Ero1b

Predicted to enable protein-disulfide reductase activity and thiol oxidase activity. Predicted to be involved in protein folding in endoplasmic reticulum. Predicted to act upstream of or within several processes, including cell redox homeostasis; insulin processing; and peptidyl-proline hydroxylation to 4-hydroxy-L-proline. Predicted to be located in membrane. Predicted to be active in endoplasmic reticulum lumen and endoplasmic reticulum membrane. Orthologous to human ERO1B (endoplasmic reticulum oxidoreductase 1 beta). [provided by Alliance of Genome Resources, Jul 2025]

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 Ero1b 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 Ero1b 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 Ero1b gene, providing context for its role in the cell.