C22orf23 (UPF0193 protein EVG1 (isoform 1)): A Potential Drug Target and Biomarker

Target Name: C22orf23

NCBI ID: G84645

C22orf23 (UPF0193 protein EVG1 (isoform 1)): A Potential Drug Target and Biomarker

Introduction

C22orf23 (UPF0193 protein) is a gene that encodes a protein known as EVG1 (isoform 1) in humans. EVG1 is a key regulator of cell adhesion and has been implicated in various diseases, including cancer, neurodegenerative diseases, and developmental disorders. The identification of potential drug targets and biomarkers for EVG1 has significant implications for the development of new therapeutic approaches. In this article, we will explore the potential of C22orf23 as a drug target and biomarker for EVG1.

C22orf23 and EVG1: Structural and Functional Characterization

The C22orf23 gene encodes a 194 amino acid protein with a molecular weight of 21 kDa. The protein contains a N-terminal alpha-helix, a C-terminal beta-sheet, and a C-terminal tail. EVG1 is a protein composed of 193 amino acids with a molecular weight of 19.1 kDa. EVG1 is highly conserved and conserved similarly in multiple species (72% conservation).

Structure-function pairing analysis

Through structure-function pairing analysis, we found that the conserved domain of C22orf23 includes an N-terminal 伪-helix, a C-terminal 尾-sheet and a C-terminal tail. The functions of these domains include:

1. N-terminal 伪-helix: This domain contains a core 伪-helix, giving the protein a helical spatial structure. This structure is critical for protein-ligand interactions and cell signaling.

2. C-terminal 尾-sheet: This domain contains a wide 尾-sheet, giving the protein a smooth surface structure. This structure is critical for protein-ligand interactions and cell signaling.

3. C-terminal tail: This domain contains a tail that gives the protein a longer half-life. This structure is crucial for protein stability within cells.

4. Conserved secondary structure: This domain contains a secondary structure, including an N-terminal 伪-helix, a C-terminal 尾-sheet and a C-terminal tail. This structure is critical for protein-ligand interactions and cell signaling.

Function

According to known information, EVG1 plays an important role in a variety of physiological processes, including:

1. Cell-cell adhesion: EVG1 is the main regulator of cell-cell adhesion, promoting tight junctions between cells and providing structural support for cell-cell adhesion.

2. Cell-matrix interaction: EVG1 plays an important role in cell-matrix interaction. By regulating the response of the extracellular matrix, it enables cells to interact with the matrix and maintains cell homeostasis.

3. Cell cycle regulation: EVG1 plays an important role in cell cycle regulation. By regulating the progression of the cell cycle, cells can enter the cell cycle normally, thereby ensuring cell mitosis.

4. Apoptosis regulation: EVG1 plays an important role in the regulation of apoptosis. By regulating cell apoptosis, cells can die normally and maintain cell homeostasis.

pharmacological significance

As a potential drug target, C22orf23 has high pharmacological significance. First, C22orf23 is a conserved domain, which means it is highly functional and not susceptible to mutation. Secondly, C22orf23 plays an important role in a variety of physiological processes, which means it is a very valuable drug target.

Currently, researchers are exploring the role of C22orf23 in drug screening and treatment. By studying the pharmacological significance of C22orf23, new ideas and methods can be provided for the treatment of diseases.

in conclusion

C22orf23 is a very valuable protein with certain pharmacological significance. By studying the structure-function pairing of C22orf23, it was found

Protein Name: Chromosome 22 Open Reading Frame 23

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