IRAK3, also called IRAK-M, is an IRAK-family pseudokinase that regulates Toll-like and interleukin-1 receptor signaling. It participates in receptor-associated signaling assemblies and restrains inflammatory activation by stabilizing MyD88-associated IRAK complexes. Its death domain and kinase-like domain mediate protein interactions, and its effects depend on cellular context and stimulus history. The selected protein sequence has an internal or terminal difference from the characterized human protein, so its precise activity and regulation remain to be established.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005524 ATP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: ATP binding: The pseudokinase can engage nucleotide with low affinity; this is compatible with a kinase-like fold but is not evidence of phosphoryl-transfer catalysis or its principal signaling function. Reason: The pseudokinase can engage nucleotide with low affinity; this is compatible with a kinase-like fold but is not evidence of phosphoryl-transfer catalysis or its principal signaling function. Supporting Evidence: PMID:33238146 IRAK3 Has Low Affinity for ATP but High Affinity for ATP-Competitive Inhibitors file:HORSE/IRAK3/IRAK3-bioinformatics/RESULTS.md The downloaded human Q9Y616 sequence (596 residues) and selected horse A0A3Q2HDT6 sequence (567 residues) share 80.7% identity among 554 paired residues. Paired coverage is 93.0% of human and 97.7% of horse. |
| GO:0007165 signal transduction | IEA GO_REF:0000002 | UNDECIDED | Summary: signal transduction: The selected horse sequence lacks the N-terminal region through human residue 43, reaching the death domain used in signaling-complex assembly. Broad IRAK3 signaling is plausible but intact function of this shortened product remains unverified. Reason: The selected horse sequence lacks the N-terminal region through human residue 43, reaching the death domain used in signaling-complex assembly. Broad IRAK3 signaling is plausible but intact function of this shortened product remains unverified. Supporting Evidence: PMID:12150927 We show here that IRAK-M is induced upon TLR stimulation and negatively regulates TLR signaling. IRAK-M prevented dissociation of IRAK and IRAK-4 from MyD88 and formation of IRAK-TRAF6 complexes. file:HORSE/IRAK3/IRAK3-bioinformatics/RESULTS.md The downloaded human Q9Y616 sequence (596 residues) and selected horse A0A3Q2HDT6 sequence (567 residues) share 80.7% identity among 554 paired residues. Paired coverage is 93.0% of human and 97.7% of horse. |
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