PROSITE documentation PDOC51132
Olfactomedin-like domain profile


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 (see <PDOC50228>), and their C-terminal part contains domains of the G-protein coupled receptors family 2 (see <PDOC00559> and <PDOC50221>). 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 [1,2,3,4].

Secondary structure predictions show that the OLF domain contains several β-strands [2,3,4]. 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 [3].

Some proteins known to contain an olfactomedin-like domain:

  • Rana catesbeiana olfactomedin, a major component of the extracellular mucus matrix of the olfactory neuroepithelium, which may influence the development of the chemosensory dendrites of olfactory neurons.
  • Human myocilin or trabecular meshwork inducible glucocorticoid response (TIGR) protein, a secreted glycoprotein that is highly expressed in the retina. Mutations of the MYOC gene cause some forms of primary open-angle glaucoma, a prevalent cause of blindness, and these are mostly located in the OLF domain [1,3].
  • Mammalian noelin or pancortin proteins, secreted glycoproteins that promote neurogenesis.
  • Mammalian optimedin, which is expressed in the brain and retina like noelin. Optimedin interacts with myocilin by the OLF domain [1].
  • Mammalian latrophilin proteins, which belong to the secretin family of G-protein coupled receptors. These receptors mediate the toxic action of α-latrotoxin, a neurotoxin present in black widow spider venom; the OLF domain is not required for this interaction.
  • Xenopus laevis tiarin, a secreted protein involved in neuronal development.
  • Purple sea urchin amassin, an intercellular adhesion protein involved in clotting of coelomocytes by forming large disulfide-bonded aggregates.
  • Caenorhabditis elegans unc-122 protein, which acts in neuromuscular junctions and affects locomotory behavior.

The profile we developed covers the entire olfactomedin-like domain.

Last update:

June 2005 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

OLF, PS51132; Olfactomedin-like domain profile  (MATRIX)


1AuthorsTorrado M. Trivedi R. Zinovieva R. Karavanova I. Tomarev S.I.
TitleOptimedin: a novel olfactomedin-related protein that interacts with myocilin.
SourceHum. Mol. Genet. 11:1291-1301(2002).
PubMed ID12019210

2AuthorsZhang J. Liu W.L. Tang D.C. Chen L. Wang M. Pack S.D. Zhuang Z. Rodgers G.P.
TitleIdentification and characterization of a novel member of olfactomedin-related protein family, hGC-1, expressed during myeloid lineage development.
SourceGene 283:83-93(2002).
PubMed ID11867215

3AuthorsNagy I. Trexler M. Patthy L.
TitleExpression and characterization of the olfactomedin domain of human myocilin.
SourceBiochem. Biophys. Res. Commun. 302:554-561(2003).
PubMed ID12615070

4AuthorsZeng L.C. Liu F. Zhang X. Zhu Z.D. Wang Z.Q. Han Z.G. Ma W.J.
TitlehOLF44, a secreted glycoprotein with distinct expression pattern, belongs to an uncharacterized olfactomedin-like subfamily newly identified by phylogenetic analysis.
SourceFEBS Lett. 571:74-80(2004).
PubMed ID15280020

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