Anti-ATP6V1A antibody [8B1F3]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

ATP6V1A also known as V-ATPase subunit A is a component of the V1 domain of the vacuolar ATPase (V-ATPase) which is a large enzyme responsible for acidifying intracellular compartments. This protein has a mass of approximately 70 kDa and operates in cellular processes by hydrolyzing ATP to drive protons across membranes. ATP6V1A displays significant expression in several cell types including neurons epithelial cells and osteoclasts. The protein enables V-ATPase functionality important for maintaining the pH balance inside cells and organelles facilitating various physiological processes.

Biological function summary

ATP6V1A is an integral part of the V1 domain of the V-ATPase complex a multi-subunit assembly critical for the acidification of intracellular organelles such as lysosomes endosomes and the Golgi apparatus. This activity supports processes like protein degradation receptor-mediated endocytosis and membrane trafficking. The V-ATPase containing ATP6V1A uses energy from ATP hydrolysis to pump protons which is essential for cellular homeostasis and ion transport.

Pathways

ATP6V1A plays an important role in the endocytosis and autophagy pathways. These pathways depend on the acidification of intracellular compartments enabling processes such as the breakdown and recycling of cellular components. ATP6V1A is related to proteins like V-ATPase subunit c (ATP6V1C) and other subunits that form the V-ATPase enzyme. These protein interactions allow the modulation and execution of cellular transport and hormone regulation pathways.

Associated diseases and disorders

Mutations or dysregulation of ATP6V1A have been linked to renal tubular acidosis and osteoporosis where improper acidification impacts bone resorption and kidney function. The protein connections include its interaction with other V-ATPase subunits like ATP6V0A3 which can also result in osteopetrosis when defective. Such conditions demonstrate how ATP6V1A's role in acidification processes is important for normal physiological function and how its dysfunction leads to disease.