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ADP-ribosylation factor-like protein 10 (ARL10) is a member of the ARF-like family of small GTPases, functioning as a molecular switch by cycling between GDP- and GTP-bound forms. ARL10 is primarily localized to mitochondria, peroxisomes, endoplasmic reticulum, and the nucleus, and contains a unique N-terminal transmembrane domain critical for its mitochondrial targeting[1]. Its biological functions, identified through proteomic mapping studies, suggest roles in regulating mitophagy, mitochondrial and peroxisome organization, protein trafficking, vacuolar transport, cilium and centrosome organization, and TOR (Target of Rapamycin) signaling[1]. While it is a protein coding gene, with predicted GTP and GTPase binding activity, its clinical or therapeutic targeting potential is not established. ARL10 mutations or dysregulation have been associated with certain cancers, such as mucinous stomach adenocarcinoma, although its detailed involvement in disease mechanisms remains undercharacterized[3].
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