Cryab

This gene encodes subunit b, one of two subunits of alpha-crystallin, which is a high molecular weight, soluble aggregate and is a member of the small heat shock protein family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. It acts as a molecular chaperone and is the major protein in the eye lens, maintaining the transparency and refractive index of the lens. Alternate promoter usage results in different transcript variants encoding the same protein. [provided by RefSeq, Sep 2014]

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 rat Cryab 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 Cryab gene in rat 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 rat Cryab gene, providing context for its role in the cell.