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Entry version 136 (02 Jun 2021)
Sequence version 1 (01 Nov 1999)
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Protein

Toll-like receptor 4

Gene

TLR4

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity).

Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate. In complex with TLR6, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. Binds electronegative LDL (LDL-) and mediates the cytokine release induced by LDL- (By similarity).

Activated by the signaling pathway regulator NMI which acts as damage-associated molecular patterns (DAMPs) in response to cell injury or pathogen invasion, therefore promoting nuclear factor NF-kappa-B activation (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei748PROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Receptor
Biological processImmunity, Inflammatory response, Innate immunity
LigandNAD

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Toll-like receptor 4 (EC:3.2.2.6PROSITE-ProRule annotation)
Alternative name(s):
CD_antigen: CD284
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TLR4
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10029 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeCricetulus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini26 – 629ExtracellularSequence analysisAdd BLAST604
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei630 – 650HelicalSequence analysisAdd BLAST21
Topological domaini651 – 838CytoplasmicSequence analysisAdd BLAST188

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003471826 – 838Toll-like receptor 4Add BLAST813

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi28 ↔ 39By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi34N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi115N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi172N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi204N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi237N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi280 ↔ 304By similarity
Glycosylationi307N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi388 ↔ 389By similarity
Glycosylationi492N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi495N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi524N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi572N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi580 ↔ 606By similarity
Disulfide bondi582 ↔ 625By similarity
Glycosylationi622N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on tyrosine residues by LYN after binding lipopolysaccharide.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in macrophages.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4. Binding to bacterial LPS leads to homodimerization.

Interacts with LY96 via the extracellular domain.

Interacts with MYD88 and TIRAP via their respective TIR domains.

Interacts with TICAM2.

Interacts with NOX4.

Interacts with CNPY3 and HSP90B1; this interaction is required for proper folding in the endoplasmic reticulum.

Interacts with MAP3K21; this interaction leads to negative regulation of TLR4 signaling.

Interacts with CD36, following CD36 stimulation by oxLDL or amyloid-beta 42, and forms a heterodimer with TLR6. 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.

Interacts with WDFY1 in response to LPS.

Interacts with SMPDL3B.

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.

Interacts with RFTN1; the interaction occurs in response to lipopolysaccharide stimulation.

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 (By similarity).

Interacts with TREM1; this interaction enhances TLR4-mediated inflammatory response (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10029.NP_001233691.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9WV82

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini26 – 53LRRNTAdd BLAST28
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati54 – 75LRR 1Add BLAST22
Repeati78 – 99LRR 2Add BLAST22
Repeati102 – 123LRR 3Add BLAST22
Repeati126 – 147LRR 4Add BLAST22
Repeati150 – 171LRR 5Add BLAST22
Repeati175 – 198LRR 6Add BLAST24
Repeati204 – 224LRR 7Add BLAST21
Repeati226 – 235LRR 810
Repeati372 – 392LRR 9Add BLAST21
Repeati398 – 420LRR 10Add BLAST23
Repeati421 – 442LRR 11Add BLAST22
Repeati446 – 468LRR 12Add BLAST23
Repeati470 – 493LRR 13Add BLAST24
Repeati495 – 516LRR 14Add BLAST22
Repeati519 – 539LRR 15Add BLAST21
Repeati543 – 564LRR 16Add BLAST22
Domaini576 – 627LRRCTAdd BLAST52
Domaini670 – 813TIRPROSITE-ProRule annotationAdd BLAST144

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The TIR domain mediates interaction with NOX4.By similarity
The TIR domain mediates NAD+ hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.PROSITE-ProRule annotation

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the Toll-like receptor family.Curated

Keywords - Domaini

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4641, Eukaryota

Identification of Orthologs from Complete Genome Data

More...
OMAi
AHNLIHS

Database of Orthologous Groups

More...
OrthoDBi
282372at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.10140, 1 hit
3.80.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000483, Cys-rich_flank_reg_C
IPR001611, Leu-rich_rpt
IPR003591, Leu-rich_rpt_typical-subtyp
IPR032675, LRR_dom_sf
IPR000157, TIR_dom
IPR017241, Toll-like_receptor
IPR035897, Toll_tir_struct_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR24365, PTHR24365, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13516, LRR_6, 1 hit
PF13855, LRR_8, 2 hits
PF01582, TIR, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF037595, Toll-like_receptor, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00369, LRR_TYP, 9 hits
SM00082, LRRCT, 1 hit
SM00255, TIR, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52200, SSF52200, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51450, LRR, 12 hits
PS50104, TIR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WV82-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMPSFCLAGT LMMALFLSSL RPESLDPCVE VDSNTSYQCM DRNLNKIPDN
60 70 80 90 100
IPSSVKHLDL SFNPLKTLGS HSFFNFPELK LLDLSRCEIE TIEDKAYQGL
110 120 130 140 150
HQLTTLILTG NPIQNLSKGT FSGLANLQNL VAVEIKLASL DSLPIGHLVT
160 170 180 190 200
LKKLNVAHNL IHSFKLPEYF SNLTNLEHLD LSNNYIQTIY YTDLQTLREN
210 220 230 240 250
PQLNLSLELS LNPIDFIQPG AFQGIRLHEL TLRSNFNSTN VMKTCIHNLD
260 270 280 290 300
GLQVHRLILG EFKNERNVER FDRYVIEGLC KVTIEEFRFT YANEFSEDIT
310 320 330 340 350
DFDCLANVSA MSLANVYLKR LEDIPKYFKW QTLAVIRCEL KQFPPLELPF
360 370 380 390 400
LKRLIFITNK GATSFPEVNL PSLTFLDLSG NGMSFRGCCS YTDLGARSLK
410 420 430 440 450
HLDLSFNGVI SMSENFMGLE QLEYLDFQHS TLKKATEFSM FLPLEKLLYL
460 470 480 490 500
DISYTNTKID FNGIFFGLTS LNTLKMAGNS FKDNILSNVF TNTTNLTFLD
510 520 530 540 550
ISKCQLQQVS WGVFDTLHRL ELLNMSHNNL LLLDLFHYKQ LHSLKTLDCS
560 570 580 590 600
FNHIETSKGI MQHFPKSLAF LNLTNNPFAC ICEHQNFLQW VKDQRLFLVK
610 620 630 640 650
TEQMTCATPV EMKDSLVLDF RNATCYVQKT IISVSVISVL VVSTIAFLVY
660 670 680 690 700
KFYFHLILIA GCKKYSRGES IYDAFVIYSS QDEDWVRNEL VKNLEEGVPP
710 720 730 740 750
FQLCLHYRDF IPGVAIAANI IQEGFHKSRK VIVVVSRHFI QSRWCIFEYE
760 770 780 790 800
IAQTWQFLSS HSGIIFIVLE KVEKSLLKQQ VELYRLLSRN TYLEWEDNAL
810 820 830
GRHIFWRRLK KALLDGRAWN PEGATEAENN QQETTTSI
Length:838
Mass (Da):96,278
Last modified:November 1, 1999 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i129B33596E908B48
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF153676 mRNA Translation: AAD41891.1

NCBI Reference Sequences

More...
RefSeqi
NP_001233691.1, NM_001246762.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSCGRT00001018473; ENSCGRP00001014236; ENSCGRG00001015165

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100689329

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cge:100689329

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF153676 mRNA Translation: AAD41891.1
RefSeqiNP_001233691.1, NM_001246762.1

3D structure databases

SMRiQ9WV82
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10029.NP_001233691.1

Genome annotation databases

EnsembliENSCGRT00001018473; ENSCGRP00001014236; ENSCGRG00001015165
GeneIDi100689329
KEGGicge:100689329

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7099

Phylogenomic databases

eggNOGiKOG4641, Eukaryota
OMAiAHNLIHS
OrthoDBi282372at2759

Family and domain databases

Gene3Di3.40.50.10140, 1 hit
3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR000483, Cys-rich_flank_reg_C
IPR001611, Leu-rich_rpt
IPR003591, Leu-rich_rpt_typical-subtyp
IPR032675, LRR_dom_sf
IPR000157, TIR_dom
IPR017241, Toll-like_receptor
IPR035897, Toll_tir_struct_dom_sf
PANTHERiPTHR24365, PTHR24365, 1 hit
PfamiView protein in Pfam
PF13516, LRR_6, 1 hit
PF13855, LRR_8, 2 hits
PF01582, TIR, 1 hit
PIRSFiPIRSF037595, Toll-like_receptor, 1 hit
SMARTiView protein in SMART
SM00369, LRR_TYP, 9 hits
SM00082, LRRCT, 1 hit
SM00255, TIR, 1 hit
SUPFAMiSSF52200, SSF52200, 1 hit
PROSITEiView protein in PROSITE
PS51450, LRR, 12 hits
PS50104, TIR, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTLR4_CRIGR
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9WV82
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: November 1, 1999
Last modified: June 2, 2021
This is version 136 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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