Cell surface glycoprotein that plays a role in cell adhesion in a calcium-independent manner (PubMed:8776764, PubMed:2022629, PubMed:11590190). Mediates heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6 (PubMed:8776764, PubMed:2022629, PubMed:11590190). Heterophilic interaction with CEACAM8 occurs in activated neutrophils (PubMed:8776764). By probing white blood cell cDNA libraries with tumor nonspecific crossreacting antigen, Arakawa et al. (1990) isolated a cDNA encoding CEACAM8, which they called NCA-W272. The deduced 349-amino acid protein contains 11 potential N-glycosylation sites and 4 cysteines expected to form 2 intramolecular disulfide linkages. It also has a signal peptide and several domains similar to those of other CEA family proteins, such as CEACAM1 (109770). Immunoblot analysis showed expression of a 70-kD protein that was reduced to a 37-kD major protein and a 34-kD minor protein in the presence of a glycosylation inhibitor.