ATP6V0E2: A Potential Drug Target and Biomarker (G155066)

Target Name: ATP6V0E2

NCBI ID: G155066

ATP6V0E2: A Potential Drug Target and Biomarker

Introduction

ATP6V0E2, also known as VA0E2_HUMAN, is a protein that is expressed in various tissues and cell types in the human body. Its function and regulation have been extensively studied, and its potential as a drug target or biomarker continue to attract researchers' interest. In this article, we will provide an overview of ATP6V0E2, its functions, potential drug targets, and its potential as a biomarker for various diseases.

F functions and localization

ATP6V0E2 is a member of the ATP6V0 family, which includes several similar proteins that are involved in various cellular processes, including metabolism, autophagy, and signaling pathways. The protein encoded by the VA0E2 gene is a 21-kDa protein that contains a N-terminal transmembrane domain, a catalytic domain, and a C-terminal T-loop region.

ATP6V0E2 is predominantly expressed in the liver, heart, skeletal muscles, and pancreas, where it is involved in various cellular processes, including metabolism, energy homeostasis, and signaling pathways. The protein is also expressed in other tissues, including the kidney, liver, and heart, but at much lower levels.

Potential drug targets

ATP6V0E2 is a protein that has potential as a drug target due to its involvement in various cellular processes that are crucial for human health. Several studies have identified potential drug targets for ATP6V0E2, including the inhibition of its catalytic activity, modulation of its expression level, and alteration of its localization to specific cellular compartments.

One of the most promising potential drug targets for ATP6V0E2 is the inhibition of its catalytic activity, which could be achieved through various mechanisms, including inhibition of ATP6V0E2-catalyzed reactions or inhibition of its interaction with other proteins. Several studies have shown that inhibitors of ATP6V0E2 can significantly reduce the amount of ATP produced in the liver, which is a key step in the metabolism of many diseases, including diabetes and cancer.

Another potential drug target for ATP6V0E2 is its modulation of expression level. The expression level of ATP6V0E2 can be regulated by various factors, including DNA methylation, RNA-binding protein, and protein degradation. Modulation of ATP6V0E2 expression level could be a promising strategy for targeting the protein in diseases that are caused by the over-expression or under-expression of ATP6V0E2.

In addition, alteration of ATP6V0E2's localization to specific cellular compartments could also be a potential drug target. ATP6V0E2 is involved in various cellular processes, including metabolism, energy homeostasis, and signaling pathways. By modulating its localization to specific cellular compartments, researchers may be able to target its functions and alter its contribution to various diseases.

Potential biomarkers

ATP6V0E2 is also a potential biomarker for various diseases due to its involvement in various cellular processes that are crucial for human health. The protein is involved in various signaling pathways, including the citric acid cycle, the electron transport chain, and the purine biosynthesis pathway. Alterations in ATP6V0E2 expression levels or function could be a potential biomarker for various diseases.

One of the most promising potential biomarkers for ATP6V0E2 is its involvement in the regulation of cellular energy homeostasis. The citric acid cycle is a key component of cellular energy homeostasis, and ATP6V0E2 is involved in the regulation of its activity

Protein Name: ATPase H+ Transporting V0 Subunit E2

Functions: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity)

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