Target Name: RCN3
NCBI ID: G57333
Review Report on RCN3 Target / Biomarker Content of Review Report on RCN3 Target / Biomarker
RCN3
Other Name(s): reticulocalbin 3, EF-hand calcium binding domain | Reticulocalbin-3 | EF-hand calcium-binding protein RLP49 | RLP49 | reticulocabin | reticulocalbin 3 | Reticulocalbin 3 | RCN3_HUMAN | Reticulocabin

RCN3: A Calcium-Binding Protein Implicated in Parkinson's Disease Treatment

RCN3 (reticulocalbin 3) is a protein that is expressed in various tissues of the body, including the nervous system, and is involved in the regulation of cell signaling pathways. It is a member of the EF-hand calcium binding domain family, which is a subfamily of the protein superfamily that is characterized by the presence of a unique calcium-binding domain in the protein sequence.

The EF-hand domain is a transmembrane protein that is involved in the regulation of a wide range of cellular processes, including cytoskeletal organization, muscle contractions, and intracellular signaling pathways. It is composed of multiple domains, including an N-terminal transmembrane domain, a coiled-coil domain, and a C-terminal protein-coding domain. The N-terminal transmembrane domain is responsible for the protein's ability to span the membrane, while the coiled-coil domain is responsible for the protein's ability to interact with other proteins and molecules. The C-terminal protein-coding domain contains the protein's amino acid sequence, which determines the specific structure and function of the protein.

RCN3 is a protein that is expressed in various tissues of the body, including the nervous system, and is involved in the regulation of cell signaling pathways. It is a member of the EF-hand calcium binding domain family, which is a subfamily of the protein superfamily that is characterized by the presence of a unique calcium-binding domain in the protein sequence.

The EF-hand domain is a transmembrane protein that is involved in the regulation of a wide range of cellular processes, including cytoskeletal organization, muscle contractions, and intracellular signaling pathways. It is composed of multiple domains, including an N-terminal transmembrane domain, a coiled-coil domain, and a C-terminal protein-coding domain. The N-terminal transmembrane domain is responsible for the protein's ability to span the membrane, while the coiled-coil domain is responsible for the protein's ability to interact with other proteins and molecules. The C-terminal protein-coding domain contains the protein's amino acid sequence, which determines the specific structure and function of the protein.

RCN3 is a protein that is characterized by the presence of a unique calcium-binding domain in its sequence. This domain is located within the N-terminal transmembrane domain of the EF-hand domain and is responsible for the regulation of cellular signaling pathways. The calcium-binding domain is a critical component of the EF-hand domain and is involved in the regulation of a wide range of cellular processes, including muscle contractions, intracellular signaling pathways, and cytoskeletal organization.

Research shows that RCN3 is a protein that is expressed in a variety of tissues and organs and is involved in regulating cell signaling pathways. It is a member of the EF-hand calcium-binding domain family, whose proteins all have unique calcium-binding domains. The EF-hand calcium-binding domain of RCN3 is located within the N-terminal transmembrane domain of the protein and is responsible for regulating cell signaling pathways. The calcium-binding domain is a key component of the EF-hand domain and is involved in regulating a variety of cellular processes such as muscle contraction, cell signaling pathways, and cytoskeletal organization.

The biological function of RCN3 has been confirmed in multiple studies. For example, studies have shown that RCN3 can regulate the excitability of neurons and thereby participate in the function of the nervous system. In addition, RCN3 can also regulate muscle contraction and participate in the process of muscle contraction and relaxation. In addition, RCN3 can also participate in the regulation of cytoskeletal organization structure, thereby participating in processes such as cell division, cell migration, and cell proliferation.

Currently, RCN3 has been widely studied as a drug target or biomarker. For example, some researchers are exploring the use of RCN3 in treating Parkinson's disease. Due to the critical role it plays in cell signaling pathways, RCN3 is considered a therapeutic

Protein Name: Reticulocalbin 3

Functions: Probable molecular chaperone assisting protein biosynthesis and transport in the endoplasmic reticulum (PubMed:16433634, PubMed:28939891). Required for the proper biosynthesis and transport of pulmonary surfactant-associated protein A/SP-A, pulmonary surfactant-associated protein D/SP-D and the lipid transporter ABCA3 (By similarity). By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis (By similarity). Has an anti-fibrotic activity by negatively regulating the secretion of type I and type III collagens (PubMed:28939891). This calcium-binding protein also transiently associates with immature PCSK6 and regulates its secretion (PubMed:16433634)

The "RCN3 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 RCN3 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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