Cryga

Three main families of major soluble proteins, the alpha, beta and gamma crystallins, are ubiquitously expressed in vertebrate lenses. This gene encodes a member of the gamma-crystallin family of proteins which may function as a structural component of the eye lens. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Five gamma-crystallin genes (gamma-A through gamma-E) are tandemly organized in a genomic segment as a gene cluster in the mouse. Another gamma-crystallin gene (gamma-F) is found some distance upstream of the cluster on the same chromosome. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation. [provided by RefSeq, Jul 2008]

A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in mouse Cryga often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.

Biological processes and signaling networks where the Cryga gene in mouse plays a role, providing insight into its function and relevance in health or disease.

The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.

Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.

Describes the biological processes, cellular components, and molecular functions associated with the mouse Cryga gene, providing context for its role in the cell.