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Comparative studies have revealed that SP‐A2 is often more biologically active than its paralog SP‐A1, and transgenic models further corroborate its integral role in surfactant structure formation and immunomodulation ["}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "].\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMutations and genetic variations in SFTPA2 have been closely linked to a spectrum of pulmonary pathologies. Rare missense mutations affecting highly conserved residues within the carbohydrate‐recognition domain impair proper protein folding and oligomerization, leading to its retention in the endoplasmic reticulum and the onset of ER stress. Such disruptions are implicated in familial idiopathic pulmonary fibrosis, lung adenocarcinoma, and other interstitial lung disorders. 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These regulatory layers contribute not only to the functional diversity observed in alveolar macrophage responses and surfactant homeostasis but also offer promising biomarkers for respiratory disorders, such as lung cancer, respiratory syncytial virus infection, asthma, and acute respiratory failure. 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