TLR2_BOSTR
ID TLR2_BOSTR Reviewed; 784 AA.
AC Q2V897;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Toll-like receptor 2;
DE AltName: CD_antigen=CD282;
DE Flags: Precursor;
GN Name=TLR2;
OS Boselaphus tragocamelus (Nilgai).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Boselaphus.
OX NCBI_TaxID=9917;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Das D.K., Saini M., Swarup D., Yadav M.P., Sharma B., Gupta P.K.;
RT "Full-length cDNA cloning of toll-like receptor 2 in Boselaphus
RT tragocamelus.";
RL Submitted (NOV-2005) 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 (By similarity). May also promote apoptosis in
CC response to lipoproteins. Forms activation clusters composed of several
CC receptors depending on the ligand, these clusters trigger signaling
CC from the cell surface and subsequently are targeted to the Golgi in a
CC lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in
CC response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to
CC triacylated lipopeptides (By similarity).
CC {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}.
CC -!- SUBUNIT: Interacts with LY96, TLR1 and TLR6 (via extracellular domain).
CC TLR2 seems to exist in heterodimers with either TLR1 or TLR6 before
CC stimulation by the ligand. The heterodimers form bigger oligomers in
CC response to their corresponding ligands as well as further heterotypic
CC associations with other receptors such as CD14 and/or CD36. Binds MYD88
CC (via TIR domain). Interacts with TICAM1. Interacts with CNPY3.
CC Interacts with ATG16L1. Interacts with PPP1R11. Interacts with TICAM2.
CC {ECO:0000250|UniProtKB:O60603, ECO:0000250|UniProtKB:Q9QUN7}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-
CC pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle,
CC phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I
CC membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts
CC before stimulation but accumulates increasingly in the raft upon the
CC presence of the microbial ligand. In response to diacylated
CC lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this
CC recruitment determine the intracellular targeting to the Golgi
CC apparatus. Triacylated lipoproteins induce the same mechanism for
CC TLR2:TLR1 heterodimers. {ECO:0000250|UniProtKB:O60603}.
CC -!- DOMAIN: Ester-bound lipid substrates are bound through a crevice formed
CC between the LRR 11 and LRR 12. {ECO:0000250}.
CC -!- DOMAIN: The ATG16L1-binding motif mediates interaction with ATG16L1.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation.
CC Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.
CC -!- PTM: Glycosylation of Asn-442 is critical for secretion of the N-
CC terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
CC -!- CAUTION: In some plant proteins and in human SARM1, the TIR domain has
CC NAD(+) hydrolase (NADase) activity (By similarity). However, despite
CC the presence of the catalytic Asp residue, the isolated TIR domain of
CC human TLR4 lacks NADase activity (By similarity). Based on this, it is
CC unlikely that Toll-like receptors have NADase activity.
CC {ECO:0000250|UniProtKB:O00206, ECO:0000305}.
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DR EMBL; DQ286731; ABB97025.1; -; mRNA.
DR AlphaFoldDB; Q2V897; -.
DR SMR; Q2V897; -.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0071726; P:cellular response to diacyl bacterial lipopeptide; ISS:UniProtKB.
DR GO; GO:0071727; P:cellular response to triacyl bacterial lipopeptide; ISS:UniProtKB.
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:0001817; P:regulation of cytokine production; IEA:InterPro.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IEA:InterPro.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 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; IPR027185; TLR2.
DR InterPro; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
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; 6.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 10.
DR PROSITE; PS50104; TIR; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Immunity;
KW Inflammatory response; Innate immunity; Isopeptide bond;
KW Leucine-rich repeat; Membrane; NAD; Receptor; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..784
FT /note="Toll-like receptor 2"
FT /id="PRO_0000253494"
FT TOPO_DOM 21..587
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 54..77
FT /note="LRR 1"
FT REPEAT 78..101
FT /note="LRR 2"
FT REPEAT 102..125
FT /note="LRR 3"
FT REPEAT 126..150
FT /note="LRR 4"
FT REPEAT 151..175
FT /note="LRR 5"
FT REPEAT 176..199
FT /note="LRR 6"
FT REPEAT 200..223
FT /note="LRR 7"
FT REPEAT 224..250
FT /note="LRR 8"
FT REPEAT 251..278
FT /note="LRR 9"
FT REPEAT 279..308
FT /note="LRR 10"
FT REPEAT 309..337
FT /note="LRR 11"
FT REPEAT 338..361
FT /note="LRR 12"
FT REPEAT 362..388
FT /note="LRR 13"
FT REPEAT 389..414
FT /note="LRR 14"
FT REPEAT 415..437
FT /note="LRR 15"
FT REPEAT 438..457
FT /note="LRR 16"
FT REPEAT 458..478
FT /note="LRR 17"
FT REPEAT 479..500
FT /note="LRR 18"
FT REPEAT 501..524
FT /note="LRR 19"
FT DOMAIN 525..579
FT /note="LRRCT"
FT DOMAIN 639..782
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT MOTIF 761..778
FT /note="ATG16L1-binding motif"
FT SITE 349
FT /note="Interaction with bacterial lipopeptide"
FT /evidence="ECO:0000250"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..36
FT /evidence="ECO:0000250"
FT DISULFID 353..382
FT /evidence="ECO:0000250"
FT DISULFID 432..454
FT /evidence="ECO:0000250"
FT CROSSLNK 754
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O60603"
SQ SEQUENCE 784 AA; 90115 MW; C98ABDDF465E4DF0 CRC64;
MPRALWPAWV WAIIILSMEG ASDKASSLSC DPTGVCDGRS RSLNSIPSGL TAGVKSLDLS
NNEITYVGNR DLQRCVNLKT LRLGANEIHT VEEDSFFHLR NLEYLDLSYN RLSNLSSSWF
RSLYVLKFLN LLGNLYKTLG ETSLFSHLPD LRTLKVGNSN SFTEIHEKDF TGLTFLEELE
ISAQNLQIYV PKSLKSIQNI SHLILHLKQP VLLVDILVDI VSSLDCLELR DTNLHTFHFS
EASISEMSTS VKKLIFRNVQ FTDESFVEVV KLFNYVSGIV EVEFDDCTHD GIGDFRALSL
DRIRHLGNVE TLTIRKLHIP QFFLFQDLSS IYPLTGKVKR VTIENSKVFL VPCLLSQHLK
SLEYLDLSEN LMSEETLKNS ACKDAWPFLQ TLVLRQNRLK SLEKTGELLL TLKNLNNLDI
SKNNFLSMPE TCQWPGKMKQ LNLSSTKIRS LTQCLPQTLE ILDVSNNNLD SFSLILPQLK
ELYISRNKLK TLPDASFLPV LSVMGISKNI INTFSKEQLD SFQQLKTLEA GGNNFICSCD
FLSFTQGQQA LGRVLVDWPD DYRCDSPSHV RGQRLQDARL SLSECHRAAV VSAACCALFL
FLLLTGVLCH RFHGLWYMKI MWAWLQAKRK PRKAPRRDIC YDAFVSYSER DSYWVENLMV
QELEHFNPPF KLCLHKRDFI PGKWIIDNII DSIEKSHKTI FVLSENFVKS EWCKYELDFS
HFRLFDENND AVILILLEPI DKKAIPQRFC KLRKIMNTKT YLEWPLDETQ QEGFWLNLRA
AIRS
