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Toll-like receptor 9 (CD antigen CD289)

 TLR9_HORSE              Reviewed;        1031 AA.
Q2EEY0;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 1.
28-MAR-2018, entry version 98.
RecName: Full=Toll-like receptor 9 {ECO:0000303|PubMed:18462806, ECO:0000312|EMBL:ABD36388.2};
AltName: CD_antigen=CD289 {ECO:0000305};
Flags: Precursor;
Name=TLR9 {ECO:0000303|PubMed:18462806, ECO:0000312|EMBL:ABD36388.2,
ECO:0000312|Ensembl:ENSECAP00000011919};
Equus caballus (Horse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9796 {ECO:0000312|EMBL:ABD36388.2};
[1] {ECO:0000312|EMBL:ABD36388.2}
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND
PHYLOGENETIC ANALYSIS.
PubMed=18462806; DOI=10.1016/j.vetimm.2008.03.005;
Zhang Y.W., Davis E.G., Blecha F., Wilkerson M.J.;
"Molecular cloning and characterization of equine Toll-like receptor
9.";
Vet. Immunol. Immunopathol. 124:209-219(2008).
[2] {ECO:0000312|Ensembl:ENSECAP00000011919}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Thoroughbred {ECO:0000312|Ensembl:ENSECAP00000011919};
PubMed=19892987; DOI=10.1126/science.1178158;
Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H.,
Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N.,
Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L.,
Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J.,
Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J.,
Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R.,
Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F.,
Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L.,
Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M.,
White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
"Genome sequence, comparative analysis, and population genetics of the
domestic horse.";
Science 326:865-867(2009).
[3]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=19548205; DOI=10.1002/ar.20927;
Schneberger D., Caldwell S., Suri S.S., Singh B.;
"Expression of toll-like receptor 9 in horse lungs.";
Anat. Rec. (Hoboken) 292:1068-1077(2009).
[4]
DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=19819162; DOI=10.1016/j.cyto.2009.08.012;
Liu M., Liu T., Bordin A., Nerren J., Cohen N.;
"Activation of foal neutrophils at different ages by CpG
oligodeoxynucleotides and Rhodococcus equi.";
Cytokine 48:280-289(2009).
[5]
TISSUE SPECIFICITY.
PubMed=21292331; DOI=10.1016/j.vetimm.2010.12.008;
Quintana A.M., Landolt G.A., Annis K.M., Hussey G.S.;
"Immunological characterization of the equine airway epithelium and of
a primary equine airway epithelial cell culture model.";
Vet. Immunol. Immunopathol. 140:226-236(2011).
[6]
DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=22197007; DOI=10.1016/j.vetimm.2011.11.012;
Bordin A.I., Liu M., Nerren J.R., Buntain S.L., Brake C.N.,
Kogut M.H., Cohen N.D.;
"Neutrophil function of neonatal foals is enhanced in vitro by CpG
oligodeoxynucleotide stimulation.";
Vet. Immunol. Immunopathol. 145:290-297(2012).
[7]
INDUCTION.
PubMed=25066759; DOI=10.1016/j.intimp.2014.07.016;
Manuja A., Kumar P., Kumar R., Kumar B., Singha H., Sharma R.K.,
Yadav S.C.;
"CpG-ODN class C-mediated immunostimulation and its potential against
Trypanosoma evansi in equines.";
Int. Immunopharmacol. 22:366-370(2014).
[8]
INDUCTION.
PubMed=24560592; DOI=10.1016/j.vetmic.2014.01.018;
Soboll Hussey G., Ashton L.V., Quintana A.M., Lunn D.P.,
Goehring L.S., Annis K., Landolt G.;
"Innate immune responses of airway epithelial cells to infection with
equine herpesvirus-1.";
Vet. Microbiol. 170:28-38(2014).
[9]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=27270960; DOI=10.1111/evj.12597;
Kennedy R., Lappin D.F., Dixon P.M., Bennett D., Riggio M.P.;
"Gingival Toll-like receptor and cytokine messenger RNA levels in
equine periodontitis and oral health.";
Equine Vet. J. 49:294-299(2017).
[10] {ECO:0000244|PDB:3WPB, ECO:0000244|PDB:3WPC, ECO:0000244|PDB:3WPD}
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 26-817 OF UNLIGANDED AND IN
COMPLEX WITH AGONIST CPG-DNA AND INHIBITORY DNA, FUNCTION, SUBUNIT,
GLYCOSYLATION AT ASN-200; ASN-210; ASN-242; ASN-309; ASN-513; ASN-567;
ASN-694 AND ASN-731, DISULFIDE BONDS, AND MUTAGENESIS OF TRP-47;
TRP-96 AND PHE-108.
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. Upon
CpG stimulation, induces B-cell proliferation, activation,
survival and antibody production (By similarity).
{ECO:0000250|UniProtKB:Q9NR96, 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 (PubMed:25686612). 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:Q9EQU3,
ECO:0000250|UniProtKB:Q9NR96, ECO:0000269|PubMed:25686612}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-16145055, EBI-16145055;
-!- 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
{ECO:0000250|UniProtKB:Q9EQU3}. Cytoplasmic vesicle, phagosome
{ECO:0000250|UniProtKB:Q9EQU3}. Cell membrane
{ECO:0000269|PubMed:19548205}. Cytoplasm
{ECO:0000269|PubMed:19548205}. Nucleus
{ECO:0000269|PubMed:19548205}. 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}.
-!- TISSUE SPECIFICITY: Expressed in airway epithelium, vascular
endothelium and inflammatory cells in blood vessels of the lungs
(at protein level). Highly expressed in pulmonary intravascular
macrophages (PIMs) and to a lesser extent in alveolar macrophages,
neutrophiles, type-II alveolar epithelial cells and bronchial
epithelial cells of the lungs (at protein level)
(PubMed:19548205). High constitutive intracellular expression in
leukocytes including polymorphonuclear leukocytes (PMNs), CD4 and
CD8 T cells (at protein level) (PubMed:18462806). Expressed
throughout the respiratory tract including larynx, upper, middle
and lower trachea, and bronchus in isolated equine respiratory
epithelial cells (ERECs) and in fully differentiated ERECs
cultured at the air-fluid interface (AFI) (at protein level)
(PubMed:21292331). Constitutively expressed in peripheral blood
mononuclear cells (PBMCs), lymph nodes and spleen. The level of
expression in PBMCs is about 2- to 3-fold higher than that in
lymph nodes and spleen. Very low expression in liver, heart, lung,
kidney, small intestine, colon and stomach (PubMed:18462806). Low
expression in the airway tissue epithelium of the larynx, upper
trachea, middle tranchea, lower trachea, bronchus and spleen, and
more abundant expression in mesenteric lymph node. Not expressed
in fully differentiated bronchus epithelial cells cultured at the
AFI for four weeks (PubMed:21292331). Expressed in gingival tissue
(PubMed:27270960). {ECO:0000269|PubMed:18462806,
ECO:0000269|PubMed:19548205, ECO:0000269|PubMed:21292331,
ECO:0000269|PubMed:27270960}.
-!- DEVELOPMENTAL STAGE: Expression increases with age in neutrophils
of an individual foal aged between 2 to 56 days (PubMed:22197007).
Expression in neutrophils of a foal at age 1 day, another
different foal at age 56 days, and of an adult horse is
constitutive at a very low level (PubMed:19819162).
{ECO:0000269|PubMed:19819162, ECO:0000269|PubMed:22197007}.
-!- INDUCTION: By mitogen phytohaemagglutinin (PHA) in peripheral
blood mononuclear cells (PBMCs) (PubMed:18462806). By
lipopolysaccharide (LPS) in cells of the lung septa. This
induction is abolished by gadolinium chloride treatment which
depletes pulmonary intravascular macrophages (PIMs)
(PubMed:19548205). By synthetic class C cytidine-phosphate-
guanosine oligodeoxynucleotides (CpG-ODNs) in PBMCs
(PubMed:25066759). Synthetic class B CpG-ODN does not induce a
significant increase of expression in vitro in neutrophils of
foals aged between 2 to 56 days nor in adult horses
(PubMed:22197007, PubMed:19819162). Expression level in
neutrophils is not significantly changed by virulent strain of
R.equi bacterium (PubMed:19819162). Up-regulated by
neuropathogenic equine herpesvirus-1 (EHV-1) infection in fully
differentiated equine respiratory epithelial cells (ERECs)
cultured at the air-fluid interface (AFI) (PubMed:24560592). Up-
regulated in gingival tissue in individuals with equine
periodontal disease. 16-fold increase in expression at diseased
sites of the gums compared to healthy sites of the same animal
(PubMed:27270960). {ECO:0000269|PubMed:18462806,
ECO:0000269|PubMed:19548205, ECO:0000269|PubMed:19819162,
ECO:0000269|PubMed:22197007, ECO:0000269|PubMed:24560592,
ECO:0000269|PubMed:25066759, ECO:0000269|PubMed:27270960}.
-!- 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; DQ390541; ABD36388.2; -; mRNA.
EMBL; AAWR02008456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001075259.1; NM_001081790.2.
UniGene; Eca.12487; -.
PDB; 3WPB; X-ray; 2.40 A; A=26-817.
PDB; 3WPC; X-ray; 1.60 A; A/B=26-817.
PDB; 3WPD; X-ray; 2.75 A; A=26-817.
PDBsum; 3WPB; -.
PDBsum; 3WPC; -.
PDBsum; 3WPD; -.
ProteinModelPortal; Q2EEY0; -.
SMR; Q2EEY0; -.
DIP; DIP-61513N; -.
STRING; 9796.ENSECAP00000011919; -.
PaxDb; Q2EEY0; -.
Ensembl; ENSECAT00000014884; ENSECAP00000011919; ENSECAG00000014294.
GeneID; 100009693; -.
KEGG; ecb:100009693; -.
CTD; 54106; -.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000230468; -.
HOVERGEN; HBG018601; -.
KO; K10161; -.
OMA; CRRCDHA; -.
OrthoDB; EOG091G0BWK; -.
TreeFam; TF325595; -.
Proteomes; UP000002281; Chromosome 16.
Bgee; ENSECAG00000014294; -.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0032009; C:early phagosome; IEA:Ensembl.
GO; GO:0036019; C:endolysosome; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005149; F:interleukin-1 receptor binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0008329; F:signaling pattern recognition receptor activity; IDA: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; IDA: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; 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; IDA:UniProtKB.
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; IDA: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: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: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; 3.
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.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Disulfide bond; Endoplasmic reticulum; Endosome;
Glycoprotein; Immunity; Inflammatory response; Innate immunity;
Leucine-rich repeat; Lysosome; Membrane; Nucleus; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1031 Toll-like receptor 9. {ECO:0000255}.
/FTId=PRO_5009710270.
TOPO_DOM 26 817 Extracellular. {ECO:0000305}.
TRANSMEM 818 838 Helical. {ECO:0000255}.
TOPO_DOM 839 1031 Cytoplasmic. {ECO:0000305}.
REPEAT 62 85 LRR 1. {ECO:0000255}.
REPEAT 87 110 LRR 2. {ECO:0000255}.
REPEAT 122 147 LRR 3. {ECO:0000255}.
REPEAT 150 166 LRR 4. {ECO:0000255}.
REPEAT 167 190 LRR 5. {ECO:0000255}.
REPEAT 198 221 LRR 6. {ECO:0000255}.
REPEAT 223 242 LRR 7. {ECO:0000255}.
REPEAT 243 268 LRR 8. {ECO:0000255}.
REPEAT 283 306 LRR 9. {ECO:0000255}.
REPEAT 308 332 LRR 10. {ECO:0000255}.
REPEAT 333 356 LRR 11. {ECO:0000255}.
REPEAT 363 386 LRR 12. {ECO:0000255}.
REPEAT 390 413 LRR 13. {ECO:0000255}.
REPEAT 414 438 LRR 14. {ECO:0000255}.
REPEAT 470 494 LRR 15. {ECO:0000255}.
REPEAT 496 519 LRR 16. {ECO:0000255}.
REPEAT 520 543 LRR 17. {ECO:0000255}.
REPEAT 545 567 LRR 18. {ECO:0000255}.
REPEAT 574 598 LRR 19. {ECO:0000255}.
REPEAT 600 622 LRR 20. {ECO:0000255}.
REPEAT 627 650 LRR 21. {ECO:0000255}.
REPEAT 652 675 LRR 22. {ECO:0000255}.
REPEAT 676 699 LRR 23. {ECO:0000255}.
REPEAT 701 723 LRR 24. {ECO:0000255}.
REPEAT 724 747 LRR 25. {ECO:0000255}.
REPEAT 749 772 LRR 26. {ECO:0000255}.
DOMAIN 866 1014 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
REGION 47 51 Interaction with CpG-DNA.
{ECO:0000244|PDB:3WPC,
ECO:0000269|PubMed:25686612}.
REGION 72 77 Interaction with CpG-DNA.
{ECO:0000244|PDB:3WPC,
ECO:0000269|PubMed:25686612}.
REGION 95 109 Interaction with CpG-DNA.
{ECO:0000244|PDB:3WPC,
ECO:0000269|PubMed:25686612}.
REGION 179 181 Interaction with CpG-DNA.
{ECO:0000244|PDB:3WPC,
ECO:0000269|PubMed:25686612}.
BINDING 132 132 CpG-DNA. {ECO:0000244|PDB:3WPC,
ECO:0000269|PubMed:25686612}.
BINDING 152 152 CpG-DNA. {ECO:0000244|PDB:3WPC,
ECO:0000269|PubMed:25686612}.
BINDING 208 208 CpG-DNA. {ECO:0000244|PDB:3WPC,
ECO:0000269|PubMed:25686612}.
BINDING 262 262 CpG-DNA. {ECO:0000244|PDB:3WPC,
ECO:0000269|PubMed:25686612}.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPC,
ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:25686612}.
/FTId=CAR_5009710267.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPC,
ECO:0000244|PDB:3WPD,
ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:25686612}.
/FTId=CAR_5009710269.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPC,
ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:25686612}.
/FTId=CAR_5009710262.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPC,
ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:25686612}.
/FTId=CAR_5009710264.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 472 472 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPC,
ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:25686612}.
/FTId=CAR_5009710260.
CARBOHYD 567 567 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPC,
ECO:0000244|PDB:3WPD,
ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:25686612}.
/FTId=CAR_5009710265.
CARBOHYD 669 669 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 694 694 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPC,
ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:25686612}.
/FTId=CAR_5009710268.
CARBOHYD 731 731 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPC,
ECO:0000244|PDB:3WPD,
ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:25686612}.
/FTId=CAR_5009710266.
DISULFID 35 45 {ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPC,
ECO:0000244|PDB:3WPD,
ECO:0000269|PubMed:25686612}.
DISULFID 98 110 {ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPC,
ECO:0000244|PDB:3WPD,
ECO:0000269|PubMed:25686612}.
DISULFID 178 184 {ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPC,
ECO:0000244|PDB:3WPD,
ECO:0000269|PubMed:25686612}.
DISULFID 255 268 {ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPC,
ECO:0000244|PDB:3WPD,
ECO:0000269|PubMed:25686612}.
DISULFID 258 265 {ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPC,
ECO:0000244|PDB:3WPD,
ECO:0000269|PubMed:25686612}.
DISULFID 470 500 {ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPC,
ECO:0000244|PDB:3WPD,
ECO:0000269|PubMed:25686612}.
DISULFID 764 790 {ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPC,
ECO:0000244|PDB:3WPD,
ECO:0000269|PubMed:25686612}.
DISULFID 766 809 {ECO:0000244|PDB:3WPB,
ECO:0000244|PDB:3WPD,
ECO:0000269|PubMed:25686612}.
MUTAGEN 47 47 W->A: Significantly decreased binding to
agonist CpG-DNA.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 96 96 W->A: Significantly decreased binding to
agonist CpG-DNA.
{ECO:0000269|PubMed:25686612}.
MUTAGEN 108 108 F->A: Significantly decreased binding to
agonist CpG-DNA.
{ECO:0000269|PubMed:25686612}.
TURN 31 34 {ECO:0000244|PDB:3WPC}.
STRAND 35 38 {ECO:0000244|PDB:3WPC}.
TURN 39 41 {ECO:0000244|PDB:3WPC}.
STRAND 42 44 {ECO:0000244|PDB:3WPC}.
STRAND 58 60 {ECO:0000244|PDB:3WPD}.
HELIX 62 64 {ECO:0000244|PDB:3WPC}.
STRAND 66 69 {ECO:0000244|PDB:3WPC}.
STRAND 91 93 {ECO:0000244|PDB:3WPC}.
STRAND 96 98 {ECO:0000244|PDB:3WPB}.
TURN 101 103 {ECO:0000244|PDB:3WPC}.
TURN 116 121 {ECO:0000244|PDB:3WPC}.
STRAND 127 129 {ECO:0000244|PDB:3WPC}.
STRAND 147 149 {ECO:0000244|PDB:3WPC}.
TURN 160 162 {ECO:0000244|PDB:3WPC}.
STRAND 171 173 {ECO:0000244|PDB:3WPC}.
STRAND 177 179 {ECO:0000244|PDB:3WPC}.
TURN 192 197 {ECO:0000244|PDB:3WPC}.
STRAND 203 205 {ECO:0000244|PDB:3WPC}.
STRAND 223 226 {ECO:0000244|PDB:3WPC}.
HELIX 237 240 {ECO:0000244|PDB:3WPC}.
STRAND 247 250 {ECO:0000244|PDB:3WPC}.
STRAND 253 256 {ECO:0000244|PDB:3WPB}.
HELIX 258 260 {ECO:0000244|PDB:3WPC}.
TURN 277 282 {ECO:0000244|PDB:3WPC}.
STRAND 288 290 {ECO:0000244|PDB:3WPC}.
HELIX 301 303 {ECO:0000244|PDB:3WPC}.
TURN 304 306 {ECO:0000244|PDB:3WPC}.
STRAND 312 314 {ECO:0000244|PDB:3WPC}.
TURN 320 322 {ECO:0000244|PDB:3WPD}.
HELIX 323 326 {ECO:0000244|PDB:3WPC}.
TURN 329 332 {ECO:0000244|PDB:3WPC}.
STRAND 338 340 {ECO:0000244|PDB:3WPC}.
TURN 347 349 {ECO:0000244|PDB:3WPD}.
HELIX 358 362 {ECO:0000244|PDB:3WPC}.
STRAND 368 370 {ECO:0000244|PDB:3WPC}.
STRAND 376 379 {ECO:0000244|PDB:3WPC}.
TURN 381 384 {ECO:0000244|PDB:3WPC}.
HELIX 385 387 {ECO:0000244|PDB:3WPC}.
STRAND 395 397 {ECO:0000244|PDB:3WPC}.
HELIX 408 411 {ECO:0000244|PDB:3WPC}.
STRAND 419 421 {ECO:0000244|PDB:3WPC}.
STRAND 470 474 {ECO:0000244|PDB:3WPD}.
STRAND 476 478 {ECO:0000244|PDB:3WPC}.
HELIX 489 492 {ECO:0000244|PDB:3WPC}.
STRAND 499 502 {ECO:0000244|PDB:3WPC}.
STRAND 512 514 {ECO:0000244|PDB:3WPB}.
TURN 516 519 {ECO:0000244|PDB:3WPC}.
STRAND 525 527 {ECO:0000244|PDB:3WPC}.
TURN 538 543 {ECO:0000244|PDB:3WPC}.
STRAND 549 551 {ECO:0000244|PDB:3WPC}.
HELIX 556 559 {ECO:0000244|PDB:3WPC}.
HELIX 569 573 {ECO:0000244|PDB:3WPC}.
STRAND 579 581 {ECO:0000244|PDB:3WPC}.
STRAND 589 591 {ECO:0000244|PDB:3WPC}.
STRAND 596 599 {ECO:0000244|PDB:3WPC}.
STRAND 602 604 {ECO:0000244|PDB:3WPC}.
HELIX 610 614 {ECO:0000244|PDB:3WPC}.
TURN 617 625 {ECO:0000244|PDB:3WPC}.
STRAND 632 634 {ECO:0000244|PDB:3WPC}.
HELIX 645 648 {ECO:0000244|PDB:3WPC}.
STRAND 657 659 {ECO:0000244|PDB:3WPC}.
HELIX 670 675 {ECO:0000244|PDB:3WPC}.
STRAND 681 683 {ECO:0000244|PDB:3WPC}.
STRAND 705 707 {ECO:0000244|PDB:3WPC}.
TURN 718 723 {ECO:0000244|PDB:3WPC}.
STRAND 729 731 {ECO:0000244|PDB:3WPC}.
HELIX 742 745 {ECO:0000244|PDB:3WPC}.
HELIX 749 751 {ECO:0000244|PDB:3WPB}.
STRAND 753 756 {ECO:0000244|PDB:3WPC}.
HELIX 770 776 {ECO:0000244|PDB:3WPC}.
HELIX 778 780 {ECO:0000244|PDB:3WPC}.
HELIX 784 787 {ECO:0000244|PDB:3WPC}.
STRAND 789 793 {ECO:0000244|PDB:3WPC}.
HELIX 794 796 {ECO:0000244|PDB:3WPC}.
HELIX 804 807 {ECO:0000244|PDB:3WPB}.
SEQUENCE 1031 AA; 115592 MW; 1B6EA2A08EE693C9 CRC64;
MGPCHGALQP LSLLVQAAML AVALAQGTLP PFLPCELQPH GLVNCNWLFL KSVPHFSAAA
PRDNVTSLSL LSNRIHHLHD SDFAQLSNLQ KLNLKWNCPP AGLSPMHFPC HMTIEPNTFL
AVPTLEELNL SYNGITTVPA LPSSLVSLIL SRTNILQLDP TSLTGLHALR FLYMDGNCYY
KNPCGRALEV APGALLGLGN LTHLSLKYNN LTTVPRSLPP SLEYLLLSYN HIVTLAPEDL
ANLTALRVLD VGGNCRRCDH ARNPCVECPH KFPQLHSDTF SHLSRLEGLV LKDSSLYQLN
PRWFRGLGNL TVLDLSENFL YDCITKTKAF QGLAQLRRLN LSFNYHKKVS FAHLTLAPSF
GSLLSLQELD MHGIFFRSLS QKTLQPLARL PMLQRLYLQM NFINQAQLGI FKDFPGLRYI
DLSDNRISGA VEPVATTGEV DGGKKVWLTS RDLTPGPLDT PSSEDFMPSC KNLSFTLDLS
RNNLVTVQPE MFAQLSRLQC LRLSHNSISQ AVNGSQFVPL TSLQVLDLSH NKLDLYHGRS
FTELPRLEAL DLSYNSQPFS MRGVGHNLSF VAQLPTLRYL SLAHNGIHSR VSQQLCSTSL
WALDFSGNSL SQMWAEGDLY LRFFQGLRSL IRLDLSQNRL HTLLPCTLGN LPKSLQLLRL
RNNYLAFFNW SSLTLLPNLE TLDLAGNQLK ALSNGSLPSG TQLQRLDVSR NSIIFVVPGF
FALATRLREL NLSANALRTV EPSWFGFLAG SLEVLDVSAN PLHCACGAAF VDFLLQVQAA
VPGLPSRVKC GSPGQLQGRS IFAQDLRLCL DESLSWDCFG LSLLVVALGL AMPMLHHLCG
WDLWYCFHLG LAWLPRRGWQ RGADALSYDA FVVFDKAQSA VADWVYNELR VRLEERRGRR
ALRLCLEERD WLPGKTLFEN LWASVYSSRK MLFVLAHTDQ VSGLLRASFL LAQQRLLEDR
KDVVVLVILS PDARRSRYVR LRQRLCRQSV LFWPHQPSGQ RSFWAQLGMA LTRDNRHFYN
QNFCRGPTMA E


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