{PDOC51132}
{PS51132; OLF}
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* Olfactomedin-like domain profile *
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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 [1-4].

Secondary  structure  predictions  show  that  the OLF domain contains several
beta-strands  [2-4].  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
   alpha-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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: June 2005 / First entry.

[ 1] Torrado M., Trivedi R., Zinovieva R., Karavanova I., Tomarev S.I.
     "Optimedin: a novel olfactomedin-related protein that interacts with
     myocilin."
     Hum. Mol. Genet. 11:1291-1301(2002).
     PubMed=12019210
[ 2] Zhang J., Liu W.L., Tang D.C., Chen L., Wang M., Pack S.D., Zhuang Z.,
     Rodgers G.P.
     "Identification and characterization of a novel member of
     olfactomedin-related protein family, hGC-1, expressed during myeloid
     lineage development."
     Gene 283:83-93(2002).
     PubMed=11867215
[ 3] Nagy I., Trexler M., Patthy L.
     "Expression and characterization of the olfactomedin domain of human
     myocilin."
     Biochem. Biophys. Res. Commun. 302:554-561(2003).
     PubMed=12615070
[ 4] Zeng L.C., Liu F., Zhang X., Zhu Z.D., Wang Z.Q., Han Z.G., Ma W.J.
     "hOLF44, a secreted glycoprotein with distinct expression pattern,
     belongs to an uncharacterized olfactomedin-like subfamily newly
     identified by phylogenetic analysis."
     FEBS Lett. 571:74-80(2004).
     PubMed=15280020; DOI=10.1016/j.febslet.2004.06.059

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