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-MAY-2013, entry version 29.
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 -!- 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).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein (By similarity).
CC -!- DOMAIN: Ester-bound lipid substrates are bound through a crevice
CC formed between the LRR 11 and LRR 12 (By similarity).
CC -!- DOMAIN: The ATG16L1-binding motif mediates interaction with
CC ATG16L1 (By similarity).
CC -!- SIMILARITY: Belongs to the Toll-like receptor family.
CC -!- SIMILARITY: Contains 19 LRR (leucine-rich) repeats.
CC -!- SIMILARITY: Contains 1 LRRCT domain.
CC -!- SIMILARITY: Contains 1 TIR domain.
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DR EMBL; AB445627; BAG55024.1; -; mRNA.
DR ProteinModelPortal; B3Y615; -.
DR HOVERGEN; HBG108574; -.
DR GO; GO:0016021; C:integral to 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 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; 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; TIR; 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 Potential.
FT CHAIN 21 784 Toll-like receptor 2.
FT /FTId=PRO_0000363774.
FT TOPO_DOM 21 587 Extracellular (Potential).
FT TRANSMEM 588 608 Helical; (Potential).
FT TOPO_DOM 609 784 Cytoplasmic (Potential).
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.
FT MOTIF 761 778 ATG16L1-binding motif.
FT SITE 349 349 Interaction with bacterial lipopeptide
FT (By similarity).
FT CARBOHYD 114 114 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 199 199 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 414 414 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 442 442 N-linked (GlcNAc...) (Potential).
FT DISULFID 30 36 By similarity.
FT DISULFID 353 382 By similarity.
FT DISULFID 432 454 By similarity.
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
//
