Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Toll-like receptor 8 (CD antigen CD288)

 TLR8_HUMAN              Reviewed;        1041 AA.
Q9NR97; B3Y654; D1CS70; D1CS76; Q495P4; Q6UXL6; Q9NYG9;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
28-MAR-2018, entry version 165.
RecName: Full=Toll-like receptor 8;
AltName: CD_antigen=CD288;
Flags: Precursor;
Name=TLR8; ORFNames=UNQ249/PRO286;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=11022119;
Du X., Poltorak A., Wei Y., Beutler B.;
"Three novel mammalian Toll-like receptors: gene structure,
expression, and evolution.";
Eur. Cytokine Netw. 11:362-371(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=11022120;
Chuang T.-H., Ulevitch R.J.;
"Cloning and characterization of a sub-family of human Toll-like
receptors: hTLR7, hTLR8 and hTLR9.";
Eur. Cytokine Netw. 11:372-378(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T.,
Kimura A.;
"Natural selection in the TLR-related genes in the course of primate
evolution.";
Immunogenetics 60:727-735(2008).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=19924287; DOI=10.1371/journal.pone.0007803;
Georgel P., Macquin C., Bahram S.;
"The heterogeneous allelic repertoire of human Toll-Like receptor
(TLR) genes.";
PLoS ONE 4:E7803-E7803(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, AND INTERACTION WITH BTK.
PubMed=17932028; DOI=10.1074/jbc.M707682200;
Doyle S.L., Jefferies C.A., Feighery C., O'Neill L.A.;
"Signaling by Toll-like receptors 8 and 9 requires Bruton's tyrosine
kinase.";
J. Biol. Chem. 282:36953-36960(2007).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-88.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 27-827 IN COMPLEXES WITH
RESIQUIMOD AND OTHER SYNTHETIC AGONISTS, FUNCTION, SUBUNIT,
LEUCINE-RICH REPEATS, MUTAGENESIS OF TYR-348; VAL-378; PHE-405;
VAL-520; ASP-543 AND THR-574, GLYCOSYLATION AT ASN-293; ASN-395;
ASN-511; ASN-546; ASN-590; ASN-640 AND ASN-680, AND DISULFIDE BONDS.
PubMed=23520111; DOI=10.1126/science.1229159;
Tanji H., Ohto U., Shibata T., Miyake K., Shimizu T.;
"Structural reorganization of the Toll-like receptor 8 dimer induced
by agonistic ligands.";
Science 339:1426-1429(2013).
-!- FUNCTION: Key component of innate and adaptive immunity. TLRs
(Toll-like receptors) control host immune response against
pathogens through recognition of molecular patterns specific to
microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B
activation, cytokine secretion and the inflammatory response.
{ECO:0000269|PubMed:17932028, ECO:0000269|PubMed:23520111}.
-!- SUBUNIT: Interacts with MYD88 via their respective TIR domains.
Interacts with UNC93B1 (By similarity). Homodimer. Interacts with
BTK. Interacts with SMPDL3B (By similarity).
{ECO:0000250|UniProtKB:P58682, ECO:0000269|PubMed:17932028,
ECO:0000269|PubMed:23520111}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NR97-1; Sequence=Displayed;
Name=2;
IsoId=Q9NR97-2; Sequence=VSP_053412;
-!- TISSUE SPECIFICITY: Detected in brain, heart, lung, liver,
placenta, in monocytes, and at lower levels in CD11c+ immature
dendritic cells.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF246971; AAF64061.1; -; mRNA.
EMBL; AF245703; AAF78036.1; -; mRNA.
EMBL; AB445666; BAG55063.1; -; mRNA.
EMBL; DQ023132; AAZ95433.1; -; Genomic_DNA.
EMBL; DQ023133; AAZ95434.1; -; Genomic_DNA.
EMBL; DQ023134; AAZ95435.1; -; Genomic_DNA.
EMBL; DQ023135; AAZ95436.1; -; Genomic_DNA.
EMBL; DQ023136; AAZ95437.1; -; Genomic_DNA.
EMBL; DQ023137; AAZ95438.1; -; Genomic_DNA.
EMBL; DQ023138; AAZ95439.1; -; Genomic_DNA.
EMBL; DQ023139; AAZ95440.1; -; Genomic_DNA.
EMBL; DQ023140; AAZ95441.1; -; Genomic_DNA.
EMBL; CH471074; EAW98808.1; -; Genomic_DNA.
EMBL; AY358296; AAQ88663.1; -; mRNA.
EMBL; AC005859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC139705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471074; EAW98809.1; -; Genomic_DNA.
EMBL; BC101076; AAI01077.1; -; mRNA.
EMBL; BC101077; AAI01078.1; -; mRNA.
CCDS; CCDS14152.1; -. [Q9NR97-1]
CCDS; CCDS14153.1; -. [Q9NR97-2]
RefSeq; NP_057694.2; NM_016610.3. [Q9NR97-2]
RefSeq; NP_619542.1; NM_138636.5. [Q9NR97-1]
RefSeq; XP_011543831.1; XM_011545529.1. [Q9NR97-2]
RefSeq; XP_011543832.1; XM_011545530.2. [Q9NR97-2]
UniGene; Hs.660543; -.
PDB; 3W3G; X-ray; 2.30 A; A/B=27-827.
PDB; 3W3J; X-ray; 2.00 A; A/B=27-827.
PDB; 3W3K; X-ray; 2.30 A; A/B=27-827.
PDB; 3W3L; X-ray; 2.33 A; A/B/C/D=27-827.
PDB; 3W3M; X-ray; 2.70 A; A=27-827.
PDB; 3W3N; X-ray; 2.10 A; A/B=27-827.
PDB; 3WN4; X-ray; 1.81 A; A=27-827.
PDB; 4QBZ; X-ray; 2.00 A; A/B=27-827.
PDB; 4QC0; X-ray; 2.10 A; A/B=27-827.
PDB; 4R07; X-ray; 2.00 A; A/B/C/D=27-827.
PDB; 4R08; X-ray; 2.40 A; A/B/C/D=27-827.
PDB; 4R09; X-ray; 2.62 A; A/B/C/D=27-827.
PDB; 4R0A; X-ray; 1.90 A; A=27-827.
PDB; 4R6A; X-ray; 2.10 A; A/B=27-827.
PDB; 5AWA; X-ray; 2.20 A; A=27-827.
PDB; 5AWB; X-ray; 2.10 A; A=27-827.
PDB; 5AWC; X-ray; 2.50 A; A/B/C/D=27-827.
PDB; 5AWD; X-ray; 2.05 A; A=27-827.
PDB; 5AZ5; X-ray; 2.40 A; A/B/C/D=27-827.
PDB; 5HDH; X-ray; 2.60 A; A=27-827.
PDB; 5WYX; X-ray; 2.40 A; A/B=27-827.
PDB; 5WYZ; X-ray; 2.30 A; A/B=27-827.
PDBsum; 3W3G; -.
PDBsum; 3W3J; -.
PDBsum; 3W3K; -.
PDBsum; 3W3L; -.
PDBsum; 3W3M; -.
PDBsum; 3W3N; -.
PDBsum; 3WN4; -.
PDBsum; 4QBZ; -.
PDBsum; 4QC0; -.
PDBsum; 4R07; -.
PDBsum; 4R08; -.
PDBsum; 4R09; -.
PDBsum; 4R0A; -.
PDBsum; 4R6A; -.
PDBsum; 5AWA; -.
PDBsum; 5AWB; -.
PDBsum; 5AWC; -.
PDBsum; 5AWD; -.
PDBsum; 5AZ5; -.
PDBsum; 5HDH; -.
PDBsum; 5WYX; -.
PDBsum; 5WYZ; -.
ProteinModelPortal; Q9NR97; -.
SMR; Q9NR97; -.
BioGrid; 119462; 1.
DIP; DIP-61413N; -.
IntAct; Q9NR97; 1.
STRING; 9606.ENSP00000218032; -.
BindingDB; Q9NR97; -.
ChEMBL; CHEMBL5805; -.
DrugBank; DB00724; Imiquimod.
GuidetoPHARMACOLOGY; 1758; -.
iPTMnet; Q9NR97; -.
PhosphoSitePlus; Q9NR97; -.
BioMuta; TLR8; -.
DMDM; 20140873; -.
PaxDb; Q9NR97; -.
PeptideAtlas; Q9NR97; -.
PRIDE; Q9NR97; -.
Ensembl; ENST00000218032; ENSP00000218032; ENSG00000101916. [Q9NR97-1]
Ensembl; ENST00000311912; ENSP00000312082; ENSG00000101916. [Q9NR97-2]
GeneID; 51311; -.
KEGG; hsa:51311; -.
UCSC; uc004cvd.4; human. [Q9NR97-1]
CTD; 51311; -.
DisGeNET; 51311; -.
EuPathDB; HostDB:ENSG00000101916.11; -.
GeneCards; TLR8; -.
H-InvDB; HIX0176772; -.
HGNC; HGNC:15632; TLR8.
HPA; HPA001608; -.
MIM; 300366; gene.
neXtProt; NX_Q9NR97; -.
OpenTargets; ENSG00000101916; -.
PharmGKB; PA38009; -.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000230468; -.
HOVERGEN; HBG018601; -.
InParanoid; Q9NR97; -.
KO; K10170; -.
OMA; WPDNPKA; -.
OrthoDB; EOG091G014D; -.
PhylomeDB; Q9NR97; -.
TreeFam; TF351113; -.
Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-HSA-168181; Toll Like Receptor 7/8 (TLR7/8) Cascade.
Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-HSA-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
Reactome; R-HSA-975155; MyD88 dependent cascade initiated on endosome.
GeneWiki; TLR8; -.
GenomeRNAi; 51311; -.
PRO; PR:Q9NR97; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000101916; -.
CleanEx; HS_TLR8; -.
Genevisible; Q9NR97; HS.
GO; GO:0036020; C:endolysosome membrane; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IDA:CAFA.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004872; F:receptor activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; TAS:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0016064; P:immunoglobulin mediated immune response; TAS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
GO; GO:2001183; P:negative regulation of interleukin-12 secretion; IDA:CAFA.
GO; GO:0045089; P:positive regulation of innate immune response; IDA:UniProtKB.
GO; GO:0045356; P:positive regulation of interferon-alpha biosynthetic process; IDA:UniProtKB.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; IDA:UniProtKB.
GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; IDA:UniProtKB.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IDA:CAFA.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IDA:CAFA.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; IMP:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0034158; P:toll-like receptor 8 signaling pathway; IDA:CAFA.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027175; TLR8.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR44312:SF2; PTHR44312:SF2; 1.
Pfam; PF13855; LRR_8; 5.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 15.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 20.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Inflammatory response; Innate immunity;
Leucine-rich repeat; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 1041 Toll-like receptor 8.
/FTId=PRO_0000034735.
TOPO_DOM 27 827 Extracellular. {ECO:0000255}.
TRANSMEM 828 848 Helical. {ECO:0000255}.
TOPO_DOM 849 1041 Cytoplasmic. {ECO:0000255}.
REPEAT 126 147 LRR 1. {ECO:0000269|PubMed:23520111}.
REPEAT 148 168 LRR 2. {ECO:0000269|PubMed:23520111}.
REPEAT 171 193 LRR 3. {ECO:0000269|PubMed:23520111}.
REPEAT 202 223 LRR 4. {ECO:0000269|PubMed:23520111}.
REPEAT 224 244 LRR 5. {ECO:0000269|PubMed:23520111}.
REPEAT 247 268 LRR 6. {ECO:0000269|PubMed:23520111}.
REPEAT 288 309 LRR 7. {ECO:0000269|PubMed:23520111}.
REPEAT 312 334 LRR 8. {ECO:0000269|PubMed:23520111}.
REPEAT 338 360 LRR 9. {ECO:0000269|PubMed:23520111}.
REPEAT 368 389 LRR 10. {ECO:0000269|PubMed:23520111}.
REPEAT 395 416 LRR 11. {ECO:0000269|PubMed:23520111}.
REPEAT 419 440 LRR 12. {ECO:0000269|PubMed:23520111}.
REPEAT 482 503 LRR 13. {ECO:0000269|PubMed:23520111}.
REPEAT 506 527 LRR 14. {ECO:0000269|PubMed:23520111}.
REPEAT 531 551 LRR 15. {ECO:0000269|PubMed:23520111}.
REPEAT 555 577 LRR 16. {ECO:0000269|PubMed:23520111}.
REPEAT 585 606 LRR 17. {ECO:0000269|PubMed:23520111}.
REPEAT 609 630 LRR 18. {ECO:0000269|PubMed:23520111}.
REPEAT 640 661 LRR 19. {ECO:0000269|PubMed:23520111}.
REPEAT 665 685 LRR 20. {ECO:0000269|PubMed:23520111}.
REPEAT 689 710 LRR 21. {ECO:0000269|PubMed:23520111}.
REPEAT 713 734 LRR 22. {ECO:0000269|PubMed:23520111}.
REPEAT 737 758 LRR 23. {ECO:0000269|PubMed:23520111}.
DOMAIN 772 824 LRRCT.
DOMAIN 878 1025 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23520111}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 362 362 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 395 395 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23520111}.
CARBOHYD 416 416 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 443 443 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 511 511 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23520111}.
CARBOHYD 546 546 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23520111}.
CARBOHYD 582 582 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 590 590 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23520111}.
CARBOHYD 640 640 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23520111}.
CARBOHYD 680 680 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23520111}.
CARBOHYD 752 752 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 49 {ECO:0000269|PubMed:23520111}.
DISULFID 181 187 {ECO:0000269|PubMed:23520111}.
DISULFID 257 270 {ECO:0000269|PubMed:23520111}.
DISULFID 260 267 {ECO:0000269|PubMed:23520111}.
DISULFID 479 509 {ECO:0000269|PubMed:23520111}.
DISULFID 776 803 {ECO:0000269|PubMed:23520111}.
VAR_SEQ 1 1 M -> MKESSLQNSSCSLGKETKK (in isoform 2).
{ECO:0000303|PubMed:11022119}.
/FTId=VSP_053412.
VARIANT 10 10 M -> V (in dbSNP:rs5744077).
/FTId=VAR_024667.
VARIANT 715 715 R -> Q (in dbSNP:rs5744082).
/FTId=VAR_052363.
MUTAGEN 348 348 Y->A: Abolishes activation of NF-kappa-B.
{ECO:0000269|PubMed:23520111}.
MUTAGEN 378 378 V->A: Increases activation of NF-kappa-B.
{ECO:0000269|PubMed:23520111}.
MUTAGEN 405 405 F->A: Abolishes activation of NF-kappa-B.
{ECO:0000269|PubMed:23520111}.
MUTAGEN 520 520 V->A: Strongly decreases activation of
NF-kappa-B.
{ECO:0000269|PubMed:23520111}.
MUTAGEN 543 543 D->A: Abolishes activation of NF-kappa-B.
{ECO:0000269|PubMed:23520111}.
MUTAGEN 574 574 T->A: Strongly decreases activation of
NF-kappa-B.
{ECO:0000269|PubMed:23520111}.
CONFLICT 217 217 P -> S (in Ref. 1; AAF64061).
{ECO:0000305}.
CONFLICT 328 328 A -> V (in Ref. 5; AAQ88663).
{ECO:0000305}.
CONFLICT 366 366 L -> P (in Ref. 1; AAF64061).
{ECO:0000305}.
CONFLICT 410 410 D -> N (in Ref. 4; AAZ95439).
{ECO:0000305}.
CONFLICT 867 867 V -> I (in Ref. 1; AAF64061).
{ECO:0000305}.
STRAND 37 39 {ECO:0000244|PDB:3WN4}.
STRAND 42 44 {ECO:0000244|PDB:4R0A}.
STRAND 46 48 {ECO:0000244|PDB:3WN4}.
STRAND 66 69 {ECO:0000244|PDB:3WN4}.
TURN 80 85 {ECO:0000244|PDB:3WN4}.
STRAND 91 93 {ECO:0000244|PDB:3WN4}.
STRAND 96 98 {ECO:0000244|PDB:3W3J}.
TURN 118 123 {ECO:0000244|PDB:3WN4}.
STRAND 129 131 {ECO:0000244|PDB:3WN4}.
STRAND 149 152 {ECO:0000244|PDB:3WN4}.
HELIX 163 166 {ECO:0000244|PDB:3WN4}.
STRAND 174 176 {ECO:0000244|PDB:3WN4}.
STRAND 179 181 {ECO:0000244|PDB:3WN4}.
STRAND 183 185 {ECO:0000244|PDB:5WYX}.
TURN 194 199 {ECO:0000244|PDB:3WN4}.
STRAND 205 207 {ECO:0000244|PDB:3WN4}.
STRAND 225 228 {ECO:0000244|PDB:3WN4}.
TURN 241 244 {ECO:0000244|PDB:3WN4}.
STRAND 250 252 {ECO:0000244|PDB:3WN4}.
HELIX 271 273 {ECO:0000244|PDB:3WN4}.
TURN 280 285 {ECO:0000244|PDB:3WN4}.
STRAND 291 293 {ECO:0000244|PDB:3WN4}.
HELIX 304 307 {ECO:0000244|PDB:3WN4}.
STRAND 315 317 {ECO:0000244|PDB:3WN4}.
STRAND 320 322 {ECO:0000244|PDB:3W3K}.
HELIX 324 329 {ECO:0000244|PDB:3WN4}.
HELIX 331 335 {ECO:0000244|PDB:3WN4}.
STRAND 341 343 {ECO:0000244|PDB:3WN4}.
HELIX 361 365 {ECO:0000244|PDB:3WN4}.
STRAND 371 373 {ECO:0000244|PDB:3WN4}.
STRAND 380 382 {ECO:0000244|PDB:3WN4}.
HELIX 384 390 {ECO:0000244|PDB:3WN4}.
STRAND 398 400 {ECO:0000244|PDB:3WN4}.
HELIX 411 416 {ECO:0000244|PDB:3WN4}.
STRAND 417 419 {ECO:0000244|PDB:3W3N}.
STRAND 421 424 {ECO:0000244|PDB:3WN4}.
STRAND 459 461 {ECO:0000244|PDB:4R07}.
STRAND 467 469 {ECO:0000244|PDB:3WN4}.
HELIX 477 480 {ECO:0000244|PDB:3WN4}.
STRAND 485 487 {ECO:0000244|PDB:3WN4}.
TURN 498 503 {ECO:0000244|PDB:3WN4}.
STRAND 508 511 {ECO:0000244|PDB:3WN4}.
TURN 525 528 {ECO:0000244|PDB:3WN4}.
STRAND 533 536 {ECO:0000244|PDB:3WN4}.
TURN 547 552 {ECO:0000244|PDB:3WN4}.
STRAND 558 560 {ECO:0000244|PDB:3WN4}.
HELIX 565 568 {ECO:0000244|PDB:3WN4}.
TURN 571 573 {ECO:0000244|PDB:3W3G}.
HELIX 578 582 {ECO:0000244|PDB:3WN4}.
STRAND 588 590 {ECO:0000244|PDB:3WN4}.
STRAND 599 601 {ECO:0000244|PDB:5WYZ}.
STRAND 607 609 {ECO:0000244|PDB:3WN4}.
STRAND 612 614 {ECO:0000244|PDB:3WN4}.
HELIX 620 623 {ECO:0000244|PDB:3WN4}.
STRAND 626 629 {ECO:0000244|PDB:5HDH}.
TURN 630 637 {ECO:0000244|PDB:3WN4}.
STRAND 638 640 {ECO:0000244|PDB:3W3M}.
STRAND 643 645 {ECO:0000244|PDB:3WN4}.
HELIX 656 660 {ECO:0000244|PDB:3WN4}.
STRAND 667 670 {ECO:0000244|PDB:3WN4}.
HELIX 681 686 {ECO:0000244|PDB:3WN4}.
STRAND 692 694 {ECO:0000244|PDB:3WN4}.
HELIX 707 709 {ECO:0000244|PDB:3WN4}.
STRAND 716 718 {ECO:0000244|PDB:3WN4}.
TURN 729 733 {ECO:0000244|PDB:3WN4}.
STRAND 734 737 {ECO:0000244|PDB:5AZ5}.
STRAND 740 742 {ECO:0000244|PDB:3WN4}.
HELIX 753 756 {ECO:0000244|PDB:3WN4}.
STRAND 758 760 {ECO:0000244|PDB:3WN4}.
STRAND 765 768 {ECO:0000244|PDB:3WN4}.
HELIX 778 780 {ECO:0000244|PDB:3WN4}.
HELIX 781 789 {ECO:0000244|PDB:3WN4}.
TURN 790 792 {ECO:0000244|PDB:4R0A}.
HELIX 798 800 {ECO:0000244|PDB:3WN4}.
STRAND 801 806 {ECO:0000244|PDB:3WN4}.
TURN 807 811 {ECO:0000244|PDB:3WN4}.
HELIX 814 816 {ECO:0000244|PDB:4QBZ}.
HELIX 819 822 {ECO:0000244|PDB:5HDH}.
SEQUENCE 1041 AA; 119828 MW; 39A38B60629291C8 CRC64;
MENMFLQSSM LTCIFLLISG SCELCAEENF SRSYPCDEKK QNDSVIAECS NRRLQEVPQT
VGKYVTELDL SDNFITHITN ESFQGLQNLT KINLNHNPNV QHQNGNPGIQ SNGLNITDGA
FLNLKNLREL LLEDNQLPQI PSGLPESLTE LSLIQNNIYN ITKEGISRLI NLKNLYLAWN
CYFNKVCEKT NIEDGVFETL TNLELLSLSF NSLSHVPPKL PSSLRKLFLS NTQIKYISEE
DFKGLINLTL LDLSGNCPRC FNAPFPCVPC DGGASINIDR FAFQNLTQLR YLNLSSTSLR
KINAAWFKNM PHLKVLDLEF NYLVGEIASG AFLTMLPRLE ILDLSFNYIK GSYPQHINIS
RNFSKLLSLR ALHLRGYVFQ ELREDDFQPL MQLPNLSTIN LGINFIKQID FKLFQNFSNL
EIIYLSENRI SPLVKDTRQS YANSSSFQRH IRKRRSTDFE FDPHSNFYHF TRPLIKPQCA
AYGKALDLSL NSIFFIGPNQ FENLPDIACL NLSANSNAQV LSGTEFSAIP HVKYLDLTNN
RLDFDNASAL TELSDLEVLD LSYNSHYFRI AGVTHHLEFI QNFTNLKVLN LSHNNIYTLT
DKYNLESKSL VELVFSGNRL DILWNDDDNR YISIFKGLKN LTRLDLSLNR LKHIPNEAFL
NLPASLTELH INDNMLKFFN WTLLQQFPRL ELLDLRGNKL LFLTDSLSDF TSSLRTLLLS
HNRISHLPSG FLSEVSSLKH LDLSSNLLKT INKSALETKT TTKLSMLELH GNPFECTCDI
GDFRRWMDEH LNVKIPRLVD VICASPGDQR GKSIVSLELT TCVSDVTAVI LFFFTFFITT
MVMLAALAHH LFYWDVWFIY NVCLAKVKGY RSLSTSQTFY DAYISYDTKD ASVTDWVINE
LRYHLEESRD KNVLLCLEER DWDPGLAIID NLMQSINQSK KTVFVLTKKY AKSWNFKTAF
YLALQRLMDE NMDVIIFILL EPVLQHSQYL RLRQRICKSS ILQWPDNPKA EGLFWQTLRN
VVLTENDSRY NNMYVDSIKQ Y


Related products :

Catalog number Product name Quantity
20-321-175144 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - FITC CONJUGATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.1 mg
20-321-175147 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - FITC CONJUGATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.1 mg
20-321-175164 TOLL-LIKE RECEPTOR 1 (TLR1. CD281) - FITC CONJUGATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 1 (TLR1. CD281); Toll_interleukin-1 receptor-like protein; TIL; CD281 antigen Monoclonal 0.1 mg
20-321-175165 TOLL-LIKE RECEPTOR 1 (TLR1. CD281) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 1 (TLR1. CD281); Toll_interleukin-1 receptor-like protein; TIL; CD281 antigen Monoclonal 0.05 mg
20-321-175148 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.05 mg
20-321-175145 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.05 mg
20-321-175143 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.1 mg
20-321-175146 TOLL-LIKE RECEPTOR 2 (TLR2. CD282) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 2 (TLR2. CD282); Toll_interleukin 1 receptor-like protein 4; CD282 antigen Monoclonal 0.1 mg
20-321-175163 TOLL-LIKE RECEPTOR 1 (TLR1. CD281) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 1 (TLR1. CD281); Toll_interleukin-1 receptor-like protein; TIL; CD281 antigen Monoclonal 0.1 mg
20-321-175150 TOLL-LIKE RECEPTOR 4 (TLR4. CD284) - FITC CONJUGATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 4 (TLR4. CD284); Toll4; CD284 antigen Monoclonal 0.1 mg
20-321-175151 TOLL-LIKE RECEPTOR 4 (TLR4. CD284) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 4 (TLR4. CD284); Toll4; CD284 antigen Monoclonal 0.05 mg
18-661-15147 Toll-like receptor 2 - Toll_interleukin 1 receptor-like protein 4; CD282 antigen Polyclonal 0.1 mg
15-288-22787 Toll-like receptor 2 - Toll_interleukin 1 receptor-like protein 4; CD282 antigen Polyclonal 0.05 mg
15-288-22787 Toll-like receptor 2 - Toll_interleukin 1 receptor-like protein 4; CD282 antigen Polyclonal 0.1 mg
20-321-175172 TOLL-LIKE RECEPTOR 3 (TLR3. CD283) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 3 (TLR3. CD283); CD283 antigen Monoclonal 0.05 mg
20-321-175167 TOLL-LIKE RECEPTOR 9 (TLR9. CD289) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 9 (TLR9. CD289); CD289 antigen Monoclonal 0.05 mg
20-321-175149 TOLL-LIKE RECEPTOR 4 (TLR4. CD284) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 4 (TLR4. CD284); Toll4; CD284 antigen Monoclonal 0.1 mg
20-321-175166 TOLL-LIKE RECEPTOR 9 (TLR9. CD289) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 9 (TLR9. CD289); CD289 antigen Monoclonal 0.1 mg
20-321-175170 TOLL-LIKE RECEPTOR 3 (TLR3. CD283) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 3 (TLR3. CD283); CD283 antigen Monoclonal 0.1 mg
15-288-22788A Toll-like receptor 3 - CD283 antigen Polyclonal 0.05 mg
15-288-22790 Toll-like receptor 9 - CD289 antigen Polyclonal 0.1 mg
P-TLR9 Toll Receptor 9, Antigen blocking peptide 100ul
P-TLR8 Toll Receptor 8, Antigen blocking peptide 100ul
P-TLR5 Toll Receptor 5, Antigen blocking peptide 100ul
P-TLR13 Toll Receptor 13, Antigen blocking peptide 100ul


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur