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Protein

Toll-like receptor 9

Gene

TLR9

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-like receptor 9
Alternative name(s):
CD_antigen: CD289
Gene namesi
Name:TLR9
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 815791ExtracellularSequence analysisAdd
BLAST
Transmembranei816 – 83621HelicalSequence analysisAdd
BLAST
Topological domaini837 – 1029193CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 10291005Toll-like receptor 9PRO_0000227006Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence analysis
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence analysis
Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence analysis
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence analysis
Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence analysis
Glycosylationi472 – 4721N-linked (GlcNAc...)Sequence analysis
Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence analysis
Glycosylationi565 – 5651N-linked (GlcNAc...)Sequence analysis
Glycosylationi667 – 6671N-linked (GlcNAc...)Sequence analysis
Glycosylationi692 – 6921N-linked (GlcNAc...)Sequence analysis
Glycosylationi729 – 7291N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ5I2M5.
PRIDEiQ5I2M5.

Interactioni

Subunit structurei

Interacts with MYD88 via their respective TIR domains. Interacts with BTK. 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.By similarity

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-61514N.
STRINGi9913.ENSBTAP00000024223.

Structurei

Secondary structure

1
1029
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni30 – 334Combined sources
Beta strandi34 – 363Combined sources
Beta strandi41 – 433Combined sources
Helixi61 – 633Combined sources
Beta strandi66 – 683Combined sources
Beta strandi90 – 923Combined sources
Turni100 – 1023Combined sources
Turni115 – 1206Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi146 – 1483Combined sources
Helixi160 – 1623Combined sources
Beta strandi170 – 1723Combined sources
Beta strandi176 – 1783Combined sources
Turni191 – 1966Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi222 – 2254Combined sources
Helixi236 – 2394Combined sources
Beta strandi246 – 2494Combined sources
Helixi276 – 2794Combined sources
Beta strandi287 – 2893Combined sources
Helixi300 – 3034Combined sources
Beta strandi311 – 3133Combined sources
Turni319 – 3213Combined sources
Helixi322 – 3254Combined sources
Turni328 – 3314Combined sources
Beta strandi337 – 3393Combined sources
Helixi357 – 3604Combined sources
Beta strandi367 – 3693Combined sources
Beta strandi375 – 3784Combined sources
Turni380 – 3834Combined sources
Helixi384 – 3885Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi403 – 4053Combined sources
Helixi407 – 4126Combined sources
Beta strandi418 – 4203Combined sources
Beta strandi474 – 4763Combined sources
Helixi487 – 4904Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi523 – 5253Combined sources
Turni536 – 5416Combined sources
Beta strandi547 – 5493Combined sources
Helixi554 – 5574Combined sources
Helixi567 – 5715Combined sources
Beta strandi577 – 5793Combined sources
Beta strandi587 – 5893Combined sources
Beta strandi595 – 5973Combined sources
Beta strandi600 – 6023Combined sources
Helixi608 – 6114Combined sources
Turni615 – 62410Combined sources
Beta strandi630 – 6323Combined sources
Helixi643 – 6475Combined sources
Beta strandi654 – 6574Combined sources
Helixi669 – 6735Combined sources
Beta strandi679 – 6813Combined sources
Beta strandi703 – 7053Combined sources
Beta strandi727 – 7293Combined sources
Helixi740 – 7423Combined sources
Beta strandi752 – 7543Combined sources
Helixi768 – 7747Combined sources
Turni775 – 7784Combined sources
Beta strandi788 – 7903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WPEX-ray2.38A25-815[»]
ProteinModelPortaliQ5I2M5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati61 – 8424LRR 1Add
BLAST
Repeati86 – 10924LRR 2Add
BLAST
Repeati121 – 14626LRR 3Add
BLAST
Repeati149 – 16517LRR 4Add
BLAST
Repeati166 – 18924LRR 5Add
BLAST
Repeati197 – 22024LRR 6Add
BLAST
Repeati222 – 24120LRR 7Add
BLAST
Repeati242 – 26726LRR 8Add
BLAST
Repeati282 – 30524LRR 9Add
BLAST
Repeati307 – 33125LRR 10Add
BLAST
Repeati332 – 35524LRR 11Add
BLAST
Repeati362 – 38524LRR 12Add
BLAST
Repeati389 – 41224LRR 13Add
BLAST
Repeati414 – 43926LRR 14Add
BLAST
Repeati469 – 49224LRR 15Add
BLAST
Repeati494 – 51724LRR 16Add
BLAST
Repeati518 – 54124LRR 17Add
BLAST
Repeati543 – 57028LRR 18Add
BLAST
Repeati572 – 59625LRR 19Add
BLAST
Repeati598 – 62023LRR 20Add
BLAST
Repeati625 – 64824LRR 21Add
BLAST
Repeati650 – 67324LRR 22Add
BLAST
Repeati674 – 69724LRR 23Add
BLAST
Repeati699 – 72123LRR 24Add
BLAST
Repeati722 – 74524LRR 25Add
BLAST
Repeati747 – 77024LRR 26Add
BLAST
Domaini864 – 1012149TIRPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi854 – 8596Poly-Arg

Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated
Contains 26 LRR (leucine-rich) repeats.Curated
Contains 1 TIR domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000230468.
HOVERGENiHBG018601.
InParanoidiQ5I2M5.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 4 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027181. TLR9.
[Graphical view]
PANTHERiPTHR24373:SF37. PTHR24373:SF37. 3 hits.
PfamiPF13516. LRR_6. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 17 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 18 hits.
PS50104. TIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5I2M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPYCAPHPL SLLVQAAALA AALAEGTLPA FLPCELQPHG QVDCNWLFLK
60 70 80 90 100
SVPHFSAGAP RANVTSLSLI SNRIHHLHDS DFVHLSNLRV LNLKWNCPPA
110 120 130 140 150
GLSPMHFPCR MTIEPNTFLA VPTLEELNLS YNGITTVPAL PSSLVSLSLS
160 170 180 190 200
HTSILVLGPT HFTGLHALRF LYMDGNCYYM NPCPRALEVA PGALLGLGNL
210 220 230 240 250
THLSLKYNNL TEVPRRLPPS LDTLLLSYNH IVTLAPEDLA NLTALRVLDV
260 270 280 290 300
GGNCRRCDHA RNPCRECPKN FPKLHPDTFS HLSRLEGLVL KDSSLYKLEK
310 320 330 340 350
DWFRGLGRLQ VLDLSENFLY DYITKTTIFN DLTQLRRLNL SFNYHKKVSF
360 370 380 390 400
AHLHLASSFG SLVSLEKLDM HGIFFRSLTN ITLQSLTRLP KLQSLHLQLN
410 420 430 440 450
FINQAQLSIF GAFPSLLFVD LSDNRISGAA TPAAALGEVD SRVEVWRLPR
460 470 480 490 500
GLAPGPLDAV SSKDFMPSCN LNFTLDLSRN NLVTIQQEMF TRLSRLQCLR
510 520 530 540 550
LSHNSISQAV NGSQFVPLTS LRVLDLSHNK LDLYHGRSFT ELPQLEALDL
560 570 580 590 600
SYNSQPFSMQ GVGHNLSFVA QLPSLRYLSL AHNGIHSRVS QKLSSASLRA
610 620 630 640 650
LDFSGNSLSQ MWAEGDLYLC FFKGLRNLVQ LDLSENHLHT LLPRHLDNLP
660 670 680 690 700
KSLRQLRLRD NNLAFFNWSS LTVLPRLEAL DLAGNQLKAL SNGSLPPGIR
710 720 730 740 750
LQKLDVSSNS IGFVIPGFFV RATRLIELNL SANALKTVDP SWFGSLAGTL
760 770 780 790 800
KILDVSANPL HCACGAAFVD FLLERQEAVP GLSRRVTCGS PGQLQGRSIF
810 820 830 840 850
TQDLRLCLDE TLSLDCFGLS LLMVALGLAV PMLHHLCGWD LWYCFHLCLA
860 870 880 890 900
HLPRRRRQRG EDTLLYDAVV VFDKVQSAVA DWVYNELRVQ LEERRGRRAL
910 920 930 940 950
RLCLEERDWL PGKTLFENLW ASVYSSRKTM FVLDHTDRVS GLLRASFLLA
960 970 980 990 1000
QQRLLEDRKD VVVLVILRPA AYRSRYVRLR QRLCRQSVLL WPHQPSGQGS
1010 1020
FWANLGIALT RDNRHFYNRN FCRGPTTAE
Length:1,029
Mass (Da):115,407
Last modified:February 15, 2005 - v1
Checksum:i02BD73CFE59E1F8D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY859726 mRNA. Translation: AAW50954.1.
UniGeneiBt.12810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY859726 mRNA. Translation: AAW50954.1.
UniGeneiBt.12810.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WPEX-ray2.38A25-815[»]
ProteinModelPortaliQ5I2M5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61514N.
STRINGi9913.ENSBTAP00000024223.

Proteomic databases

PaxDbiQ5I2M5.
PRIDEiQ5I2M5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG4641. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000230468.
HOVERGENiHBG018601.
InParanoidiQ5I2M5.

Family and domain databases

Gene3Di3.40.50.10140. 1 hit.
3.80.10.10. 4 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000157. TIR_dom.
IPR027181. TLR9.
[Graphical view]
PANTHERiPTHR24373:SF37. PTHR24373:SF37. 3 hits.
PfamiPF13516. LRR_6. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 17 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF52200. SSF52200. 1 hit.
PROSITEiPS51450. LRR. 18 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Bovine toll-like receptor 9: a comparative analysis of molecular structure, function and expression."
    Griebel P.J., Brownlie R., Manuja A., Nichani A., Mookherjee N., Popowych Y., Mutwiri G., Hecker R., Babiuk L.A.
    Vet. Immunol. Immunopathol. 108:11-16(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Spleen.

Entry informationi

Entry nameiTLR9_BOVIN
AccessioniPrimary (citable) accession number: Q5I2M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: February 15, 2005
Last modified: May 11, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.