Ticam2
entrez
225471
canonical
uniprot
Q8BJQ4
canonical
ensembl
ENSMUSG00000056130
resolver
ensp
ENSMUSP00000066239
resolver
enst
ENSMUST00000070084
resolver
genesymbol
Ticam2
resolver
genesymbol_syn
Tirp
resolver
genesymbol_syn
Tram
resolver
uniprot
Q3U996
resolver
uniprot_entry
TCAM2_MOUSE
resolver
uniprot_sec
Q3U996
resolver
amino_acid_sequence
MGVGKSKLDKCPLSWHKKDSVDADQDGHESDSKNSEEACLRGFVEQSSGSEPPTGEQDQPEAKGAGPEEQDEEEFLKFVILHAEDDTDEALRVQDLLQNDFGIRPGIVFAEMPCGRLHLQNLDDAVNGSAWTILLLTENFLRDTWCNFQFYTSLMNSVSRQHKYNSVIPMRPLNSPLPRERTPLALQTINALEEESQGFSTQVERIFRESVFERQQSIWKETRSVSQKQFIA
uniprot
proteins
function
FUNCTION: Functions as a sorting adapter in different signaling pathways to facilitate downstream signaling leading to type I interferon induction. In TLR4 signaling, physically bridges TLR4 and TICAM1 and functionally transmits signal to TICAM1 in early endosomes after endocytosis of TLR4. In TLR2 signaling, physically bridges TLR2 and MYD88 and is required for the TLR2-dependent movement of MYD88 to endosomes following ligand engagement. Involved in IL-18 signaling and is proposed to function as a sorting adapter for MYD88 in IL-18 signaling during adaptive immune response. Forms a complex with RAB11FIP2 that is recruited to the phagosomes to promote the activation of the actin-regulatory GTPases RAC1 and CDC42 and subsequent phagocytosis of Gram-negative bacteria. {ECO:0000250|UniProtKB:Q86XR7, ECO:0000269|PubMed:14556004, ECO:0000269|PubMed:18297073, ECO:0000269|PubMed:22685567}.
uniprot
proteins
mass_dalton
26362
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Results in relocalization from membrane to cytosol; impairs ability to promote LPS-induced IL6 and CCL5 production."; /evidence="ECO:0000269|PubMed:18297073"; MUTAGEN 7; /note="K->E: Results in exclusive localization to early endosomes and no effect on ability to promote LPS-induced IL6 and CCL5 production; when associated with E-15 and E-17."; /evidence="ECO:0000269|PubMed:18297073"; MUTAGEN 15; /note="W->E: Results in exclusive localization to early endosomes and no effect on ability to promote LPS-induced IL6 and CCL5 production; when associated with E-7 and E-17."; /evidence="ECO:0000269|PubMed:18297073"; MUTAGEN 17; /note="K->E: Results in exclusive localization to early endosomes and no effect on ability to promote LPS-induced IL6 and CCL5 production; when associated with E-7 and E-15."; /evidence="ECO:0000269|PubMed:18297073
uniprot
proteins
post_translational_modification
PTM: Myristoylated. Required for membrane association which is critical for its ability to initiate efficient signaling. {ECO:0000250|UniProtKB:Q86XR7}.; PTM: Phosphorylated by PRKCE in response to LPS. Phosphorylation is essential for its function. It is depleted from the membrane upon phosphorylation. Tyrosine phosphorylation is inhibited by phosphatase PTPN4. {ECO:0000250|UniProtKB:Q86XR7}.
uniprot
proteins
pubmed
12721283
uniprot
proteins
pubmed
14517278
uniprot
proteins
pubmed
14519765
uniprot
proteins
pubmed
14556004
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18297073
uniprot
proteins
pubmed
22685567
uniprot
proteins
sequence_length
232
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18297073}. Early endosome {ECO:0000269|PubMed:18297073}. Late endosome {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q86XR7}. Note=Localized to the plasma membrane as a result of myristoylation. {ECO:0000250}.
uniprot
proteins