Target Name: ATP6V1A
NCBI ID: G523
Review Report on ATP6V1A Target / Biomarker Content of Review Report on ATP6V1A Target / Biomarker
ATP6V1A
Other Name(s): H(+)-transporting two-sector ATPase, subunit A | VPP2 | VATA_HUMAN | V-ATPase subunit A | V-type proton ATPase catalytic subunit A | HO68 | Vacuolar proton pump subunit alpha | Vacuolar ATPase isoform VA68 | vacuolar proton pump subunit alpha | ATP6V1A1 | V-type proton ATPase (V-ATPase) catalytic subunit A | VA68 | Vacuolar ATP synthase catalytic subunit A, ubiquitous isoform | ATP6A1 | IECEE3 | H+-transporting ATPase chain A, vacuolar (VA68 type) | vacuolar proton pump alpha subunit 1 | ARCL2D | ATPase H+ transporting V1 subunit A | ATPase, H+ transporting, lysosomal, subunit A1 | V-ATPase 69 kDa subunit | V-ATPase A subunit 1 | DEE93 | V-ATPase 69 kDa subunit 1 | Vma1 | Vacuolar proton pump alpha subunit 1 | ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A

Unlocking The Potential of ATP6V1A as A Drug Target

Unlocking the Potential of ATP6V1A as a Drug Target: High-Accurate ATPase Subunit for Analyzing cellular Energy Metabolism

Abstract:
ATP6V1A, the H(+)-transporting two-sector ATPase subunit A, has been identified as a promising drug target and a biomarker for various diseases. This article summarizes the structure, function, and potential therapeutic applications of ATP6V1A, highlighting its unique features and the scientific advancements that have been made in its study.

Introduction:
ATP (adenosine triphosphate) is the primary energy source for the cell and plays a crucial role in regulating various cellular processes. The H(+)-transporting two-sector ATPase, subunit A (ATP6V1A), is a protein that enables the efficient production of ATP fromADP and Pi (phosphate) via a two-sector mechanism. This subunit is highly conserved across various species, which suggests its importance in the fundamental cellular energy metabolism.

Structure and Function:
ATP6V1A is a 21-kDa protein that consists of two distinct subunits, A and B. Subunit A contains 105 amino acid residues, while subunit B contains 94 amino acid residues. Both subunits have a unique 尾-sheet structure, which is characterized by a central 尾-helix and two distinct 尾-strands. The 尾-sheet is flanked by two conserved amino acids, Asp22 and Asn23, which are involved in the stability of the subunit.

ATP6V1A functions as the H(+)-transporting two-sector ATPase, subunit A by using the unique 尾-sheet structure to regulate the ATP production. The subunit has three distinct regions: an N-terminal region (residues 1-20), a catalytic region (residues 21-94), and a C-terminal region (residues 95-105). The N-terminal region contains the ATP-binding site, which is critical for the efficient production of ATP.

The catalytic region is the site of ATP binding and hydrolysis. The 尾-sheet plays a crucial role in the regulation of the ATP binding and hydrolysis. The 尾-sheet is flanked by two conserved amino acids, Asp22 and Asn23, which are involved in the stability of the subunit. The Asp22 residue is involved in the ATP binding, while Asn23 residue is involved in the ATP hydrolysis.

The C-terminal region is involved in the regulation of the ATP binding and hydrolysis. This region contains a unique ion-pair, which is composed of a Calcium ion (Ca2+) and a Serine ion (Ser). The ion-pair plays a crucial role in the regulation of ATP binding and hydrolysis by controlling the calcium ions concentration in the cell.

Potential Therapeutic Applications:
The unique function of ATP6V1A as the H(+)-transporting two-sector ATPase, subunit A has led to its potential as a drug target and biomarker for various diseases.

1. Diabetes: Diabetes is a chronic metabolic disease that is characterized by high blood sugar levels. The H(+)-transporting two-sector ATPase, subunit A plays a crucial role in the regulation of ATP production fromADP and Pi. Therefore, targeting

Protein Name: ATPase H+ Transporting V1 Subunit A

Functions: Catalytic subunit of the V1 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 (PubMed:8463241). 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 (PubMed:32001091). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633). May play a role in neurite development and synaptic connectivity (PubMed:29668857)

The "ATP6V1A Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about ATP6V1A comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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