TLR8
entrez
51311
canonical
uniprot
Q9NR97
canonical
ensembl
ENSG00000101916
resolver
ensp
ENSP00000218032
resolver
ensp
ENSP00000312082
resolver
genesymbol
TLR8
resolver
hgnc
HGNC:15632
resolver
uniprot
A0AA49X8T4
resolver
uniprot
B3Y654
resolver
uniprot
D1CS70
resolver
uniprot
D1CS76
resolver
uniprot
Q495P4
resolver
uniprot
Q6UXL6
resolver
uniprot
Q9NYG9
resolver
uniprot_entry
A0AA49X8T4_HUMAN
resolver
uniprot_entry
TLR8_HUMAN
resolver
uniprot_sec
B3Y654
resolver
uniprot_sec
D1CS70
resolver
uniprot_sec
D1CS76
resolver
uniprot_sec
Q495P4
resolver
uniprot_sec
Q6UXL6
resolver
uniprot_sec
Q9NYG9
resolver
activity_regulation
ACTIVITY REGULATION: Activated by RNAs having enough uridines. {ECO:0000269|PubMed:25599397, ECO:0000269|PubMed:26929371}.
uniprot
proteins
amino_acid_sequence
MENMFLQSSMLTCIFLLISGSCELCAEENFSRSYPCDEKKQNDSVIAECSNRRLQEVPQTVGKYVTELDLSDNFITHITNESFQGLQNLTKINLNHNPNVQHQNGNPGIQSNGLNITDGAFLNLKNLRELLLEDNQLPQIPSGLPESLTELSLIQNNIYNITKEGISRLINLKNLYLAWNCYFNKVCEKTNIEDGVFETLTNLELLSLSFNSLSHVPPKLPSSLRKLFLSNTQIKYISEEDFKGLINLTLLDLSGNCPRCFNAPFPCVPCDGGASINIDRFAFQNLTQLRYLNLSSTSLRKINAAWFKNMPHLKVLDLEFNYLVGEIASGAFLTMLPRLEILDLSFNYIKGSYPQHINISRNFSKLLSLRALHLRGYVFQELREDDFQPLMQLPNLSTINLGINFIKQIDFKLFQNFSNLEIIYLSENRISPLVKDTRQSYANSSSFQRHIRKRRSTDFEFDPHSNFYHFTRPLIKPQCAAYGKALDLSLNSIFFIGPNQFENLPDIACLNLSANSNAQVLSGTEFSAIPHVKYLDLTNNRLDFDNASALTELSDLEVLDLSYNSHYFRIAGVTHHLEFIQNFTNLKVLNLSHNNIYTLTDKYNLESKSLVELVFSGNRLDILWNDDDNRYISIFKGLKNLTRLDLSLNRLKHIPNEAFLNLPASLTELHINDNMLKFFNWTLLQQFPRLELLDLRGNKLLFLTDSLSDFTSSLRTLLLSHNRISHLPSGFLSEVSSLKHLDLSSNLLKTINKSALETKTTTKLSMLELHGNPFECTCDIGDFRRWMDEHLNVKIPRLVDVICASPGDQRGKSIVSLELTTCVSDVTAVILFFFTFFITTMVMLAALAHHLFYWDVWFIYNVCLAKVKGYRSLSTSQTFYDAYISYDTKDASVTDWVINELRYHLEESRDKNVLLCLEERDWDPGLAIIDNLMQSINQSKKTVFVLTKKYAKSWNFKTAFYLALQRLMDENMDVIIFILLEPVLQHSQYLRLRQRICKSSILQWPDNPKAEGLFWQTLRNVVLTENDSRYNNMYVDSIKQY
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 98 with autoinflammation, X-linked (IMD98) [MIM:301078]: An X-linked disorder characterized by onset of recurrent infections associated with lymphoproliferation and autoinflammation in the first decade of life. Mostly males are affected; carrier females may have mild symptoms. Features include mouth ulcers, fever, poor early growth, hepatosplenomegaly, lymphadenopathy, polyarthritis, and non-infectious enteritis. {ECO:0000269|PubMed:33512449, ECO:0000269|PubMed:34981838}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Endosomal receptor that plays a key role in innate and adaptive immunity (PubMed:25297876, PubMed:32433612). Controls host immune response against pathogens through recognition of RNA degradation products specific to microorganisms that are initially processed by RNASET2 (PubMed:31778653). Recognizes GU-rich single-stranded RNA (GU-rich RNA) derived from SARS-CoV-2, SARS-CoV-1 and HIV-1 viruses (PubMed:33718825). Upon binding to agonists, undergoes dimerization that brings TIR domains from the two molecules into direct contact, leading to the recruitment of TIR-containing downstream adapter MYD88 through homotypic interaction (PubMed:23520111, PubMed:25599397, PubMed:26929371, PubMed:33718825). In turn, the Myddosome signaling complex is formed involving IRAK4, IRAK1, TRAF6, TRAF3 leading to activation of downstream transcription factors NF-kappa-B and IRF7 to induce pro-inflammatory cytokines and interferons, respectively (PubMed:16737960, PubMed:17932028, PubMed:29155428). {ECO:0000269|PubMed:16737960, ECO:0000269|PubMed:17932028, ECO:0000269|PubMed:23520111, ECO:0000269|PubMed:25297876, ECO:0000269|PubMed:25599397, ECO:0000269|PubMed:26929371, ECO:0000269|PubMed:29155428, ECO:0000269|PubMed:31778653, ECO:0000269|PubMed:32433612, ECO:0000269|PubMed:33718825}.
uniprot
proteins
mass_dalton
119828
uniprot
proteins
mutagenesis
MUTAGEN 348; /note="Y->A: Abolishes activation of NF-kappa-B."; /evidence="ECO:0000269|PubMed:23520111"; MUTAGEN 348; /note="Y->A: Abolishes responses to both ssRNA and chemical ligands."; /evidence="ECO:0000269|PubMed:25599397"; MUTAGEN 378; /note="V->A: Increases activation of NF-kappa-B."; /evidence="ECO:0000269|PubMed:23520111"; MUTAGEN 405; /note="F->A: Abolishes activation of NF-kappa-B."; /evidence="ECO:0000269|PubMed:23520111"; MUTAGEN 405; /note="F->A: Abolishes responses to both ssRNA and chemical ligands."; /evidence="ECO:0000269|PubMed:25599397"; MUTAGEN 452..455; /note="RKRR->NQSN: Monomeric and inactive."; /evidence="ECO:0000269|PubMed:26929371"; MUTAGEN 520; /note="V->A: Strongly decreases activation of NF-kappa-B."; /evidence="ECO:0000269|PubMed:23520111"; MUTAGEN 543; /note="D->A: Abolishes activation of NF-kappa-B."; /evidence="ECO:0000269|PubMed:23520111, ECO:0000269|PubMed:33512449"; MUTAGEN 543; /note="D->A: Abolishes responses to both ssRNA and chemical ligands."; /evidence="ECO:0000269|PubMed:25599397"; MUTAGEN 574; /note="T->A: Abolishes responses to both ssRNA and chemical ligands."; /evidence="ECO:0000269|PubMed:25599397"; MUTAGEN 574; /note="T->A: Strongly decreases activation of NF-kappa-B."; /evidence="ECO:0000269|PubMed:23520111
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by RNF216; leading to degradation by the proteasome. {ECO:0000269|PubMed:31385713}.; PTM: Proteolytic processing occurs in monocytes and monocyte-derived macrophages by both furin-like proprotein convertase and cathepsins (PubMed:25297876). The cleavage is necessary for dimer formation and subsequent activation (PubMed:26929371). {ECO:0000269|PubMed:25297876, ECO:0000269|PubMed:26929371}.
uniprot
proteins
protein_family
Toll-like receptor family
uniprot
proteins
pubmed
11022119
uniprot
proteins
pubmed
11022120
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16737960
uniprot
proteins
pubmed
17932028
uniprot
proteins
pubmed
18810425
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19924287
uniprot
proteins
pubmed
23520111
uniprot
proteins
pubmed
25297876
uniprot
proteins
pubmed
25599397
uniprot
proteins
pubmed
26929371
uniprot
proteins
pubmed
29155428
uniprot
proteins
pubmed
31385713
uniprot
proteins
pubmed
31778653
uniprot
proteins
pubmed
32433612
uniprot
proteins
pubmed
33512449
uniprot
proteins
pubmed
33718825
uniprot
proteins
pubmed
34981838
uniprot
proteins
sequence_length
1041
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:25297876}; Single-pass type I membrane protein {ECO:0000250}. Note=Endosomal localization confers distinctive proteolytic processing. {ECO:0000269|PubMed:25297876}.
uniprot
proteins
transmembrane_region
TRANSMEM 828..848; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins