ID TLR22_CHICK Reviewed; 781 AA.
AC Q9DGB6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=Toll-like receptor 2 type-2;
DE Flags: Precursor;
GN Name=TLR2-2;
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).
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. Mediates the response
CC to mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2).
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. Also detected in brain,
CC heart, lung, liver, spleen and kidney, and at low levels in gizzard,
CC muscle, testis and proventriculus.
CC -!- PTM: N-glycosylated.
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; AB046533; BAB16842.1; -; mRNA.
DR RefSeq; NP_001155122.1; NM_001161650.1.
DR AlphaFoldDB; Q9DGB6; -.
DR SMR; Q9DGB6; -.
DR STRING; 9031.ENSGALP00000038134; -.
DR GlyCosmos; Q9DGB6; 8 sites, No reported glycans.
DR PaxDb; 9031-ENSGALP00000038134; -.
DR Ensembl; ENSGALT00010035770.1; ENSGALP00010020743.1; ENSGALG00010014865.1.
DR Ensembl; ENSGALT00010035774.1; ENSGALP00010020745.1; ENSGALG00010014865.1.
DR Ensembl; ENSGALT00010035778.1; ENSGALP00010020746.1; ENSGALG00010014865.1.
DR Ensembl; ENSGALT00010035781.1; ENSGALP00010020748.1; ENSGALG00010014865.1.
DR Ensembl; ENSGALT00010035786.1; ENSGALP00010020751.1; ENSGALG00010014865.1.
DR GeneID; 769014; -.
DR KEGG; gga:769014; -.
DR CTD; 7097; -.
DR VEuPathDB; HostDB:geneid_769014; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000156323; -.
DR InParanoid; Q9DGB6; -.
DR OMA; FRNCTIV; -.
DR OrthoDB; 21383at2759; -.
DR PhylomeDB; Q9DGB6; -.
DR PRO; PR:Q9DGB6; -.
DR Proteomes; UP000000539; Chromosome 4.
DR GO; GO:0016020; C: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: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:0042494; P:detection of bacterial lipoprotein; NAS:Roslin.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
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; 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; 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; 3.
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; 4.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR PROSITE; PS51450; LRR; 11.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..781
FT /note="Toll-like receptor 2 type-2"
FT /id="PRO_0000034714"
FT TOPO_DOM 25..585
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..781
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 53..74
FT /note="LRR 1"
FT REPEAT 77..98
FT /note="LRR 2"
FT REPEAT 101..122
FT /note="LRR 3"
FT REPEAT 125..146
FT /note="LRR 4"
FT REPEAT 150..171
FT /note="LRR 5"
FT REPEAT 174..195
FT /note="LRR 6"
FT REPEAT 358..378
FT /note="LRR 7"
FT REPEAT 385..406
FT /note="LRR 8"
FT REPEAT 411..432
FT /note="LRR 9"
FT REPEAT 434..455
FT /note="LRR 10"
FT REPEAT 456..474
FT /note="LRR 11"
FT REPEAT 475..496
FT /note="LRR 12"
FT REPEAT 497..518
FT /note="LRR 13"
FT DOMAIN 530..584
FT /note="LRRCT"
FT DOMAIN 636..779
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..36
FT /evidence="ECO:0000250"
FT DISULFID 350..379
FT /evidence="ECO:0000250"
FT DISULFID 429..451
FT /evidence="ECO:0000250"
SQ SEQUENCE 781 AA; 89095 MW; 7211B399C6320454 CRC64;
MHTWKMWAIC TALAAHLPEE QALRQACLSC DATQSCNCSF MGLDFIPPGL TGKITVLNLA
HNRIKVIRTH DLQKAVNLRT LLLQSNQISS IDEDSFGSQG KLELLDLSNN SLAHLSPVWF
GPLFSLQHLR IQGNSYSDLG ESSPFSSLRN LSSLHLGNPQ FSIIRQGNFE GIVFLNTLRI
DGDNLSQYEP GSLKSIRKIN HMIISIRRID VFSAVIRDLL HSAIWLDVRK LAFSVPEKIQ
LLRIMSSSFA KKISLKQCLF TDATVPEIVS ILEGMPKLME VEMKDCTLLG TGKWYKQIHA
NQSQSLRILT IENLSIEEFY LFTDLQSVLD LLSLFRKVTV ENTKVFLVPC KLSQHLLSLE
YLDLSANLLG DQSLEHSACQ GAWPSLQTLN LSQNSLSDLK MTGKSLFHLR NLNLLDISEN
NFGEIPDMCE WPENLKYLNL SSTQIPKLTT CIPSTLEVLD VSANNLQDFG LQLPFLKELY
LTKNHLKTLP EATDIPNLVA MSISRNKLNS FSKEEFESFK QMELLDASAN NFICSCEFLS
FIHHEAGIAQ VLVGWPESYI CDSPLTVRGA QVGSVQLSLM ECHRSLLVSL ICTLVFLFIL
ILVVVGYKYH AVWYMRMTWA WLQAKRKPKR APTKDICYDA FVSYSENDSN WVENIMVQQL
EQACPPFRLC LHKRDFVPGK WIVDNIIDSI EKSHKTLFVL SEHFVQSEWC KYELDFSHFR
LFDENNDVAI LILLEPIQSQ AIPKRFCKLR KIMNTKTYLE WPPDEEQQQM FWENLKAALK
S
//
