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 9 (CD antigen CD289)

 TLR9_MOUSE              Reviewed;        1032 AA.
Q9EQU3; F8VPN5; Q4L0K3; Q4L0K4; Q99MF2; Q99MQ8;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 3.
05-JUL-2017, entry version 152.
RecName: Full=Toll-like receptor 9;
AltName: CD_antigen=CD289;
Flags: Precursor;
Name=Tlr9;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11130078; DOI=10.1038/35047123;
Hemmi H., Takeuchi O., Kawai T., Kaisho T., Sato S., Sanjo H.,
Matsumoto M., Hoshino K., Wagner H., Takeda K., Akira S.;
"A Toll-like receptor recognizes bacterial DNA.";
Nature 408:740-745(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Macrophage;
PubMed=11470918; DOI=10.1073/pnas.161293498;
Bauer S.M., Kirschning C.J., Hacker H., Redecke V., Hausmann S.,
Akira S., Wagner H., Lipford G.B.;
"Human TLR9 confers responsiveness to bacterial DNA via species-
specific CpG motif recognition.";
Proc. Natl. Acad. Sci. U.S.A. 98:9237-9242(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=11867692;
Chuang T.-H., Lee J., Kline L., Mathison J.C., Ulevitch R.J.;
"Toll-like receptor 9 mediates CpG-DNA signaling.";
J. Leukoc. Biol. 71:538-544(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-964, FUNCTION, TISSUE
SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=BALB/cJ, and C57BL/6J;
PubMed=17474149; DOI=10.1002/eji.200636562;
Anderson A.E., Worku M.L., Khamri W., Bamford K.B., Walker M.M.,
Thursz M.R.;
"TLR9 polymorphisms determine murine lymphocyte responses to
Helicobacter: results from a genome-wide scan.";
Eur. J. Immunol. 37:1548-1561(2007).
[6]
FUNCTION IN CYTOMEGALOVIRUS INFECTION, AND MUTAGENESIS OF LEU-499.
PubMed=14993594; DOI=10.1073/pnas.0400525101;
Tabeta K., Georgel P., Janssen E., Du X., Hoebe K., Crozat K.,
Mudd S., Shamel L., Sovath S., Goode J., Alexopoulou L., Flavell R.A.,
Beutler B.;
"Toll-like receptors 9 and 3 as essential components of innate immune
defense against mouse cytomegalovirus infection.";
Proc. Natl. Acad. Sci. U.S.A. 101:3516-3521(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH UNC93B1.
PubMed=17452530; DOI=10.1083/jcb.200612056;
Brinkmann M.M., Spooner E., Hoebe K., Beutler B., Ploegh H.L.,
Kim Y.M.;
"The interaction between the ER membrane protein UNC93B and TLR3, 7,
and 9 is crucial for TLR signaling.";
J. Cell Biol. 177:265-275(2007).
[8]
INTERACTION WITH CNPY3.
PubMed=18780723; DOI=10.1093/intimm/dxn098;
Kiyokawa T., Akashi-Takamura S., Shibata T., Matsumoto F.,
Nishitani C., Kuroki Y., Seto Y., Miyake K.;
"A single base mutation in the PRAT4A gene reveals differential
interaction of PRAT4A with Toll-like receptors.";
Int. Immunol. 20:1407-1415(2008).
[9]
SUBCELLULAR LOCATION.
PubMed=18305481; DOI=10.1038/nature06726;
Kim Y.M., Brinkmann M.M., Paquet M.E., Ploegh H.L.;
"UNC93B1 delivers nucleotide-sensing toll-like receptors to
endolysosomes.";
Nature 452:234-238(2008).
[10]
FUNCTION, INTERACTION WITH MYD88, SUBCELLULAR LOCATION, AND
PROTEOLYTIC CLEAVAGE.
PubMed=18820679; DOI=10.1038/nature07405;
Ewald S.E., Lee B.L., Lau L., Wickliffe K.E., Shi G.P., Chapman H.A.,
Barton G.M.;
"The ectodomain of Toll-like receptor 9 is cleaved to generate a
functional receptor.";
Nature 456:658-662(2008).
[11]
FUNCTION, INTERACTION WITH UNC93B1, SUBCELLULAR LOCATION, PROTEOLYTIC
CLEAVAGE, AND 3D-STRUCTURE MODELING OF THE ECTODOMAIN.
PubMed=18931679; DOI=10.1038/ni.1669;
Park B., Brinkmann M.M., Spooner E., Lee C.C., Kim Y.M., Ploegh H.L.;
"Proteolytic cleavage in an endolysosomal compartment is required for
activation of Toll-like receptor 9.";
Nat. Immunol. 9:1407-1414(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
INTERACTION WITH CNPY3 AND HSP90B1.
PubMed=20865800; DOI=10.1038/ncomms1070;
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y.,
Hao B., Bona R., Han D., Li Z.;
"Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a
substrate-specific cochaperone.";
Nat. Commun. 1:79-79(2010).
[14]
ERRATUM.
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y.,
Hao B., Bona R., Han D., Li Z.;
Nat. Commun. 3:653-653(2012).
[15]
FUNCTION, AND PROTEOLYTIC CLEAVAGE.
PubMed=21402738; DOI=10.1084/jem.20100682;
Ewald S.E., Engel A., Lee J., Wang M., Bogyo M., Barton G.M.;
"Nucleic acid recognition by Toll-like receptors is coupled to
stepwise processing by cathepsins and asparagine endopeptidase.";
J. Exp. Med. 208:643-651(2011).
[16]
INTERACTION WITH CD300LH.
PubMed=21940676; DOI=10.4049/jimmunol.1003806;
Wu Y., Zhu X., Li N., Chen T., Yang M., Yao M., Liu X., Jin B.,
Wang X., Cao X.;
"CMRF-35-like molecule 3 preferentially promotes TLR9-triggered
proinflammatory cytokine production in macrophages by enhancing TNF
receptor-associated factor 6 ubiquitination.";
J. Immunol. 187:4881-4889(2011).
[17]
INTERACTION WITH SMPDL3B.
PubMed=26095358; DOI=10.1016/j.celrep.2015.05.006;
Heinz L.X., Baumann C.L., Koeberlin M.S., Snijder B., Gawish R.,
Shui G., Sharif O., Aspalter I.M., Mueller A.C., Kandasamy R.K.,
Breitwieser F.P., Pichlmair A., Bruckner M., Rebsamen M., Blueml S.,
Karonitsch T., Fauster A., Colinge J., Bennett K.L., Knapp S.,
Wenk M.R., Superti-Furga G.;
"The lipid-modifying enzyme SMPDL3B negatively regulates innate
immunity.";
Cell Rep. 11:1919-1928(2015).
[18]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 26-818 OF UNLIGANDED REDUCED
GLYCOSYLATION MUTANT AND IN COMPLEXES WITH INHIBITORY DNA, FUNCTION,
GLYCOSYLATION AT ASN-210; ASN-332 AND ASN-732, DISULFIDE BONDS, AND
MUTAGENESIS OF TRP-47; ARG-74; SER-104; PHE-108; TYR-132; HIS-152;
TYR-179; TYR-229; HIS-642; PHE-668 AND ASN-695.
PubMed=25686612; DOI=10.1038/nature14138;
Ohto U., Shibata T., Tanji H., Ishida H., Krayukhina E., Uchiyama S.,
Miyake K., Shimizu T.;
"Structural basis of CpG and inhibitory DNA recognition by Toll-like
receptor 9.";
Nature 520:702-705(2015).
-!- 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. TLR9 is a nucleotide-sensing TLR which is
activated by unmethylated cytidine-phosphate-guanosine (CpG)
dinucleotides. Acts via MYD88 and TRAF6, leading to NF-kappa-B
activation, cytokine secretion and the inflammatory response
(PubMed:18931679, PubMed:21402738, PubMed:14993594,
PubMed:17474149, PubMed:25686612, PubMed:18820679). Plays a role
in defense against systemic mouse cytomegalovirus infection
(PubMed:14993594). Controls lymphocyte response to Helicobacter
infection (PubMed:17474149). {ECO:0000269|PubMed:14993594,
ECO:0000269|PubMed:17474149, ECO:0000269|PubMed:18820679,
ECO:0000269|PubMed:18931679, ECO:0000269|PubMed:21402738,
ECO:0000269|PubMed:25686612}.
-!- SUBUNIT: Monomer and homodimer. Exists as a monomer in the absence
of unmethylated cytidine-phosphate-guanosine (CpG) ligand.
Proteolytic processing of an insertion loop (Z-loop) is required
for homodimerization upon binding to the unmethylated CpG ligand
leading to its activation (By similarity). Interacts with MYD88
via their respective TIR domains (PubMed:18820679). Interacts with
BTK (By similarity). Interacts (via transmembrane domain) with
UNC93B1 (PubMed:17452530, PubMed:18931679). Interacts with
CD300LH; the interaction may promote full activation of TLR9-
triggered innate responses (PubMed:21940676). Interacts with CNPY3
and HSP90B1; this interaction is required for proper folding in
the endoplasmic reticulum (PubMed:18780723, PubMed:20865800).
Interacts with SMPDL3B (PubMed:26095358).
{ECO:0000250|UniProtKB:Q2EEY0, ECO:0000250|UniProtKB:Q9NR96,
ECO:0000269|PubMed:17452530, ECO:0000269|PubMed:18780723,
ECO:0000269|PubMed:18820679, ECO:0000269|PubMed:18931679,
ECO:0000269|PubMed:20865800, ECO:0000269|PubMed:21940676,
ECO:0000269|PubMed:26095358}.
-!- INTERACTION:
P11507:Atp2a2 (xeno); NbExp=4; IntAct=EBI-9979528, EBI-916319;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:18305481}; Single-pass type I membrane protein
{ECO:0000269|PubMed:18305481}. Endosome
{ECO:0000269|PubMed:18305481}. Lysosome
{ECO:0000269|PubMed:18305481, ECO:0000269|PubMed:18820679}.
Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:18305481,
ECO:0000269|PubMed:18820679}. Note=Relocalizes from endoplasmic
reticulum to endosome and lysosome upon stimulation with agonist
(PubMed:18305481). Exit from the ER requires UNC93B1
(PubMed:18820679). Endolysosomal localization is required for
proteolytic cleavage and subsequent activation (PubMed:18931679,
PubMed:18820679). Intracellular localization of the active
receptor may prevent from responding to self nucleic acid
(PubMed:18820679). {ECO:0000269|PubMed:18305481,
ECO:0000269|PubMed:18820679, ECO:0000269|PubMed:18931679}.
-!- TISSUE SPECIFICITY: Expressed in the basolateral region of gastric
epithelial cells with high levels detected in antrum and body
mucosa (at protein level). Detected in spleen and stomach at
higher levels in C57BL/6 mice than BALB/C.
{ECO:0000269|PubMed:17474149}.
-!- INDUCTION: Following Helicobacter infection, down-regulated in
C57BL/6 mice and up-regulated in BALB/C mice.
{ECO:0000269|PubMed:17474149}.
-!- PTM: Activated by proteolytic cleavage of the flexible loop
between repeats LRR14 and LRR15 within the ectodomain
(PubMed:18931679, PubMed:18820679). Cleavage requires UNC93B1
(PubMed:18820679). Proteolytically processed by first removing the
majority of the ectodomain by either asparagine endopeptidase
(AEP) or a cathepsin followed by a trimming event that is solely
cathepsin mediated and required for optimal receptor signaling
(PubMed:21402738). {ECO:0000269|PubMed:18820679,
ECO:0000269|PubMed:18931679, ECO:0000269|PubMed:21402738}.
-!- DISRUPTION PHENOTYPE: Reduced proliferation of lymphocytes,
reduced interferon-gamma production by splenocytes and reduced
neutrophil numbers following Helicobacter infection.
{ECO:0000269|PubMed:17474149}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB045181; BAB19260.1; -; mRNA.
EMBL; AF348140; AAK29625.1; -; mRNA.
EMBL; AF314224; AAK28488.1; -; mRNA.
EMBL; AC164430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY649790; AAU04980.1; -; Genomic_DNA.
EMBL; AY649791; AAU04981.1; -; Genomic_DNA.
CCDS; CCDS40755.1; -.
RefSeq; NP_112455.2; NM_031178.2.
UniGene; Mm.44889; -.
PDB; 3WPF; X-ray; 1.96 A; A=26-818.
PDB; 3WPG; X-ray; 2.25 A; A=26-818.
PDB; 3WPH; X-ray; 2.33 A; A=26-818.
PDB; 3WPI; X-ray; 2.25 A; A=26-818.
PDB; 4QDH; X-ray; 2.40 A; A/B=480-753.
PDBsum; 3WPF; -.
PDBsum; 3WPG; -.
PDBsum; 3WPH; -.
PDBsum; 3WPI; -.
PDBsum; 4QDH; -.
ProteinModelPortal; Q9EQU3; -.
SMR; Q9EQU3; -.
IntAct; Q9EQU3; 28.
STRING; 10090.ENSMUSP00000082207; -.
ChEMBL; CHEMBL6128; -.
iPTMnet; Q9EQU3; -.
PhosphoSitePlus; Q9EQU3; -.
MaxQB; Q9EQU3; -.
PaxDb; Q9EQU3; -.
PeptideAtlas; Q9EQU3; -.
PRIDE; Q9EQU3; -.
Ensembl; ENSMUST00000062241; ENSMUSP00000082207; ENSMUSG00000045322.
GeneID; 81897; -.
KEGG; mmu:81897; -.
UCSC; uc009rjh.1; mouse.
CTD; 54106; -.
MGI; MGI:1932389; Tlr9.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000230468; -.
HOVERGEN; HBG018601; -.
InParanoid; Q9EQU3; -.
KO; K10161; -.
OMA; CRRCDHA; -.
OrthoDB; EOG091G0BWK; -.
TreeFam; TF325595; -.
Reactome; R-MMU-109704; PI3K Cascade.
Reactome; R-MMU-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-MMU-168138; Toll Like Receptor 9 (TLR9) Cascade.
Reactome; R-MMU-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-MMU-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
Reactome; R-MMU-975155; MyD88 dependent cascade initiated on endosome.
PRO; PR:Q9EQU3; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000045322; -.
CleanEx; MM_TLR9; -.
Genevisible; Q9EQU3; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0032009; C:early phagosome; IDA:UniProtKB.
GO; GO:0036019; C:endolysosome; IMP:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; IGI:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005578; C:proteinaceous extracellular matrix; IBA:GO_Central.
GO; GO:0005149; F:interleukin-1 receptor binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0045322; F:unmethylated CpG binding; ISS:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
GO; GO:1902350; P:cellular response to chloroquine; IDA:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071248; P:cellular response to metal ion; IEA:Ensembl.
GO; GO:0001816; P:cytokine production; IDA:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
GO; GO:0051607; P:defense response to virus; IGI:MGI.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0007252; P:I-kappaB phosphorylation; ISO:MGI.
GO; GO:0006955; P:immune response; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:BHF-UCL.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IPI:UniProtKB.
GO; GO:1901895; P:negative regulation of calcium-transporting ATPase activity; ISO:MGI.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:BHF-UCL.
GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; ISO:MGI.
GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
GO; GO:0045356; P:positive regulation of interferon-alpha biosynthetic process; ISS:UniProtKB.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; ISS:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:BHF-UCL.
GO; GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; ISS:UniProtKB.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
GO; GO:0032741; P:positive regulation of interleukin-18 production; IDA:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:MGI.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; IMP:UniProtKB.
GO; GO:0034123; P:positive regulation of toll-like receptor signaling pathway; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0050864; P:regulation of B cell activation; IGI:MGI.
GO; GO:0050707; P:regulation of cytokine secretion; IEA:InterPro.
GO; GO:0002730; P:regulation of dendritic cell cytokine production; IDA:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IMP:BHF-UCL.
GO; GO:0001932; P:regulation of protein phosphorylation; IDA:MGI.
GO; GO:0002237; P:response to molecule of bacterial origin; TAS:BHF-UCL.
GO; GO:0009615; P:response to virus; IMP:MGI.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IEA:InterPro.
GO; GO:0032640; P:tumor necrosis factor production; IMP:UniProtKB.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 7.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027181; TLR9.
PANTHER; PTHR24373:SF187; PTHR24373:SF187; 1.
Pfam; PF13855; LRR_8; 3.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 15.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 16.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasmic vesicle; Disulfide bond;
Endoplasmic reticulum; Endosome; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Leucine-rich repeat; Lysosome;
Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1032 Toll-like receptor 9.
/FTId=PRO_0000034738.
TOPO_DOM 26 818 Extracellular. {ECO:0000255}.
TRANSMEM 819 839 Helical. {ECO:0000255}.
TOPO_DOM 840 1032 Cytoplasmic. {ECO:0000255}.
REPEAT 62 85 LRR 1.
REPEAT 87 110 LRR 2.
REPEAT 122 147 LRR 3.
REPEAT 150 166 LRR 4.
REPEAT 167 190 LRR 5.
REPEAT 198 221 LRR 6.
REPEAT 223 242 LRR 7.
REPEAT 243 268 LRR 8.
REPEAT 283 306 LRR 9.
REPEAT 308 332 LRR 10.
REPEAT 333 356 LRR 11.
REPEAT 363 386 LRR 12.
REPEAT 390 413 LRR 13.
REPEAT 415 440 LRR 14.
REPEAT 471 495 LRR 15.
REPEAT 497 520 LRR 16.
REPEAT 521 544 LRR 17.
REPEAT 546 573 LRR 18.
REPEAT 575 599 LRR 19.
REPEAT 601 623 LRR 20.
REPEAT 628 651 LRR 21.
REPEAT 653 676 LRR 22.
REPEAT 677 700 LRR 23.
REPEAT 702 724 LRR 24.
REPEAT 725 748 LRR 25.
REPEAT 750 773 LRR 26.
DOMAIN 868 1016 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
REGION 47 51 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
REGION 72 77 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
REGION 95 109 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
REGION 179 181 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
BINDING 132 132 CpG-DNA. {ECO:0000250|UniProtKB:Q2EEY0}.
BINDING 208 208 CpG-DNA. {ECO:0000250|UniProtKB:Q2EEY0}.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPF, ECO:0000255,
ECO:0000269|PubMed:25686612}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPF,
ECO:0000244|PDB:3WPH, ECO:0000255,
ECO:0000269|PubMed:25686612}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 495 495 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 514 514 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 568 568 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 670 670 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 695 695 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 700 700 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 732 732 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPF,
ECO:0000244|PDB:3WPG,
ECO:0000244|PDB:3WPH,
ECO:0000244|PDB:3WPI, ECO:0000255,
ECO:0000269|PubMed:25686612}.
CARBOHYD 752 752 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 45 {ECO:0000244|PDB:3WPF,
ECO:0000244|PDB:3WPG,
ECO:0000244|PDB:3WPH,
ECO:0000244|PDB:3WPI,
ECO:0000269|PubMed:25686612}.
DISULFID 98 110 {ECO:0000244|PDB:3WPF,
ECO:0000244|PDB:3WPG,
ECO:0000244|PDB:3WPH,
ECO:0000244|PDB:3WPI,
ECO:0000269|PubMed:25686612}.
DISULFID 178 184 {ECO:0000244|PDB:3WPF,
ECO:0000244|PDB:3WPG,
ECO:0000244|PDB:3WPH,
ECO:0000244|PDB:3WPI,
ECO:0000269|PubMed:25686612}.
DISULFID 255 268 {ECO:0000244|PDB:3WPF,
ECO:0000244|PDB:3WPG,
ECO:0000244|PDB:3WPH,
ECO:0000244|PDB:3WPI,
ECO:0000269|PubMed:25686612}.
DISULFID 258 265 {ECO:0000244|PDB:3WPF,
ECO:0000244|PDB:3WPG,
ECO:0000244|PDB:3WPH,
ECO:0000244|PDB:3WPI,
ECO:0000269|PubMed:25686612}.
DISULFID 471 501 {ECO:0000244|PDB:3WPF,
ECO:0000244|PDB:3WPG,
ECO:0000244|PDB:3WPH,
ECO:0000244|PDB:3WPI,
ECO:0000269|PubMed:25686612}.
DISULFID 765 791 {ECO:0000244|PDB:3WPF,
ECO:0000244|PDB:3WPG,
ECO:0000244|PDB:3WPH,
ECO:0000244|PDB:3WPI,
ECO:0000269|PubMed:25686612}.
DISULFID 767 810 {ECO:0000244|PDB:3WPF,
ECO:0000244|PDB:3WPG,
ECO:0000244|PDB:3WPH,
ECO:0000244|PDB:3WPI,
ECO:0000269|PubMed:25686612}.
MUTAGEN 47 47 W->A: Significantly decreased NF-kappa-B
activation.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 74 74 R->A: Significantly decreased NF-kappa-B
activation.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 104 104 S->A: Significantly decreased NF-kappa-B
activation.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 108 108 F->A: Significantly decreased NF-kappa-B
activation.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 132 132 Y->A: Significantly decreased NF-kappa-B
activation.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 152 152 H->A: Significantly decreased NF-kappa-B
activation.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 179 179 Y->A: Significantly decreased NF-kappa-B
activation.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 229 229 Y->A: Significantly decreased NF-kappa-B
activation.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 499 499 L->P: Highly susceptible to mouse
cytomegalovirus infection. Shows low
level of cytokine induction and natural
killer activation on viral infection.
{ECO:0000269|PubMed:14993594}.
MUTAGEN 642 642 H->A: Loss of NF-kappa-B activation.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 668 668 F->A: Significantly decreased NF-kappa-B
activation.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 695 695 N->A: Significantly decreased NF-kappa-B
activation.
{ECO:0000269|PubMed:25686612}.
CONFLICT 325 325 T -> N (in Ref. 1; BAB19260, 2; AAK29625,
3; AAK28488 and 5; AAU04980).
{ECO:0000305}.
CONFLICT 378 378 L -> S (in Ref. 1; BAB19260, 2; AAK29625,
3; AAK28488 and 5; AAU04980).
{ECO:0000305}.
CONFLICT 554 554 S -> G (in Ref. 3; AAK28488).
{ECO:0000305}.
CONFLICT 562 562 M -> I (in Ref. 3; AAK28488).
{ECO:0000305}.
CONFLICT 573 573 T -> A (in Ref. 2; AAK29625, 3; AAK28488
and 5; AAU04980). {ECO:0000305}.
CONFLICT 579 579 Q -> H (in Ref. 2; AAK29625, 3; AAK28488
and 5; AAU04980). {ECO:0000305}.
CONFLICT 867 867 T -> A (in Ref. 2; AAK29625, 3; AAK28488
and 5; AAU04980). {ECO:0000305}.
CONFLICT 897 897 E -> G (in Ref. 3; AAK28488).
{ECO:0000305}.
TURN 31 34 {ECO:0000244|PDB:3WPF}.
STRAND 35 38 {ECO:0000244|PDB:3WPF}.
TURN 39 41 {ECO:0000244|PDB:3WPF}.
STRAND 42 44 {ECO:0000244|PDB:3WPF}.
STRAND 67 69 {ECO:0000244|PDB:3WPF}.
TURN 80 83 {ECO:0000244|PDB:3WPF}.
HELIX 84 86 {ECO:0000244|PDB:3WPF}.
STRAND 90 93 {ECO:0000244|PDB:3WPF}.
STRAND 100 102 {ECO:0000244|PDB:3WPI}.
TURN 116 121 {ECO:0000244|PDB:3WPF}.
STRAND 127 129 {ECO:0000244|PDB:3WPF}.
STRAND 147 149 {ECO:0000244|PDB:3WPF}.
HELIX 160 163 {ECO:0000244|PDB:3WPF}.
STRAND 171 173 {ECO:0000244|PDB:3WPF}.
STRAND 177 179 {ECO:0000244|PDB:3WPF}.
TURN 192 197 {ECO:0000244|PDB:3WPF}.
STRAND 203 205 {ECO:0000244|PDB:3WPF}.
STRAND 223 226 {ECO:0000244|PDB:3WPF}.
HELIX 237 239 {ECO:0000244|PDB:3WPF}.
STRAND 247 250 {ECO:0000244|PDB:3WPF}.
STRAND 254 256 {ECO:0000244|PDB:3WPF}.
STRAND 269 272 {ECO:0000244|PDB:3WPF}.
TURN 277 282 {ECO:0000244|PDB:3WPF}.
STRAND 288 290 {ECO:0000244|PDB:3WPF}.
HELIX 301 304 {ECO:0000244|PDB:3WPF}.
STRAND 312 314 {ECO:0000244|PDB:3WPF}.
STRAND 317 319 {ECO:0000244|PDB:3WPF}.
HELIX 321 324 {ECO:0000244|PDB:3WPF}.
HELIX 329 332 {ECO:0000244|PDB:3WPI}.
STRAND 338 340 {ECO:0000244|PDB:3WPF}.
STRAND 347 349 {ECO:0000244|PDB:3WPF}.
HELIX 358 362 {ECO:0000244|PDB:3WPF}.
STRAND 368 370 {ECO:0000244|PDB:3WPF}.
STRAND 377 379 {ECO:0000244|PDB:3WPF}.
TURN 381 384 {ECO:0000244|PDB:3WPF}.
HELIX 385 387 {ECO:0000244|PDB:3WPF}.
STRAND 395 397 {ECO:0000244|PDB:3WPF}.
HELIX 408 412 {ECO:0000244|PDB:3WPF}.
STRAND 413 416 {ECO:0000244|PDB:3WPI}.
STRAND 419 421 {ECO:0000244|PDB:3WPF}.
STRAND 473 475 {ECO:0000244|PDB:3WPF}.
STRAND 477 479 {ECO:0000244|PDB:3WPF}.
HELIX 490 493 {ECO:0000244|PDB:3WPF}.
STRAND 501 503 {ECO:0000244|PDB:3WPF}.
TURN 517 520 {ECO:0000244|PDB:3WPH}.
STRAND 526 528 {ECO:0000244|PDB:3WPF}.
TURN 539 544 {ECO:0000244|PDB:3WPF}.
STRAND 550 552 {ECO:0000244|PDB:3WPF}.
HELIX 570 574 {ECO:0000244|PDB:3WPF}.
STRAND 580 582 {ECO:0000244|PDB:3WPF}.
STRAND 590 592 {ECO:0000244|PDB:4QDH}.
STRAND 597 600 {ECO:0000244|PDB:3WPF}.
STRAND 603 605 {ECO:0000244|PDB:3WPF}.
HELIX 611 615 {ECO:0000244|PDB:3WPF}.
TURN 620 626 {ECO:0000244|PDB:3WPF}.
STRAND 633 635 {ECO:0000244|PDB:3WPF}.
HELIX 646 650 {ECO:0000244|PDB:3WPF}.
STRAND 658 660 {ECO:0000244|PDB:3WPF}.
HELIX 671 676 {ECO:0000244|PDB:3WPF}.
STRAND 682 684 {ECO:0000244|PDB:3WPF}.
STRAND 706 708 {ECO:0000244|PDB:3WPF}.
TURN 719 724 {ECO:0000244|PDB:3WPF}.
STRAND 730 732 {ECO:0000244|PDB:3WPF}.
HELIX 743 745 {ECO:0000244|PDB:3WPF}.
HELIX 747 751 {ECO:0000244|PDB:3WPF}.
STRAND 754 757 {ECO:0000244|PDB:3WPF}.
HELIX 771 777 {ECO:0000244|PDB:3WPF}.
HELIX 779 781 {ECO:0000244|PDB:3WPF}.
TURN 783 788 {ECO:0000244|PDB:3WPF}.
STRAND 789 794 {ECO:0000244|PDB:3WPF}.
TURN 795 797 {ECO:0000244|PDB:3WPF}.
HELIX 807 809 {ECO:0000244|PDB:3WPF}.
SEQUENCE 1032 AA; 116412 MW; C13A7888588CE297 CRC64;
MVLRRRTLHP LSLLVQAAVL AETLALGTLP AFLPCELKPH GLVDCNWLFL KSVPRFSAAA
SCSNITRLSL ISNRIHHLHN SDFVHLSNLR QLNLKWNCPP TGLSPLHFSC HMTIEPRTFL
AMRTLEELNL SYNGITTVPR LPSSLVNLSL SHTNILVLDA NSLAGLYSLR VLFMDGNCYY
KNPCTGAVKV TPGALLGLSN LTHLSLKYNN LTKVPRQLPP SLEYLLVSYN LIVKLGPEDL
ANLTSLRVLD VGGNCRRCDH APNPCIECGQ KSLHLHPETF HHLSHLEGLV LKDSSLHTLN
SSWFQGLVNL SVLDLSENFL YESITHTNAF QNLTRLRKLN LSFNYRKKVS FARLHLASSF
KNLVSLQELN MNGIFFRLLN KYTLRWLADL PKLHTLHLQM NFINQAQLSI FGTFRALRFV
DLSDNRISGP STLSEATPEE ADDAEQEELL SADPHPAPLS TPASKNFMDR CKNFKFTMDL
SRNNLVTIKP EMFVNLSRLQ CLSLSHNSIA QAVNGSQFLP LTNLQVLDLS HNKLDLYHWK
SFSELPQLQA LDLSYNSQPF SMKGIGHNFS FVTHLSMLQS LSLAHNDIHT RVSSHLNSNS
VRFLDFSGNG MGRMWDEGGL YLHFFQGLSG LLKLDLSQNN LHILRPQNLD NLPKSLKLLS
LRDNYLSFFN WTSLSFLPNL EVLDLAGNQL KALTNGTLPN GTLLQKLDVS SNSIVSVVPA
FFALAVELKE VNLSHNILKT VDRSWFGPIV MNLTVLDVRS NPLHCACGAA FVDLLLEVQT
KVPGLANGVK CGSPGQLQGR SIFAQDLRLC LDEVLSWDCF GLSLLAVAVG MVVPILHHLC
GWDVWYCFHL CLAWLPLLAR SRRSAQTLPY DAFVVFDKAQ SAVADWVYNE LRVRLEERRG
RRALRLCLED RDWLPGQTLF ENLWASIYGS RKTLFVLAHT DRVSGLLRTS FLLAQQRLLE
DRKDVVVLVI LRPDAHRSRY VRLRQRLCRQ SVLFWPQQPN GQGGFWAQLS TALTRDNRHF
YNQNFCRGPT AE


Related products :

Catalog number Product name Quantity
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
20-321-175166 TOLL-LIKE RECEPTOR 9 (TLR9. CD289) - MONOCLONAL ANTIBODY TO HUMAN TOLL-LIKE RECEPTOR 9 (TLR9. CD289); CD289 antigen Monoclonal 0.1 mg
15-288-22790 Toll-like receptor 9 - CD289 antigen Polyclonal 0.1 mg
15-288-22790 Toll-like receptor 9 - CD289 antigen Polyclonal 0.05 mg
20-321-175046 TOLL-LIKE RECEPTOR 9 (TLR9. CD289) - BIOTINYLATED MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 9 (TLR9. CD289) Monoclonal 0.05 mg
20-321-175045 TOLL-LIKE RECEPTOR 9 (TLR9. CD289) - MONOCLONAL ANTIBODY TO MOUSE TOLL-LIKE RECEPTOR 9 (TLR9. CD289) Monoclonal 0.1 mg
UT-E04527 Human Toll-Like Receptor 9 (TLR-9 CD289) ELISA Kit 96T
GWB-CF8A75 TOLL-LIKE RECEPTOR 9 (TLR9. CD289), Antibody
UB-E04527 Human Toll-like receptor 9(TLR-9 per CD289)ELISA Kit 96T
GWB-86AFF8 TOLL-LIKE RECEPTOR 9 (TLR9. CD289), Antibody
GWB-57E784 TOLL-LIKE RECEPTOR 9 (TLR9. CD289), Antibody
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
20-321-175147 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
20-321-175144 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
20-321-175148 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
20-321-175165 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
20-321-175163 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
20-321-175143 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
20-321-175150 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
15-288-22787 Toll-like receptor 2 - Toll_interleukin 1 receptor-like protein 4; CD282 antigen Polyclonal 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 0.1 mg


 

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