECLELR DTDLDTFHFS
     ELSTGETNSL IKKFTFRNVK ITDESLFQVM KLLNQISGLL ELEFDDCTLN GVGNFRASDN
     DRVIDPGKVE TLTIRRLHIP RFYLFYDLST LYSLTERVKR ITVENSKVFL VPCLLSQHLK
     SLEYLDLSEN LMVEEYLKNS ACEDAWPSLQ TLILRQNHLA SLEKTGETLL TLKNLTNVDI
     SKNSFHSMPE TCQWPEKMKY LNLSSTRIHS VTGCIPKTLE ILDVSNNNLN LFSLNLPQLK
     ELYISRNKLM TLPDASLLPM LLVLKISRNA ITTFSKEQLD SFHTLKTLEA GGNNFICSCE
     FLSFTQEQQA LAKVLIDWPA NYLCDSPSHV RGQQVQDVRL SVSECHRTAL VSGMCCALFL
     LILLTGVLCH RFHGLWYMKM MWAWLQAKRK PRKAPSRNIC YDAFVSYSER DAYWVENLMV
     QELENFNPPF KLCLHKRDFI PGKWIIDNII DSIEKSHKTV FVLSENFVKS EWCKYELDFS
     HFRLFDENND AAILILLEPI EKKAIPQRFC KLRKIMNTKT YLEWPMDEAQ REGFWVNLRA
     AIKS
//
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