The olfactomedin-like or OLF domain is a module of ~260 residues present in metazoan secreted glycoproteins with a characteristic tissue-specific expression. The domain is named after bullfrog olfactomedin, an extracellular matrix protein of olfactory neuroepithelium, whereof it forms the C-terminal part. Other proteins of the olfactomedin family contain the OLF domain in the C-terminal part … expand

The olfactomedin-like or OLF domain is a module of ~260 residues present in metazoan secreted glycoproteins with a characteristic tissue-specific expression. The domain is named after bullfrog olfactomedin, an extracellular matrix protein of olfactory neuroepithelium, whereof it forms the C-terminal part. Other proteins of the olfactomedin family contain the OLF domain in the C-terminal part, while the N terminus is more variable. Proteins of the latrophilin subfamily have an OLF domain in the N-terminal extracellular part, C-terminal to a SUEL-type lectin domain, and their C-terminal part contains domains of the G-protein coupled receptors family 2. Some OLF domain proteins are involved in the formation of the extracellular matrix, e.g. bullfrog olfactomedin, sea urchin amassin and C. elegans unc-122. In addition, OLF domain proteins can function in developmental processes, e.g. noelin and tiarin [ PUBMED:12019210 PUBMED:11867215 PUBMED:12615070 PUBMED:15280020 ].

Secondary structure predictions show that the OLF domain contains several β-strands [ PUBMED:11867215 PUBMED:12615070 PUBMED:15280020 ]. A disulfide bond between two conserved cysteines within the OLF domain of human myocilin is implicated in mutations associated with severe forms of primary open angle glaucoma [ PUBMED:12615070 ].