Olfactomedins (OLF) were first discovered in the frog olfactory neuroepithelium (Snyder et al., 1991). The OLF domain has a length of about 250 amino acids and it is present in at least 13 proteins in mammals (Tomarev and Nakaya, 2009). A growing body of evidence indicates that these proteins play important roles in normal development and disease in mammals, and mutations in some of these genes lead to profound pathologies in humans (Anholt, 2014). The most extensively studied OLF-containing protein is probably myocilin in which mutations are found in more than 10% of juvenile open-angle glaucoma cases and in 3–4% of patients with adult onset primary open-angle glaucoma (POAG) (Fingert et al., 1999; Stone et al., 1997). The available crystal structures of gliomedin and myocilin, two members of the OLF family reveal a 5-blade β-propeller fold and the presence of Ca2+ and/or Na+ in the central pore (Donegan et al., 2014; Han and Kursula, 2015). Recent findings on the extracellular domain of FLRT3 reveal that this protein has the tendency to homo-dimerize but a precise characterization of dimerization potential is
