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7C77

Cryo-EM structure of mouse TLR3 in complex with UNC93B1

Functional Information from GO Data
ChainGOidnamespacecontents
A0002224biological_processtoll-like receptor signaling pathway
A0004888molecular_functiontransmembrane signaling receptor activity
A0006955biological_processimmune response
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
B0000902biological_processcell morphogenesis
B0002224biological_processtoll-like receptor signaling pathway
B0002250biological_processadaptive immune response
B0002457biological_processT cell antigen processing and presentation
B0005515molecular_functionprotein binding
B0005764cellular_componentlysosome
B0005768cellular_componentendosome
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006886biological_processintracellular protein transport
B0016020cellular_componentmembrane
B0019882biological_processantigen processing and presentation
B0019886biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II
B0032009cellular_componentearly phagosome
B0032735biological_processpositive regulation of interleukin-12 production
B0032755biological_processpositive regulation of interleukin-6 production
B0034138biological_processtoll-like receptor 3 signaling pathway
B0034154biological_processtoll-like receptor 7 signaling pathway
B0034162biological_processtoll-like receptor 9 signaling pathway
B0035325molecular_functionToll-like receptor binding
B0045087biological_processinnate immune response
B0045335cellular_componentphagocytic vesicle
B0051607biological_processdefense response to virus
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues240
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BVAL64-MET84
BVAL428-LEU448
BPHE469-SER489
BALA495-GLU515
BLYS110-ILE130
BPHE132-THR152
BTHR160-GLY180
BILE223-LEU243
BLEU285-GLY305
BLEU343-LEU363
BLEU378-TRP398
BVAL403-ALA423

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9H1C4
ChainResidueDetails
BSER547
BSER550

site_idSWS_FT_FI3
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN251
BASN272
BASN449

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O15455
ChainResidueDetails
ATYR760
ATYR859

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN53
AASN58
AASN125
AASN248

site_idSWS_FT_FI6
Number of Residues11
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18420935
ChainResidueDetails
AASN71
AASN663
AASN668
AASN197
AASN253
AASN276
AASN292
AASN399
AASN414
AASN425
AASN508

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:O15455
ChainResidueDetails
ALYS766
ALYS813
ALYS832

224004

PDB entries from 2024-08-21

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