Tlr9
entrez
81897
canonical
uniprot
Q9EQU3
canonical
ensembl
ENSMUSG00000045322
resolver
ensp
ENSMUSP00000082207
resolver
enst
ENSMUST00000062241
resolver
genesymbol
Tlr9
resolver
uniprot
F8VPN5
resolver
uniprot
Q4L0K3
resolver
uniprot
Q4L0K4
resolver
uniprot
Q99MF2
resolver
uniprot
Q99MQ8
resolver
uniprot_entry
TLR9_MOUSE
resolver
uniprot_sec
F8VPN5
resolver
uniprot_sec
Q4L0K3
resolver
uniprot_sec
Q4L0K4
resolver
uniprot_sec
Q99MF2
resolver
uniprot_sec
Q99MQ8
resolver
amino_acid_sequence
MVLRRRTLHPLSLLVQAAVLAETLALGTLPAFLPCELKPHGLVDCNWLFLKSVPRFSAAASCSNITRLSLISNRIHHLHNSDFVHLSNLRQLNLKWNCPPTGLSPLHFSCHMTIEPRTFLAMRTLEELNLSYNGITTVPRLPSSLVNLSLSHTNILVLDANSLAGLYSLRVLFMDGNCYYKNPCTGAVKVTPGALLGLSNLTHLSLKYNNLTKVPRQLPPSLEYLLVSYNLIVKLGPEDLANLTSLRVLDVGGNCRRCDHAPNPCIECGQKSLHLHPETFHHLSHLEGLVLKDSSLHTLNSSWFQGLVNLSVLDLSENFLYESITHTNAFQNLTRLRKLNLSFNYRKKVSFARLHLASSFKNLVSLQELNMNGIFFRLLNKYTLRWLADLPKLHTLHLQMNFINQAQLSIFGTFRALRFVDLSDNRISGPSTLSEATPEEADDAEQEELLSADPHPAPLSTPASKNFMDRCKNFKFTMDLSRNNLVTIKPEMFVNLSRLQCLSLSHNSIAQAVNGSQFLPLTNLQVLDLSHNKLDLYHWKSFSELPQLQALDLSYNSQPFSMKGIGHNFSFVTHLSMLQSLSLAHNDIHTRVSSHLNSNSVRFLDFSGNGMGRMWDEGGLYLHFFQGLSGLLKLDLSQNNLHILRPQNLDNLPKSLKLLSLRDNYLSFFNWTSLSFLPNLEVLDLAGNQLKALTNGTLPNGTLLQKLDVSSNSIVSVVPAFFALAVELKEVNLSHNILKTVDRSWFGPIVMNLTVLDVRSNPLHCACGAAFVDLLLEVQTKVPGLANGVKCGSPGQLQGRSIFAQDLRLCLDEVLSWDCFGLSLLAVAVGMVVPILHHLCGWDVWYCFHLCLAWLPLLARSRRSAQTLPYDAFVVFDKAQSAVADWVYNELRVRLEERRGRRALRLCLEDRDWLPGQTLFENLWASIYGSRKTLFVLAHTDRVSGLLRTSFLLAQQRLLEDRKDVVVLVILRPDAHRSRYVRLRQRLCRQSVLFWPQQPNGQGGFWAQLSTALTRDNRHFYNQNFCRGPTAE
uniprot
proteins
function
FUNCTION: Key component of innate and adaptive immunity (PubMed:31408613). TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms (PubMed:31408613). TLR9 is a nucleotide-sensing TLR which is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides (PubMed:31408613). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:14993594, PubMed:17474149, PubMed:18820679, PubMed:18931679, PubMed:21402738, PubMed:25686612). Also acts via ADCY7, leading to cyclic di-AMP (c-di-AMP) synthesis and activation of the NLRP3 inflammasome (PubMed:40419769). Plays a role in defense against systemic mouse cytomegalovirus infection (PubMed:14993594). Controls lymphocyte response to Helicobacter infection (PubMed:17474149). Upon CpG stimulation, induces B-cell proliferation, activation, survival and antibody production (By similarity). {ECO:0000250|UniProtKB:Q9NR96, ECO:0000269|PubMed:14993594, ECO:0000269|PubMed:17474149, ECO:0000269|PubMed:18820679, ECO:0000269|PubMed:18931679, ECO:0000269|PubMed:21402738, ECO:0000269|PubMed:25686612, ECO:0000269|PubMed:31408613}.
uniprot
proteins
mass_dalton
116412
uniprot
proteins
mutagenesis
MUTAGEN 47; /note="W->A: Significantly decreased NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612"; MUTAGEN 74; /note="R->A: Significantly decreased NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612"; MUTAGEN 104; /note="S->A: Significantly decreased NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612"; MUTAGEN 108; /note="F->A: Significantly decreased NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612"; MUTAGEN 132; /note="Y->A: Significantly decreased NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612"; MUTAGEN 152; /note="H->A: Significantly decreased NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612"; MUTAGEN 179; /note="Y->A: Significantly decreased NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612"; MUTAGEN 229; /note="Y->A: Significantly decreased NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612"; MUTAGEN 499; /note="L->P: Highly susceptible to mouse cytomegalovirus infection. Shows low level of cytokine induction and natural killer activation on viral infection."; /evidence="ECO:0000269|PubMed:14993594"; MUTAGEN 642; /note="H->A: Loss of NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612"; MUTAGEN 668; /note="F->A: Significantly decreased NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612"; MUTAGEN 695; /note="N->A: Significantly decreased NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:25686612
uniprot
proteins
post_translational_modification
PTM: Activated by proteolytic cleavage of the flexible loop between repeats LRR14 and LRR15 within the ectodomain (PubMed:18820679, PubMed:18931679). Cleavage requires UNC93B1 (PubMed:18820679). Proteolytically processed by first removing the majority of the ectodomain by either asparagine endopeptidase (AEP) or a cathepsin followed by a trimming event that is solely cathepsin mediated and required for optimal receptor signaling (PubMed:21402738). {ECO:0000269|PubMed:18820679, ECO:0000269|PubMed:18931679, ECO:0000269|PubMed:21402738}.; PTM: Palmitoylated by ZDHHC3 in the Golgi regulates TLR9 trafficking from the Golgi to endosomes. Depalmitoylation by PPT1 controls the release of TLR9 from UNC93B1 in endosomes. {ECO:0000250|UniProtKB:Q9NR96}.; PTM: Phosphorylation of Tyr-870 by SYK and Tyr-980 by EGFR is essential for TLR9-mediated gene induction. {ECO:0000250|UniProtKB:Q9NR96}.
uniprot
proteins
protein_family
Toll-like receptor family
uniprot
proteins
pubmed
11130078
uniprot
proteins
pubmed
11470918
uniprot
proteins
pubmed
11867692
uniprot
proteins
pubmed
14993594
uniprot
proteins
pubmed
17452530
uniprot
proteins
pubmed
17474149
uniprot
proteins
pubmed
18305481
uniprot
proteins
pubmed
18780723
uniprot
proteins
pubmed
18820679
uniprot
proteins
pubmed
18931679
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20865800
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21402738
uniprot
proteins
pubmed
21940676
uniprot
proteins
pubmed
25686612
uniprot
proteins
pubmed
25917084
uniprot
proteins
pubmed
26095358
uniprot
proteins
pubmed
31408613
uniprot
proteins
pubmed
40419769
uniprot
proteins
sequence_length
1032
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305481, ECO:0000269|PubMed:31408613}; Single-pass type I membrane protein {ECO:0000269|PubMed:18305481}. Endosome {ECO:0000269|PubMed:18305481, ECO:0000269|PubMed:25917084}. Lysosome {ECO:0000269|PubMed:18305481, ECO:0000269|PubMed:18820679, ECO:0000269|PubMed:25917084}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:18305481, ECO:0000269|PubMed:18820679}. Note=Relocalizes from endoplasmic reticulum to endosome and lysosome upon stimulation with agonist (PubMed:18305481). Exit from the ER requires UNC93B1 (PubMed:18820679). Endolysosomal localization is required for proteolytic cleavage and subsequent activation (PubMed:18820679, PubMed:18931679). Intracellular localization of the active receptor may prevent from responding to self nucleic acid (PubMed:18820679). {ECO:0000269|PubMed:18305481, ECO:0000269|PubMed:18820679, ECO:0000269|PubMed:18931679}.
uniprot
proteins
transmembrane_region
TRANSMEM 819..839; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins