O00206 · TLR4_HUMAN
- ProteinToll-like receptor 4
- GeneTLR4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids839 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transmembrane receptor that functions as a pattern recognition receptor recognizing pathogen- and damage-associated molecular patterns (PAMPs and DAMPs) to induce innate immune responses via downstream signaling pathways (PubMed:10835634, PubMed:15809303, PubMed:16622205, PubMed:17292937, PubMed:17478729, PubMed:20037584, PubMed:20711192, PubMed:23880187, PubMed:27022195, PubMed:29038465).
At the plasma membrane, cooperates with LY96 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:27022195).
Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni2+ (PubMed:20711192).
Mechanistically, acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:10835634, PubMed:21393102, PubMed:27022195, PubMed:36945827, PubMed:9237759).
Alternatively, CD14-mediated TLR4 internalization via endocytosis is associated with the initiation of a MYD88-independent signaling via the TICAM1-TBK1-IRF3 axis leading to type I interferon production (PubMed:14517278).
In addition to the secretion of proinflammatory cytokines, initiates the activation of NLRP3 inflammasome and formation of a positive feedback loop between autophagy and NF-kappa-B signaling cascade (PubMed:32894580).
In complex with TLR6, promotes inflammation in monocytes/macrophages by associating with TLR6 and the receptor CD86 (PubMed:23880187).
Upon ligand binding, such as oxLDL or amyloid-beta 42, the TLR4:TLR6 complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway (PubMed:23880187).
In myeloid dendritic cells, vesicular stomatitis virus glycoprotein G but not LPS promotes the activation of IRF7, leading to type I IFN production in a CD14-dependent manner (PubMed:15265881, PubMed:23880187).
Required for the migration-promoting effects of ZG16B/PAUF on pancreatic cancer cells
At the plasma membrane, cooperates with LY96 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:27022195).
Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni2+ (PubMed:20711192).
Mechanistically, acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:10835634, PubMed:21393102, PubMed:27022195, PubMed:36945827, PubMed:9237759).
Alternatively, CD14-mediated TLR4 internalization via endocytosis is associated with the initiation of a MYD88-independent signaling via the TICAM1-TBK1-IRF3 axis leading to type I interferon production (PubMed:14517278).
In addition to the secretion of proinflammatory cytokines, initiates the activation of NLRP3 inflammasome and formation of a positive feedback loop between autophagy and NF-kappa-B signaling cascade (PubMed:32894580).
In complex with TLR6, promotes inflammation in monocytes/macrophages by associating with TLR6 and the receptor CD86 (PubMed:23880187).
Upon ligand binding, such as oxLDL or amyloid-beta 42, the TLR4:TLR6 complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway (PubMed:23880187).
In myeloid dendritic cells, vesicular stomatitis virus glycoprotein G but not LPS promotes the activation of IRF7, leading to type I IFN production in a CD14-dependent manner (PubMed:15265881, PubMed:23880187).
Required for the migration-promoting effects of ZG16B/PAUF on pancreatic cancer cells
Miscellaneous
His-456 and His-458 are found in TLR4 of human and several other primate species and may be responsible for inflammatory responses triggered by nickel (Ni2+).
Ni2+ may cross-link the two receptor monomers through specific histidines, triggering the formation of a dimer that structurally resembles that induced by LPS. This process may be the basis for the development of contact allergy to Ni2+. A mouse model of contact allergy to Ni2+ in which TLR4-deficient mice expresses human TLR4 has been proposed.
Ni2+ may cross-link the two receptor monomers through specific histidines, triggering the formation of a dimer that structurally resembles that induced by LPS. This process may be the basis for the development of contact allergy to Ni2+. A mouse model of contact allergy to Ni2+ in which TLR4-deficient mice expresses human TLR4 has been proposed.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameToll-like receptor 4
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00206
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: Upon complex formation with CD36 and TLR6, internalized through dynamin-dependent endocytosis (PubMed:20037584).
Colocalizes with RFTN1 at cell membrane and then together with RFTN1 moves to endosomes, upon lipopolysaccharide stimulation. Co-localizes with ZG16B/PAUF at the cell membrane of pancreatic cancer cells (PubMed:36232715).
Colocalizes with RFTN1 at cell membrane and then together with RFTN1 moves to endosomes, upon lipopolysaccharide stimulation. Co-localizes with ZG16B/PAUF at the cell membrane of pancreatic cancer cells (PubMed:36232715).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 24-631 | Extracellular | ||||
Sequence: ESWEPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNEGNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFPTLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEHLDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQCQLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNK | ||||||
Transmembrane | 632-652 | Helical | ||||
Sequence: TIIGVSVLSVLVVSVVAVLVY | ||||||
Topological domain | 653-839 | Cytoplasmic | ||||
Sequence: KFYFHLMLLAGCIKYGRGENIYDAFVIYSSQDEDWVRNELVKNLEEGVPPFQLCLHYRDFIPGVAIAANIIHEGFHKSRKVIVVVSQHFIQSRWCIFEYEIAQTWQFLSSRAGIIFIVLQKVEKTLLRQQVELYRLLSRNTYLEWEDSVLGRHIFWRRLRKALLDGKSWNPEGTVGTGCNWQEATSI |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_021977 | 175 | in dbSNP:rs16906079 | |||
Sequence: T → A | ||||||
Natural variant | VAR_018729 | 188 | in dbSNP:rs5030713 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_018730 | 246 | in dbSNP:rs5030714 | |||
Sequence: C → S | ||||||
Natural variant | VAR_074187 | 287 | ||||
Sequence: E → D | ||||||
Natural variant | VAR_012739 | 299 | in allele TLR4*B; reduced LPS-response; associated with an increased risk for age-related macular degeneration in Caucasian carriers; dbSNP:rs4986790 | |||
Sequence: D → G | ||||||
Natural variant | VAR_047563 | 306 | in dbSNP:rs2770145 | |||
Sequence: C → W | ||||||
Natural variant | VAR_047564 | 310 | in dbSNP:rs2770144 | |||
Sequence: V → G | ||||||
Natural variant | VAR_018731 | 329 | in dbSNP:rs5030715 | |||
Sequence: N → S | ||||||
Natural variant | VAR_020334 | 342 | in dbSNP:rs5031050 | |||
Sequence: F → Y | ||||||
Natural variant | VAR_037668 | 385 | in dbSNP:rs11536884 | |||
Sequence: L → F | ||||||
Natural variant | VAR_012740 | 399 | in allele TLR4*B; reduced LPS-response; dbSNP:rs4986791 | |||
Sequence: T → I | ||||||
Natural variant | VAR_020335 | 400 | in dbSNP:rs4987233 | |||
Sequence: S → N | ||||||
Mutagenesis | 431 | Partially diminishes NF-kappa-B activation induced by Ni2+. Strongly reduces NF-kappa-B activation induced by Ni2+; when associated with A-456 or A-458. | ||||
Sequence: H → A | ||||||
Natural variant | VAR_018732 | 443 | in dbSNP:rs5030716 | |||
Sequence: F → L | ||||||
Mutagenesis | 456 | Partially diminishes NF-kappa-B activation induced by Ni2+. Strongly reduces NF-kappa-B activation induced by Ni2+; when associated with A-431. Suppresses NF-kappa-B activation induced by Ni2+; when associated with A-458. | ||||
Sequence: H → A | ||||||
Mutagenesis | 458 | Partially diminishes NF-kappa-B activation induced by Ni2+. Strongly reduces NF-kappa-B activation induced by Ni2+; when associated with A-431. Suppresses NF-kappa-B activation induced by Ni2+; when associated with A-456. | ||||
Sequence: H → A | ||||||
Natural variant | VAR_018733 | 474 | in dbSNP:rs5030718 | |||
Sequence: E → K | ||||||
Natural variant | VAR_018734 | 510 | in dbSNP:rs5030719 | |||
Sequence: Q → H | ||||||
Mutagenesis | 526 | Abolishes LPS-response and prevents the cell surface expression. | ||||
Sequence: N → A | ||||||
Mutagenesis | 575 | Abolishes LPS-response and prevents the cell surface expression. | ||||
Sequence: N → A | ||||||
Natural variant | VAR_018735 | 694 | in dbSNP:rs5030722 | |||
Sequence: K → R | ||||||
Mutagenesis | 697 | Abolishes LPS-response. | ||||
Sequence: E → R | ||||||
Mutagenesis | 710 | Abolishes LPS-response. | ||||
Sequence: R → E | ||||||
Mutagenesis | 711 | Abolishes LPS-response. | ||||
Sequence: D → K | ||||||
Mutagenesis | 714 | Abolishes MYD88-binding and LPS-response. | ||||
Sequence: P → H, R, or E | ||||||
Natural variant | VAR_018736 | 763 | in dbSNP:rs5030723 | |||
Sequence: R → H | ||||||
Natural variant | VAR_018737 | 834 | ||||
Sequence: Q → H |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,379 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MMSASRLAGTLIPAMAFLSCVRP | ||||||
Chain | PRO_0000034722 | 24-839 | Toll-like receptor 4 | |||
Sequence: ESWEPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNEGNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFPTLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEHLDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQCQLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNKTIIGVSVLSVLVVSVVAVLVYKFYFHLMLLAGCIKYGRGENIYDAFVIYSSQDEDWVRNELVKNLEEGVPPFQLCLHYRDFIPGVAIAANIIHEGFHKSRKVIVVVSQHFIQSRWCIFEYEIAQTWQFLSSRAGIIFIVLQKVEKTLLRQQVELYRLLSRNTYLEWEDSVLGRHIFWRRLRKALLDGKSWNPEGTVGTGCNWQEATSI | ||||||
Disulfide bond | 29↔40 | |||||
Sequence: CVEVVPNITYQC | ||||||
Glycosylation | 35 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 173 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 205 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 281↔306 | |||||
Sequence: CNLTIEEFRLAYLDYYLDDIIDLFNC | ||||||
Glycosylation | 282 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 309 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 390↔391 | |||||
Sequence: CC | ||||||
Glycosylation | 497 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 526 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 575 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 583↔609 | |||||
Sequence: CTCEHQSFLQWIKDQRQLLVEVERMEC | ||||||
Disulfide bond | 585↔627 | |||||
Sequence: CEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITC | ||||||
Glycosylation | 624 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 630 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated. Glycosylation of Asn-526 and Asn-575 seems to be necessary for the expression of TLR4 on the cell surface and the LPS-response. Likewise, mutants lacking two or more of the other N-glycosylation sites were deficient in interaction with LPS.
Phosphorylated on tyrosine residues by LYN after binding lipopolysaccharide.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in placenta, spleen and peripheral blood leukocytes (PubMed:9237759, PubMed:9435236).
Detected in monocytes, macrophages, dendritic cells and several types of T-cells (PubMed:27022195, PubMed:9237759).
Expressed in pancreatic cancer cells but not in normal pancreatic cells (at protein level) (PubMed:36232715).
Detected in monocytes, macrophages, dendritic cells and several types of T-cells (PubMed:27022195, PubMed:9237759).
Expressed in pancreatic cancer cells but not in normal pancreatic cells (at protein level) (PubMed:36232715).
Induction
By LPS in plasmacytoid dendritic cells.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 (PubMed:11274165).
Binding to bacterial LPS leads to homodimerization. Interacts with LY96 via the extracellular domain (PubMed:17803912, PubMed:19252480).
Interacts with MYD88 (PubMed:36232715).
Interacts (via TIR domains) with TIRAP (By similarity).
Interacts with TICAM2 (PubMed:14519765, PubMed:25736436).
Interacts with NOX4 (PubMed:15356101).
Interacts with CNPY3 (By similarity).
Interacts with HSP90B1. The interaction with both CNPY3 and HSP90B1 is required for proper folding in the endoplasmic reticulum. Interacts with MAP3K21; this interaction leads to negative regulation of TLR4 signaling (PubMed:21602844).
Interacts with CD36, following CD36 stimulation by oxLDL or amyloid-beta 42, and forms a heterodimer with TLR6 (PubMed:20037584).
The trimeric complex is internalized and triggers inflammatory response. LYN kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Interacts with TICAM1 in response to LPS in a WDFY1-dependent manner (PubMed:25736436, PubMed:36232715).
Interacts with WDFY1 in response to LPS (By similarity).
Interacts with SMPDL3B (By similarity).
Interacts with CEACAM1; upon lipopolysaccharide stimulation, forms a complex including TLR4 and the phosphorylated form of SYK and CEACAM1, which in turn, recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome (By similarity).
Interacts with RFTN1; the interaction occurs in response to lipopolysaccharide stimulation (PubMed:27022195).
Interacts with SCIMP; the interaction occurs in response to lipopolysaccharide stimulation and is enhanced by phosphorylation of SCIMP by LYN (By similarity).
This interaction facilitates the phosphorylation of TLR4 by LYN which elicits a selective cytokine response in macrophages (By similarity).
Interacts with TRAF3IP3 (PubMed:30573680).
Interacts with TREM1; this interaction enhances TLR4-mediated inflammatory response (PubMed:17098818, PubMed:21393102).
Interacts with ZG16B/PAUF (PubMed:36232715).
Interacts with CD82; this interaction inhibits TLR4-mediated signaling pathway (PubMed:36945827).
Interacts with neutrophil recruitment protein from Aedes aegypti saliva; the interaction probably promotes activation of canonical NF-kappa-B signaling in skin-resident macrophages and subsequent expression of neutrophil chemoattractants (PubMed:38378891).
Binding to bacterial LPS leads to homodimerization. Interacts with LY96 via the extracellular domain (PubMed:17803912, PubMed:19252480).
Interacts with MYD88 (PubMed:36232715).
Interacts (via TIR domains) with TIRAP (By similarity).
Interacts with TICAM2 (PubMed:14519765, PubMed:25736436).
Interacts with NOX4 (PubMed:15356101).
Interacts with CNPY3 (By similarity).
Interacts with HSP90B1. The interaction with both CNPY3 and HSP90B1 is required for proper folding in the endoplasmic reticulum. Interacts with MAP3K21; this interaction leads to negative regulation of TLR4 signaling (PubMed:21602844).
Interacts with CD36, following CD36 stimulation by oxLDL or amyloid-beta 42, and forms a heterodimer with TLR6 (PubMed:20037584).
The trimeric complex is internalized and triggers inflammatory response. LYN kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Interacts with TICAM1 in response to LPS in a WDFY1-dependent manner (PubMed:25736436, PubMed:36232715).
Interacts with WDFY1 in response to LPS (By similarity).
Interacts with SMPDL3B (By similarity).
Interacts with CEACAM1; upon lipopolysaccharide stimulation, forms a complex including TLR4 and the phosphorylated form of SYK and CEACAM1, which in turn, recruits PTPN6 that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome (By similarity).
Interacts with RFTN1; the interaction occurs in response to lipopolysaccharide stimulation (PubMed:27022195).
Interacts with SCIMP; the interaction occurs in response to lipopolysaccharide stimulation and is enhanced by phosphorylation of SCIMP by LYN (By similarity).
This interaction facilitates the phosphorylation of TLR4 by LYN which elicits a selective cytokine response in macrophages (By similarity).
Interacts with TRAF3IP3 (PubMed:30573680).
Interacts with TREM1; this interaction enhances TLR4-mediated inflammatory response (PubMed:17098818, PubMed:21393102).
Interacts with ZG16B/PAUF (PubMed:36232715).
Interacts with CD82; this interaction inhibits TLR4-mediated signaling pathway (PubMed:36945827).
Interacts with neutrophil recruitment protein from Aedes aegypti saliva; the interaction probably promotes activation of canonical NF-kappa-B signaling in skin-resident macrophages and subsequent expression of neutrophil chemoattractants (PubMed:38378891).
(Microbial infection) In case of infection, interacts with uropathogenic E.coli protein TcpC.
(Microbial infection) In case of infection, interacts with B.melitensis protein TcpB; TcpB abolishes the TLR4-TIRAP interaction in vitro.
(Microbial infection) Interacts with ebolavirus protein GP; this interaction leads to the production of proinflammatory cytokines and suppressor of cytokine signaling 1/SOCS1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00206 | ADIPOR1 Q96A54 | 2 | EBI-528701, EBI-1632076 | |
BINARY | O00206 | LY96 Q9Y6Y9 | 7 | EBI-528701, EBI-1539247 | |
BINARY | O00206 | MBL2 P11226 | 2 | EBI-528701, EBI-5325353 | |
BINARY | O00206 | MYD88 Q99836 | 4 | EBI-528701, EBI-447677 | |
BINARY | O00206 | NOX4 Q9NPH5 | 4 | EBI-528701, EBI-11301574 | |
BINARY | O00206 | SIGLEC5 O15389 | 2 | EBI-528701, EBI-750381 | |
BINARY | O00206 | SIGLEC6 O43699-3 | 2 | EBI-528701, EBI-12161783 | |
BINARY | O00206 | SIGLEC9 Q9Y336 | 2 | EBI-528701, EBI-12857926 | |
BINARY | O00206 | TICAM2 Q86XR7 | 3 | EBI-528701, EBI-525927 | |
BINARY | O00206 | TIRAP P58753 | 6 | EBI-528701, EBI-528644 | |
BINARY | O00206 | TLR4 O00206 | 3 | EBI-528701, EBI-528701 | |
BINARY | O00206 | TLR6 Q9Y2C9 | 2 | EBI-528701, EBI-13940779 | |
BINARY | O00206 | TNC P24821 | 4 | EBI-528701, EBI-9979894 | |
XENO | O00206-1 | DERP2 P49278 | 3 | EBI-15745059, EBI-15745025 | |
BINARY | O00206-1 | LY96 Q9Y6Y9 | 5 | EBI-15745059, EBI-1539247 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 55-76 | LRR 1 | ||||
Sequence: STKNLDLSFNPLRHLGSYSFFS | ||||||
Repeat | 79-100 | LRR 2 | ||||
Sequence: ELQVLDLSRCEIQTIEDGAYQS | ||||||
Repeat | 103-124 | LRR 3 | ||||
Sequence: HLSTLILTGNPIQSLALGAFSG | ||||||
Repeat | 127-148 | LRR 4 | ||||
Sequence: SLQKLVAVETNLASLENFPIGH | ||||||
Repeat | 151-172 | LRR 5 | ||||
Sequence: TLKELNVAHNLIQSFKLPEYFS | ||||||
Repeat | 176-199 | LRR 6 | ||||
Sequence: NLEHLDLSSNKIQSIYCTDLRVLH | ||||||
Repeat | 205-225 | LRR 7 | ||||
Sequence: NLSLDLSLNPMNFIQPGAFKE | ||||||
Repeat | 227-247 | LRR 8 | ||||
Sequence: RLHKLTLRNNFDSLNVMKTCI | ||||||
Repeat | 331-351 | LRR 9 | ||||
Sequence: GWQHLELVNCKFGQFPTLKLK | ||||||
Repeat | 352-373 | LRR 10 | ||||
Sequence: SLKRLTFTSNKGGNAFSEVDLP | ||||||
Repeat | 374-394 | LRR 11 | ||||
Sequence: SLEFLDLSRNGLSFKGCCSQS | ||||||
Repeat | 400-422 | LRR 12 | ||||
Sequence: SLKYLDLSFNGVITMSSNFLGLE | ||||||
Repeat | 423-444 | LRR 13 | ||||
Sequence: QLEHLDFQHSNLKQMSEFSVFL | ||||||
Repeat | 448-456 | LRR 14 | ||||
Sequence: NLIYLDISH | ||||||
Repeat | 472-495 | LRR 15 | ||||
Sequence: SLEVLKMAGNSFQENFLPDIFTEL | ||||||
Repeat | 497-518 | LRR 16 | ||||
Sequence: NLTFLDLSQCQLEQLSPTAFNS | ||||||
Repeat | 521-542 | LRR 17 | ||||
Sequence: SLQVLNMSHNNFFSLDTFPYKC | ||||||
Repeat | 545-565 | LRR 18 | ||||
Sequence: SLQVLDYSLNHIMTSKKQELQ | ||||||
Domain | 579-629 | LRRCT | ||||
Sequence: NDFACTCEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQM | ||||||
Domain | 672-815 | TIR | ||||
Sequence: NIYDAFVIYSSQDEDWVRNELVKNLEEGVPPFQLCLHYRDFIPGVAIAANIIHEGFHKSRKVIVVVSQHFIQSRWCIFEYEIAQTWQFLSSRAGIIFIVLQKVEKTLLRQQVELYRLLSRNTYLEWEDSVLGRHIFWRRLRKAL |
Domain
The TIR domain mediates interaction with NOX4.
Sequence similarities
Belongs to the Toll-like receptor family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing.
O00206-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length839
- Mass (Da)95,680
- Last updated1998-01-01 v2
- Checksum92C48F55821133E8
O00206-2
- Name2
- Differences from canonical
- 1-40: Missing
O00206-3
- Name3
- Differences from canonical
- 1-200: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y7P4 | A0A2R8Y7P4_HUMAN | TLR4 | 32 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_035794 | 1-40 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_035793 | 1-200 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 73 | in Ref. 11; ABU41664 | ||||
Sequence: S → R | ||||||
Sequence conflict | 400 | in Ref. 7; BAF82742 | ||||
Sequence: S → C | ||||||
Sequence conflict | 581 | in Ref. 7; BAG64706 | ||||
Sequence: F → S |
Polymorphism
Allele TLR4*B (Gly-299, Ile-399) is associated with a blunted response to inhaled LPS.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U93091 EMBL· GenBank· DDBJ | AAC80227.1 EMBL· GenBank· DDBJ | mRNA | ||
AB445638 EMBL· GenBank· DDBJ | BAG55035.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ018107 EMBL· GenBank· DDBJ | AAY82267.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ018108 EMBL· GenBank· DDBJ | AAY82268.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ018109 EMBL· GenBank· DDBJ | AAY82269.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK290053 EMBL· GenBank· DDBJ | BAF82742.1 EMBL· GenBank· DDBJ | mRNA | ||
AK293068 EMBL· GenBank· DDBJ | BAF85757.1 EMBL· GenBank· DDBJ | mRNA | ||
AK303730 EMBL· GenBank· DDBJ | BAG64706.1 EMBL· GenBank· DDBJ | mRNA | ||
AL160272 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471090 EMBL· GenBank· DDBJ | EAW87448.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471090 EMBL· GenBank· DDBJ | EAW87451.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC117422 EMBL· GenBank· DDBJ | AAI17423.1 EMBL· GenBank· DDBJ | mRNA | ||
EF535831 EMBL· GenBank· DDBJ | ABU41662.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EF535832 EMBL· GenBank· DDBJ | ABU41663.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
EF535833 EMBL· GenBank· DDBJ | ABU41664.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF177765 EMBL· GenBank· DDBJ | AAF05316.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF177766 EMBL· GenBank· DDBJ | AAF07823.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172171 EMBL· GenBank· DDBJ | AAF89753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172169 EMBL· GenBank· DDBJ | AAF89753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF172170 EMBL· GenBank· DDBJ | AAF89753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U88880 EMBL· GenBank· DDBJ | AAC34135.1 EMBL· GenBank· DDBJ | mRNA |