TLR21_CHICK
ID TLR21_CHICK Reviewed; 793 AA.
AC Q9DD78;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Toll-like receptor 2 type-1;
DE Flags: Precursor;
GN Name=TLR2-1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=11590137; DOI=10.1074/jbc.m103902200;
RA Fukui A., Inoue N., Matsumoto M., Nomura M., Yamada K., Matsuda Y.,
RA Toyoshima K., Seya T.;
RT "Molecular cloning and functional characterization of chicken Toll-like
RT receptors. A single chicken Toll covers multiple molecular patterns.";
RL J. Biol. Chem. 276:47143-47149(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Takahashi T.;
RT "Molecular cloning and expression analysis of the chick Toll-like receptor
RT 2 in embryonic ventricular myocytes.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in the innate immune response to microbial
CC agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation,
CC cytokine secretion and the inflammatory response (By similarity). Does
CC not respond to LPS and responds with less ability than TLR2-2 to
CC mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds MYD88 (via TIR domain). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in ovary. Detected at lower levels
CC in heart, lung, gizzard and testis.
CC -!- PTM: N-glycosylated. TLR2-1 is more heavily glycosylated than TLR2-2.
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; AB050005; BAB16843.1; -; mRNA.
DR EMBL; AB046119; BAB16113.2; -; mRNA.
DR RefSeq; NP_989609.1; NM_204278.1.
DR AlphaFoldDB; Q9DD78; -.
DR SMR; Q9DD78; -.
DR STRING; 9031.ENSGALP00000015018; -.
DR PaxDb; Q9DD78; -.
DR Ensembl; ENSGALT00000077237; ENSGALP00000045282; ENSGALG00000034722.
DR GeneID; 374141; -.
DR KEGG; gga:374141; -.
DR CTD; 101792125; -.
DR VEuPathDB; HostDB:geneid_374141; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000156323; -.
DR InParanoid; Q9DD78; -.
DR OrthoDB; 282372at2759; -.
DR PhylomeDB; Q9DD78; -.
DR TreeFam; TF351113; -.
DR Reactome; R-GGA-433822; NFkB and MAPK activation mediated by TRAF6.
DR Reactome; R-GGA-451514; MyD88:TIRAP-dependent cascade initiated on plasma membrane.
DR Reactome; R-GGA-517856; TLR2 subfamily cascade.
DR PRO; PR:Q9DD78; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000034722; Expressed in granulocyte and 13 other tissues.
DR ExpressionAtlas; Q9DD78; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0042497; F:triacyl lipopeptide binding; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
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:0002237; P:response to molecule of bacterial origin; IEA:InterPro.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IEA:InterPro.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; 3.
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 Disulfide bond; Glycoprotein; Immunity; Inflammatory response;
KW Innate immunity; Leucine-rich repeat; Membrane; NAD; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..793
FT /note="Toll-like receptor 2 type-1"
FT /id="PRO_0000034713"
FT TOPO_DOM 26..597
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 619..793
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 64..85
FT /note="LRR 1"
FT REPEAT 88..109
FT /note="LRR 2"
FT REPEAT 112..133
FT /note="LRR 3"
FT REPEAT 136..157
FT /note="LRR 4"
FT REPEAT 161..182
FT /note="LRR 5"
FT REPEAT 185..206
FT /note="LRR 6"
FT REPEAT 370..391
FT /note="LRR 7"
FT REPEAT 397..418
FT /note="LRR 8"
FT REPEAT 423..444
FT /note="LRR 9"
FT REPEAT 446..467
FT /note="LRR 10"
FT REPEAT 468..486
FT /note="LRR 11"
FT REPEAT 487..508
FT /note="LRR 12"
FT REPEAT 509..530
FT /note="LRR 13"
FT DOMAIN 542..596
FT /note="LRRCT"
FT DOMAIN 648..791
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..47
FT /evidence="ECO:0000250"
FT DISULFID 362..391
FT /evidence="ECO:0000250"
FT DISULFID 441..463
FT /evidence="ECO:0000250"
SQ SEQUENCE 793 AA; 90767 MW; 2BF659D9305D4562 CRC64;
MFNQSKQKPT MKLMWQAWLI YTALAAHLPE EQALRQACLS CDATQSCNCS FMGLDFIPPG
LTGKITVLNL AHNRIKLIRT HDLQKAVNLR TLLLQSNQIS SIDEDSFGSQ GKLELLDLSN
NSLAHLSPVW FGPLFSLQHL RIQGNSYSDL GESSPFSSLR NLSSLHLGNP QFSIIRQGNF
EGIVFLNTLR IDGDNLSQYE PGSLKSIRKI NHMIISIRRI DVFSAVIRDL LHSAIWLEVR
EIKLDIENEK LVQNSTLPLT IQKLTFTGAS FTDKYISQIA VLLKEIRSLR ELEAIDCVLE
GKGAWDMTEI ARSKQSSIET LSITNMTILD FYLFFDLEGI ETQVGKLKRL SIASSKVFMV
PCRLARYFSS LLYLDFHDNL LVNNRLGETI CEDAWPSLQT LNLSKNSLKS LKQAARYISN
LHKLINLDIS ENNFGEIPDM CEWPENLKYL NLSSTQIPKL TTCIPSTLEV LDVSANNLQD
FGLQLPFLKE LYLTKNHLKT LPEATDIPNL VAMSISRNKL NSFSKEEFES FKQMELLDAS
ANNFICSCEF LSFIHHEAGI AQVLVGWPES YICDSPLTVR GAQVGSVQLS LMECHRSLLV
SLICTLVFLF ILILVVVGYK YHAVWYMRMT WAWLQAKRKP KRAPTKDICY DAFVSYSEND
SNWVENIMVQ QLEQACPPFR LCLHKRDFVP GKWIVDNIID SIEKSHKTLF VLSEHFVQSE
WCKYELDFSH FRLFDENNDV AILILLEPIQ SQAIPKRFCK LRKIMNTKTY LEWPPDEEQQ
QMFWENLKAA LKS
