Ceacam6

Predicted to enable identical protein binding activity; protein heterodimerization activity; and protein tyrosine kinase binding activity. Predicted to be involved in several processes, including heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; homophilic cell adhesion via plasma membrane adhesion molecules; and positive regulation of cell adhesion. Predicted to be located in apical plasma membrane and extracellular space. Predicted to be active in cell surface and plasma membrane. Orthologous to several human genes including CEACAM6 (CEA cell adhesion molecule 6); PSG4 (pregnancy specific beta-1-glycoprotein 4); and PSG6 (pregnancy specific beta-1-glycoprotein 6). [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 Ceacam6 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.

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