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Toll-like receptor 9 (CD antigen CD289)

 TLR9_PIG                Reviewed;        1030 AA.
Q5I2M3;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
28-MAR-2018, entry version 85.
RecName: Full=Toll-like receptor 9;
AltName: CD_antigen=CD289;
Flags: Precursor;
Name=TLR9;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
Brownlie R., Mookherjee N., Mutwiri G., Babiuk L., Hecker R.,
Lipford G., Griebel P.;
"Sus scrofa 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; AY859728; AAW50956.1; -; mRNA.
UniGene; Ssc.16634; -.
ProteinModelPortal; Q5I2M3; -.
SMR; Q5I2M3; -.
STRING; 9823.ENSSSCP00000012188; -.
PaxDb; Q5I2M3; -.
PRIDE; Q5I2M3; -.
Ensembl; ENSSSCT00000012516; ENSSSCP00000012188; ENSSSCG00000011436.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000230468; -.
HOVERGEN; HBG018601; -.
InParanoid; Q5I2M3; -.
OMA; CRRCDHA; -.
OrthoDB; EOG091G0BWK; -.
TreeFam; TF325595; -.
Reactome; R-SSC-109704; PI3K Cascade.
Reactome; R-SSC-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-SSC-168138; Toll Like Receptor 9 (TLR9) Cascade.
Reactome; R-SSC-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-SSC-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
Reactome; R-SSC-975155; MyD88 dependent cascade initiated on endosome.
Proteomes; UP000008227; Chromosome 13.
Bgee; ENSSSCG00000011436; -.
Genevisible; Q5I2M3; SS.
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:0005578; C:proteinaceous extracellular matrix; 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; PF13516; LRR_6; 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; 17.
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 24 {ECO:0000255}.
CHAIN 25 1030 Toll-like receptor 9.
/FTId=PRO_0000227009.
TOPO_DOM 25 816 Extracellular. {ECO:0000255}.
TRANSMEM 817 837 Helical. {ECO:0000255}.
TOPO_DOM 838 1030 Cytoplasmic. {ECO:0000255}.
REPEAT 61 84 LRR 1.
REPEAT 86 109 LRR 2.
REPEAT 121 146 LRR 3.
REPEAT 149 165 LRR 4.
REPEAT 166 189 LRR 5.
REPEAT 197 220 LRR 6.
REPEAT 222 241 LRR 7.
REPEAT 242 267 LRR 8.
REPEAT 282 305 LRR 9.
REPEAT 307 331 LRR 10.
REPEAT 332 355 LRR 11.
REPEAT 362 385 LRR 12.
REPEAT 389 412 LRR 13.
REPEAT 414 439 LRR 14.
REPEAT 469 493 LRR 15.
REPEAT 495 518 LRR 16.
REPEAT 519 542 LRR 17.
REPEAT 544 571 LRR 18.
REPEAT 573 597 LRR 19.
REPEAT 599 621 LRR 20.
REPEAT 626 649 LRR 21.
REPEAT 651 674 LRR 22.
REPEAT 675 698 LRR 23.
REPEAT 700 722 LRR 24.
REPEAT 723 746 LRR 25.
REPEAT 748 771 LRR 26.
DOMAIN 865 1013 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
REGION 46 50 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
REGION 71 76 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
REGION 94 108 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
REGION 178 180 Interaction with CpG-DNA.
{ECO:0000250|UniProtKB:Q2EEY0}.
BINDING 131 131 CpG-DNA. {ECO:0000250|UniProtKB:Q2EEY0}.
BINDING 151 151 CpG-DNA. {ECO:0000250|UniProtKB:Q2EEY0}.
BINDING 207 207 CpG-DNA. {ECO:0000250|UniProtKB:Q2EEY0}.
BINDING 261 261 CpG-DNA. {ECO:0000250|UniProtKB:Q2EEY0}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 339 339 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 512 512 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 566 566 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 668 668 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 693 693 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 730 730 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 44 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 97 109 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 177 183 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 254 267 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 257 264 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 469 499 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 763 789 {ECO:0000250|UniProtKB:Q2EEY0}.
DISULFID 765 808 {ECO:0000250|UniProtKB:Q2EEY0}.
SEQUENCE 1030 AA; 115883 MW; 5D81A7DC80EE4D32 CRC64;
MGPRCTLHPL SLLVQVTALA AALAQGRLPA FLPCELQPHG LVNCNWLFLK SVPHFSAAAP
RANVTSLSLL SNRIHHLHDS DFVHLSSLRT LNLKWNCPPA GLSPMHFPCH MTIEPNTFLA
VPTLEELNLS YNSITTVPAL PDSLVSLSLS RTNILVLDPT HLTGLHALRY LYMDGNCYYK
NPCQGALEVV PGALLGLGNL THLSLKYNNL TEVPRSLPPS LETLLLSYNH IVTLTPEDLA
NLTALRVLDV GGNCRRCDHA RNPCRECPKD HPKLHSDTFS HLSRLEGLVL KDSSLYNLDT
RWFRGLDRLQ VLDLSENFLY DCITKTTAFQ GLARLRSLNL SFNYHKKVSF AHLHLAPSFG
HLRSLKELDM HGIFFRSLSE TTLQPLVQLP MLQTLRLQMN FINQAQLSIF GAFPGLLYVD
LSDNRISGAA RPVAITREVD GRERVWLPSR NLAPRPLDTL RSEDFMPNCK AFSFTLDLSR
NNLVTIQSEM FARLSRLECL RLSHNSISQA VNGSQFVPLT SLRVLDLSHN KLDLYHGRSF
TELPRLEALD LSYNSQPFTM QGVGHNLSFV AQLPALRYLS LAHNDIHSRV SQQLCSASLC
ALDFSGNDLS RMWAEGDLYL RFFQGLRSLV WLDLSQNHLH TLLPRALDNL PKSLKHLHLR
DNNLAFFNWS SLTLLPKLET LDLAGNQLKA LSNGSLPSGT QLRRLDLSGN SIGFVNPGFF
ALAKQLEELN LSANALKTVE PSWFGSMVGN LKVLDVSANP LHCACGATFV GFLLEVQAAV
PGLPSRVKCG SPGQLQGHSI FAQDLRLCLD ETLSWNCFGI SLLAMALGLV VPMLHHLCGW
DLWYCFHLCL AWLPHRGQRR GADALFYDAF VVFDKAQSAV ADWVYNELRV QLEERRGRRA
LRLCLEERDW LPGKTLFENL WASVYSSRKT LFVLAHTDRV SGLLRASFLL AQQRLLEDRK
DVVVLVILRP DAYRSRYVRL RQRLCRQSVL LWPHQPRGQG SFWAQLGTAL TRDNHHFYNR
NFCRGPTTAE


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