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Toll-like receptor 9 (CD antigen CD289)

 TLR9_CANLF              Reviewed;        1032 AA.
Q5I2M8;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
20-JUN-2018, entry version 92.
RecName: Full=Toll-like receptor 9;
AltName: CD_antigen=CD289;
Flags: Precursor;
Name=TLR9;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
Brownlie R., Mookherjee N., Mutwiri G., Babiuk L., Hecker R.,
Lipford G., Griebel P.;
"Canis familiaris toll-like receptor 9 mRNA.";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
-!- 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. Upon
CpG stimulation, induces B-cell proliferation, activation,
survival and antibody production (By similarity).
{ECO:0000250|UniProtKB:Q9EQU3, ECO:0000250|UniProtKB:Q9NR96}.
-!- 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 (By similarity). Interacts with
BTK (By similarity). Interacts (via transmembrane domain) with
UNC93B1. Interacts with CD300LH; the interaction may promote full
activation of TLR9-triggered innate responses. Interacts with
CNPY3 and HSP90B1; this interaction is required for proper folding
in the endoplasmic reticulum. Interacts with SMPDL3B (By
similarity). {ECO:0000250|UniProtKB:Q2EEY0,
ECO:0000250|UniProtKB:Q9EQU3, ECO:0000250|UniProtKB:Q9NR96}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9EQU3}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q9EQU3}. Endosome
{ECO:0000250|UniProtKB:Q9EQU3}. Lysosome
{ECO:0000250|UniProtKB:Q9EQU3}. Cytoplasmic vesicle, phagosome
{ECO:0000250|UniProtKB:Q9EQU3}. Note=Relocalizes from endoplasmic
reticulum to endosome and lysosome upon stimulation with agonist.
Exit from the ER requires UNC93B1. Endolysosomal localization is
required for proteolytic cleavage and subsequent activation.
Intracellular localization of the active receptor may prevent from
responding to self nucleic acid. {ECO:0000250|UniProtKB:Q9EQU3}.
-!- PTM: Activated by proteolytic cleavage of the flexible loop
between repeats LRR14 and LRR15 within the ectodomain. Cleavage
requires UNC93B1. 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.
{ECO:0000250|UniProtKB:Q9EQU3}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY859723; AAW50951.1; -; mRNA.
RefSeq; XP_013977197.1; XM_014121722.1.
UniGene; Cfa.824; -.
ProteinModelPortal; Q5I2M8; -.
SMR; Q5I2M8; -.
STRING; 9615.ENSCAFP00000030804; -.
PaxDb; Q5I2M8; -.
Ensembl; ENSCAFT00000035532; ENSCAFP00000030804; ENSCAFG00000023201.
GeneID; 403502; -.
CTD; 54106; -.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000230468; -.
HOVERGEN; HBG018601; -.
InParanoid; Q5I2M8; -.
OMA; CRRCDHA; -.
OrthoDB; EOG091G0BWK; -.
TreeFam; TF325595; -.
Reactome; R-CFA-109704; PI3K Cascade.
Reactome; R-CFA-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-CFA-168138; Toll Like Receptor 9 (TLR9) Cascade.
Reactome; R-CFA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-CFA-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
Reactome; R-CFA-975155; MyD88 dependent cascade initiated on endosome.
Proteomes; UP000002254; Chromosome 20.
Bgee; ENSCAFG00000023201; -.
GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
GO; GO:0036019; C:endolysosome; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; ISS: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; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005149; F:interleukin-1 receptor binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0008329; F:signaling pattern recognition receptor 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:0007409; P:axonogenesis; IBA:GO_Central.
GO; GO:1902350; P:cellular response to chloroquine; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IEA:Ensembl.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:Ensembl.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0050871; P:positive regulation of B cell activation; ISS:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; ISS:UniProtKB.
GO; GO:0002639; P:positive regulation of immunoglobulin production; ISS:UniProtKB.
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:0045078; P:positive regulation of interferon-gamma biosynthetic process; ISS:UniProtKB.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
GO; GO:0032741; P:positive regulation of interleukin-18 production; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl.
GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0045577; P:regulation of B cell differentiation; ISS:UniProtKB.
GO; GO:0050707; P:regulation of cytokine secretion; IEA:InterPro.
GO; GO:0002730; P:regulation of dendritic cell cytokine production; IEA:Ensembl.
GO; GO:0034163; P:regulation of toll-like receptor 9 signaling pathway; ISS:UniProtKB.
GO; GO:0002237; P:response to molecule of bacterial origin; IBA:GO_Central.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IEA:InterPro.
GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
GO; GO:0032640; P:tumor necrosis factor production; IEA:Ensembl.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027181; TLR9.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR24373:SF37; PTHR24373:SF37; 1.
Pfam; PF00560; LRR_1; 1.
Pfam; PF13855; LRR_8; 4.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 16.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 18.
PROSITE; PS50104; TIR; 1.
2: Evidence at transcript level;
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_0000227007.
TOPO_DOM 26 815 Extracellular. {ECO:0000255}.
TRANSMEM 816 836 Helical. {ECO:0000255}.
TOPO_DOM 837 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 472 496 LRR 15.
REPEAT 498 521 LRR 16.
REPEAT 522 545 LRR 17.
REPEAT 547 574 LRR 18.
REPEAT 576 600 LRR 19.
REPEAT 602 624 LRR 20.
REPEAT 629 652 LRR 21.
REPEAT 654 677 LRR 22.
REPEAT 678 701 LRR 23.
REPEAT 703 725 LRR 24.
REPEAT 726 749 LRR 25.
REPEAT 751 774 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 152 152 CpG-DNA. {ECO:0000250|UniProtKB:Q2EEY0}.
BINDING 208 208 CpG-DNA. {ECO:0000250|UniProtKB:Q2EEY0}.
BINDING 262 262 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 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 476 476 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 569 569 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 671 671 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 696 696 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 701 701 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 733 733 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 45 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 98 110 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 178 184 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 255 268 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 258 265 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 472 502 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 766 792 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 768 811 {ECO:0000250|UniProtKB:Q2EEY0}.
SEQUENCE 1032 AA; 115292 MW; 515C77FF681B74A2 CRC64;
MGPCRGALHP LSLLVQAAAL ALALAQGTLP AFLPCELQPH GLVNCNWLFL KSVPRFSAAA
PRGNVTSLSL YSNRIHHLHD YDFVHFVHLR RLNLKWNCPP ASLSPMHFPC HMTIEPNTFL
AVPTLEDLNL SYNSITTVPA LPSSLVSLSL SRTNILVLDP ATLAGLYALR FLFLDGNCYY
KNPCQQALQV APGALLGLGN LTHLSLKYNN LTVVPRGLPP SLEYLLLSYN HIITLAPEDL
ANLTALRVLD VGGNCRRCDH ARNPCRECPK GFPQLHPNTF GHLSHLEGLV LRDSSLYSLD
PRWFHGLGNL MVLDLSENFL YDCITKTKAF YGLARLRRLN LSFNYHKKVS FAHLHLASSF
GSLLSLQELD IHGIFFRSLS KTTLQSLAHL PMLQRLHLQL NFISQAQLSI FGAFPGLRYV
DLSDNRISGA AEPAAATGEV EADCGERVWP QSRDLALGPL GTPGSEAFMP SCRTLNFTLD
LSRNNLVTVQ PEMFVRLARL QCLGLSHNSI SQAVNGSQFV PLSNLRVLDL SHNKLDLYHG
RSFTELPRLE ALDLSYNSQP FSMRGVGHNL SFVAQLPALR YLSLAHNGIH SRVSQQLRSA
SLRALDFSGN TLSQMWAEGD LYLRFFQGLR SLVQLDLSQN RLHTLLPRNL DNLPKSLRLL
RLRDNYLAFF NWSSLALLPK LEALDLAGNQ LKALSNGSLP NGTQLQRLDL SGNSIGFVVP
SFFALAVRLR ELNLSANALK TVEPSWFGSL AGALKVLDVT ANPLHCACGA TFVDFLLEVQ
AAVPGLPSRV KCGSPGQLQG RSIFAQDLRL CLDEALSWVC FSLSLLAVAL SLAVPMLHQL
CGWDLWYCFH LCLAWLPRRG RRRGVDALAY DAFVVFDKAQ SSVADWVYNE LRVQLEERRG
RRALRLCLEE RDWVPGKTLF ENLWASVYSS RKTLFVLART DRVSGLLRAS FLLAQQRLLE
DRKDVVVLVI LCPDAHRSRY VRLRQRLCRQ SVLLWPHQPS GQRSFWAQLG TALTRDNRHF
YNQNFCRGPT TA


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