SLC10A7 is a Golgi-localized orphan transporter essential for skeletal and dental development 1. Unlike other SLC10 family members, SLC10A7 does not transport bile acids or steroid sulfates 2. Its primary function involves regulating intracellular calcium homeostasis as a negative regulator of store-operated calcium entry 3. SLC10A7 maintains tight ER and Golgi calcium regulation, which is critical for proper O-GalNAc glycosylation and glycosaminoglycan synthesis 4. Loss of SLC10A7 function impairs post-Golgi protein transport and causes defective N-glycosylation with accumulation of hybrid-type N-glycans 1. These glycosylation defects compromise extracellular matrix formation and mineralization, essential for bone development 5. SLC10A7 mutations cause a rare autosomal recessive congenital disorder of glycosylation (SLC10A7-CDG) characterized by skeletal dysplasia with multiple joint dislocations, short stature, amelogenesis imperfecta, and decreased bone mineral density 56. Mouse models recapitulate human pathology with shortened long bones, growth plate disorganization, and enamel anomalies 5. The mechanisms involve altered abundance of glycosylation enzymes (COSMC, C1GALT1) and abnormal Golgi localization of calcium-binding proteins 4. Manganese supplementation can partially rescue glycosylation defects, suggesting therapeutic potential 4.