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Protein unc-119 homolog B (UNC119B) is a lipid-binding trafficking chaperone that accommodates and solubilizes N-myristoylated proteins, preventing their inappropriate localization and facilitating their directed transport within the cell. UNC119B contains an immunoglobulin-like β-sandwich fold which generates a hydrophobic pocket, allowing it to bind the myristoyl moiety of specific cargo proteins. Two classes of cargoes are distinguished by their affinity for UNC119B, and release is regulated by small GTPases such as ARL2 and ARL3. UNC119B exhibits nuanced specificity compared to its paralog UNC119A, including unique sequence features and alternative structural conformations which influence cargo protein binding and release. Its trafficking activity enables delivery of signaling proteins to the primary cilium and immunological synapse, making it essential for spatial regulation of membrane-associated proteins in various cell types, including photoreceptors, sensory neurons, and immune cells
Not applicable; UNC119B is not a direct drug target in current therapeutic strategies. Its function is protein-protein interaction based
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