Anti-ATP6V0D2 antibody

Supplementary info

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

Activity summary

ATP6V0D2 also known as V-type proton ATPase subunit d 2 is a subunit of the V-ATPase complex. It has a mass of approximately 38 kDa. This protein is expressed in various tissues with significant expression noted in bone and white adipose tissue. Mechanically ATP6V0D2 contributes to the acidification of intracellular compartments. It functions as part of the proton pump machinery facilitating the transfer of protons across membranes which is essential for processes like endocytosis and intracellular trafficking.

Biological function summary

ATP6V0D2 plays a significant role in bone resorption and adipogenesis. It is a component of the larger V-ATPase complex important for creating acidic environments required for enzyme activity particularly in osteoclasts. This acidity enables the breakdown of bone matrix which is a fundamental part of bone remodeling. Additionally ATP6V0D2 influences fat cell differentiation by modulating the function of cytosolic components within the complex.

Pathways

ATP6V0D2 functions as an integral part of the bone remodeling and lysosomal degradation pathways. In the bone remodeling pathway the protein works closely with other proton pump components like ATP6V0A3 to regulate osteoclast activity. In lysosomal degradation it aids in maintaining the acidity essential for lysosomal enzyme activity. Both pathways are connected through ATP6V0D2's regulation of intracellular pH and ion homeostasis.

Associated diseases and disorders

ATP6V0D2 has associations with osteoporosis and obesity. In osteoporosis deficient or dysfunctional ATP6V0D2 activity can impair osteoclast function leading to altered bone resorption and skeletal fragility. In the context of obesity this protein influences adipocyte differentiation and function. ATP6V0D2's role in these disorders connects it to other proteins like RANKL in bone metabolism and PPARγ in adipogenesis linking it beyond just its structural function within proton pumps.