Q86XR7
uniprot
Q86XR7
canonical
amino_acid_sequence
MGIGKSKINSCPLSLSWGKRHSVDTSPGYHESDSKKSEDLSLCNVAEHSNTTEGPTGKQEGAQSVEEMFEEEAEEEVFLKFVILHAEDDTDEALRVQNLLQDDFGIKPGIIFAEMPCGRQHLQNLDDAVNGSAWTILLLTENFLRDTWCNFQFYTSLMNSVNRQHKYNSVIPMRPLNNPLPRERTPFALQTINALEEESRGFPTQVERIFQESVYKTQQTIWKETRNMVQRQFIA
uniprot
proteins
function
FUNCTION: Functions as a sorting adapter in different signaling pathways to facilitate downstream signaling leading to type I interferon induction (PubMed:16603631, PubMed:16757566, PubMed:25385819, PubMed:25825441). 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 (PubMed:25385819). Involved in IL-18 signaling and is proposed to function as a sorting adapter for MYD88 in IL-18 signaling during adaptive immune response (PubMed:22685567). 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 (PubMed:30883606). {ECO:0000269|PubMed:16603631, ECO:0000269|PubMed:16757566, ECO:0000269|PubMed:22685567, ECO:0000269|PubMed:25385819, ECO:0000269|PubMed:25825441, ECO:0000269|PubMed:30883606}.; FUNCTION: [Isoform 2]: Proposed to inhibit LPS-TLR4 signaling at the late endosome by interaction with isoform 1 thereby disrupting the association of isoform 1 with TICAM1. May be involved in TLR4 degradation in late endosomes.
uniprot
proteins
mass_dalton
26916
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Results in relocalization from membrane to cytosol; Loss of ability to transduce TLR4-signal. Loss of TLR2-mediated activation of IRF7."; /evidence="ECO:0000269|PubMed:16603631, ECO:0000269|PubMed:25385819"; MUTAGEN 6; /note="S->A: Loss of phosphorylation. Significant reduction in the ability to activate IRF3 or NF-kappa-B."; /evidence="ECO:0000269|PubMed:16757566"; MUTAGEN 10; /note="S->A: No effect on phosphorylation and on the ability to activate IRF3 or NF-kappa-B."; /evidence="ECO:0000269|PubMed:16757566"; MUTAGEN 14; /note="S->A: No effect on phosphorylation and on the ability to activate IRF3 or NF-kappa-B."; /evidence="ECO:0000269|PubMed:16757566"; MUTAGEN 16; /note="S->A: Loss of phosphorylation. Abolishes ability to activate IRF3 or NF-kappa-B and to transduce TLR4 signal."; /evidence="ECO:0000269|PubMed:16757566"; MUTAGEN 16; /note="S->E: Significant decrease of localization in the membrane."; /evidence="ECO:0000269|PubMed:16757566"; MUTAGEN 116; /note="P->H: Loss of ability to dimerize. Significant loss of RANTES-inducing activity. Loss of ability to induce NF-kappa-B activation."; /evidence="ECO:0000269|PubMed:14517278, ECO:0000269|PubMed:14519765"; MUTAGEN 117; /note="C->H: Loss of ability to dimerize. Loss of RANTES-inducing activity and ability to induce NF-kappa-B activation. Inhibition of TLR4-dependent activation of IRF3 and IRF7. Loss of interaction with TLR4."; /evidence="ECO:0000269|PubMed:14517278, ECO:0000269|PubMed:14519765"; MUTAGEN 154; /note="Y->F: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:25825441"; MUTAGEN 167; /note="Y->F: Complete loss of phosphorylation in response to LPS."; /evidence="ECO:0000269|PubMed:25825441
uniprot
proteins
post_translational_modification
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:0000269|PubMed:16757566, ECO:0000269|PubMed:25825441}.; PTM: Isoform 1 is myristoylated. Required for membrane association which is critical for its ability to initiate efficient signaling. {ECO:0000269|PubMed:16603631}.
uniprot
proteins
pubmed
12721283
uniprot
proteins
pubmed
12761501
uniprot
proteins
pubmed
14517278
uniprot
proteins
pubmed
14519765
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16603631
uniprot
proteins
pubmed
16757566
uniprot
proteins
pubmed
18810425
uniprot
proteins
pubmed
19412184
uniprot
proteins
pubmed
22685567
uniprot
proteins
pubmed
25385819
uniprot
proteins
pubmed
25825441
uniprot
proteins
pubmed
30883606
uniprot
proteins
sequence_length
235
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:25825441}. Golgi apparatus. Cell membrane {ECO:0000269|PubMed:25825441}. Endoplasmic reticulum. Early endosome membrane. Late endosome membrane. Cell projection, phagocytic cup {ECO:0000269|PubMed:30883606}. Note=Localized to the plasma membrane as a result of myristoylation. Phosphorylation on Ser-16 leads to its depletion from the membrane. Upon LPS stimulation colcoalizes with isoform 2 in late endosomes.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum. Early endosome membrane. Late endosome membrane. Note=Translocates to late endosomes upon LPS stimulation where it colcoalizes with isoform 1.
uniprot
proteins