Fibronectin Type III Domain Containing 5 Human Recombinant
Fibronectin Type III Domain Containing 5 Human Recombinant, Yeast
The Fibronectin Type III (FN3) domain is an evolutionarily conserved protein domain found in a wide variety of animal proteins. It was first identified in the fibronectin protein, which contains 16 copies of this domain. The FN3 domain is approximately 100 amino acids long and has a beta-sandwich structure . Unlike other fibronectin-type domains, the FN3 domain does not contain disulfide bonds .
Key Biological Properties: FN3 domains are characterized by their beta-sandwich structure, which provides stability and flexibility. They are involved in various cellular processes, including cell adhesion, migration, and signaling .
Expression Patterns and Tissue Distribution: FN3 domains are widely distributed across different tissues and are found in various proteins, including those involved in the immune system, cardiovascular system, and nervous system . For example, FNDC5, a protein containing the FN3 domain, is predominantly expressed in skeletal muscle and adipose tissue .
Primary Biological Functions: FN3 domains play crucial roles in cell adhesion, migration, and extracellular matrix organization. They are involved in the formation of cell-matrix interactions, which are essential for tissue development and repair .
Role in Immune Responses and Pathogen Recognition: FN3 domains are also implicated in immune responses. For instance, FNDC4 has been described as an anti-inflammatory factor, upregulated in inflammatory bowel disease . FN3 domains in immune receptors help in recognizing and binding to pathogens, facilitating immune responses .
Mechanisms with Other Molecules and Cells: FN3 domains interact with various molecules and cells through their beta-sandwich structure. These interactions are crucial for cell signaling and adhesion .
Binding Partners and Downstream Signaling Cascades: FN3 domains bind to integrins and other cell surface receptors, initiating downstream signaling cascades that regulate cellular processes such as proliferation, differentiation, and migration . For example, FNDC5 interacts with integrins to modulate glycolipid metabolism and cardiovascular homeostasis .
Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of FN3 domain-containing proteins are regulated at multiple levels, including transcriptional regulation and post-translational modifications .
Transcriptional Regulation: The transcription of FN3 domain-containing genes is regulated by various transcription factors and signaling pathways. For instance, FNDC5 expression is induced by exercise through the PGC1α pathway .
Post-Translational Modifications: FN3 domain-containing proteins undergo post-translational modifications such as phosphorylation, glycosylation, and proteolytic cleavage, which modulate their activity and function .
Biomedical Research: FN3 domains are used as models to study protein folding and stability due to their well-defined structure .
Diagnostic Tools: FN3 domain-containing proteins, such as FNDC3B, are being explored as biomarkers for various diseases, including glioblastoma and pancreatic cancer .
Therapeutic Strategies: FN3 domains are potential targets for therapeutic interventions. For example, FNDC5-derived irisin is being investigated for its role in metabolic diseases and muscle health .
Role Throughout the Life Cycle: FN3 domains play essential roles throughout the life cycle, from development to aging and disease. During development, they are involved in tissue formation and organogenesis . In adulthood, they maintain tissue homeostasis and repair . In aging and disease, alterations in FN3 domain-containing proteins can contribute to pathological conditions such as cancer and cardiovascular diseases .