ATPase Class VI Type 11C: A Potential Drug Target and Biomarker

Target Name: ATP11C

NCBI ID: G286410

ATPase Class VI Type 11C: A Potential Drug Target and Biomarker

ATP (adenosine triphosphate) is a crucial molecule in the cell's energy metabolism. It is the primary energy source for most cellular processes and is responsible for generating the energy needed for the cell to maintain its structure, function, and survival. The production and regulation of ATP is regulated by a complex network of enzymes, including the ATPases. ATPases are a group of transmembrane proteins that catalyze the conversion of ATP to ADP and Pi (phosphorylated inositol). There are several ATPases, classified into different types based on their catalytic mechanism, substrate specificity, and expression level in the cell. In this article, we will focus on the ATPase class VI type 11C (ATPase-like protein 11C), which is a potential drug target and biomarker.

Composition and Structure

ATPases are a diverse family of proteins that share a conserved catalytic core. The catalytic core consists of a nucleotide-binding domain (NBD), a transmembrane region (TM), and an C-terminal region (CTM) that is involved in substrate recognition and catalytic activity. The NBD is the site of the ATP-dependent hydrolysis, which releases energy to drive the reaction.

ATPase class VI type 11C is a member of the ATPase family and is characterized by its NBD, TM, and CTM regions. The NBD of class VI type 11C contains a single nucleotide-binding domain (NBD) that is similar to other ATPases. The TM region of class VI type 11C is also conserved and contains a transmembrane domain, as well as a cytoplasmic region (C-terminus) that is involved in protein-protein interactions. The CTM region of class VI type 11C is unique and contains a helical structure that is involved in substrate recognition and activation.

Substrate Specificity

ATPase class VI type 11C is specific for its substrate, ADP. It can catalyze the hydrolysis of ADP to produce ATP, which is then converted to ADP by the enzyme ATP synthase. The ATPase reaction is reversible, and the product of the reaction can be reacted with additional ATP to produce ADP and Pi.

Class VI type 11C is a potent ATPase that is involved in various cellular processes, including intracellular signaling, DNA replication, and protein synthesis. It is expressed in various cell types and tissues and is involved in the regulation of ATP homeostasis. The reversible ATPase reaction of class VI type 11C can generate a large amount of ATP, which can be used to maintain the cellular energy homeostasis.

Drug Target Potential

ATPase class VI type 11C is a potential drug target due to its unique structure and function. The NBD and TM regions of class VI type 11C are involved in the catalytic activity, which makes them attractive targets for small molecules. The unique CTM region of class VI type 11C is involved in substrate recognition and activation, which can be targeted by small molecules that can modulate the activity of the enzyme.

In addition to its potential as a drug target, class VI type 11C also has the potential to serve as a biomarker. The reversible ATPase reaction of class VI type 11C can be used as a sensitive assay for the detection of ATP. The activity of class

Protein Name: ATPase Phospholipid Transporting 11C

Functions: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane (PubMed:25315773, PubMed:32493773, PubMed:24904167, PubMed:26567335). Major PS-flippase in immune cell subsets. In erythrocyte plasma membrane, it is required to maintain PS in the inner leaflet preventing its exposure on the surface. This asymmetric distribution is critical for the survival of erythrocytes in circulation since externalized PS is a phagocytic signal for erythrocyte clearance by splenic macrophages (PubMed:26944472). Required for B cell differentiation past the pro-B cell stage (By similarity). Seems to mediate PS flipping in pro-B cells (By similarity). May be involved in the transport of cholestatic bile acids (By similarity)

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