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Transmembrane protein 208 (TMEM208) is a highly conserved, ER-localized, integral membrane protein, possessing three putative transmembrane domains and a C-terminal ER retention motif (KKxx-like) that governs its ER localization. TMEM208 functions as a key component of the SRP-independent (SND) pathway, responsible for translocation of proteins with internal transmembrane domains into the ER. It negatively regulates autophagy and modulates the ER stress response, serving as a possible molecular link between these two cellular processes. TMEM208 interacts with planar cell polarity signaling proteins (e.g., Frizzled receptor) and is essential for normal development and tissue organization. Loss-of-function mutations have been connected to developmental delay and multisystem disorders in humans, and lethality in model organisms. TMEM208 contains the domain of unknown function DUF788, which spans most of the protein sequence and contributes to its evolutionary conservation.
Not applicable; no drugs targeting TMEM208 are documented
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