Anti-ATP6V1C1 antibody

Supplementary info

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

Activity summary

ATP6V1C1 also known as ATPase H+ transporting V1 subunit C1 is a component of the V1 sector of the V-ATPase complex with a mass around 45 kDa. It is a part of the proton pump which plays an important role in acidifying intracellular compartments. ATP6V1C1 is expressed in various tissues with high levels seen in kidney liver and lungs. Its function as a subunit involves assembly stability and regulation of the ATPase complex which is essential for translocating protons across membranes.

Biological function summary

ATP6V1C1 functions within the V-ATPase complex that consists of V1 and V0 domains. This complex actively transports hydrogen ions (H+) across organelle membranes and plasma membranes which is important for processes such as protein degradation receptor-mediated endocytosis and neurotransmitter release. The activity of ATP6V1C1 supports cellular homeostasis by maintaining the acidic environment required for these processes.

Pathways

ATP6V1C1 plays a role in important pathways such as lysosomal acidification and bone resorption. It closely interacts with other V-ATPase subunits such as ATP6V0D1 in these pathways. The V-ATPase activity in lysosomal acidification facilitates the function of lysosomal enzymes while in bone resorption it helps osteoclasts to dissolve bone minerals highlighting its significance in both metabolic and skeletal systems.

Associated diseases and disorders

ATP6V1C1 has a connection to osteopetrosis and renal tubular acidosis. Mutations or dysfunction in ATP6V1C1 may lead to impaired V-ATPase function influencing disease progression. Osteopetrosis is connected through its effect on osteoclast function while ATP6V1C1's role in acidifying urine implicates it in renal tubular acidosis. Its interactions with other proteins like ATP6V0A4 further elaborate its involvement in these diseases impacting treatment and research directions.