{PDOC00699}
{PS00898; EPENDYMIN_1}
{PS00899; EPENDYMIN_2}
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* Ependymins signatures *
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Ependymins  were originally identified in the ependymal zone of goldfish brain
and  are  the  major  glycoprotein  component  of cerebrospinal fluid (CSF) in
various  orders of teleost fish [1,2,3,4]. Several N-glycosylation variants of
ependymin have been identified and an important role appears to be the binding
of  calcium  via  N-linked  sialic  acid residues [5]. The precise function of
ependymins  is still being elucidated. Beside the piscine ependymin this group
is  formed by Ependymin Related Proteins (ERP) in Xenopus and in mammals (MERP
or UCC1).

A  predominant  feature  of MERPs, Xenopus ERP and fish ependymins is the four
conserved  cysteine  residues.  Potentially,  these  cysteine  residues may be
important in maintaining protein conformation through disulfide bonding. Human
and  mouse  MERPs  are  of similar length to fish ependymins (224 amino acids)
and,  like  fish  ependymins,  are  predominantly  hydrophilic  and  contain a
cleavable  hydrophobic  signal  sequence that is typical of secretory proteins
[6].

We developed two signature patterns for ependymins.  The first one corresponds
to a well conserved region located between two conserved N-glycosylation sites
and which  include a conserved cysteine residue. The second pattern is located
in the C-terminal section and also includes one of the conserved cysteines.

-Consensus pattern: [DE]-[SQLM]-[KAH]-[NT]-[QEK]-[SQ]-C-[SRKH]-x-[EQKM]-[STM]-
                    L
                    [C may be involved in a disulfide bond]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: F-x-[PL]-P-[STA]-[FYT]-C-[DEQ]-[GAMI]-[LVMA]-x-[TLF]-[DE]-
                    [DEK]
                    [C may be involved in a disulfide bond]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Hoffmann W.; werner.hoffmann@medizin.uni-magdeburg.de
           Apostolopoulos J.; japostolopoulos@arcbs.redcross.org.au

-Last update: December 2001 / Patterns and text revised.

[ 1] Hoffmann W.
     "Ependymins and their potential role in neuroplasticity and
     regeneration: calcium-binding meningeal glycoproteins of the
     cerebrospinal fluid and extracellular matrix."
     Int. J. Biochem. 26:607-619(1994).
     PubMed=8005346
[ 2] Shashoua V.E.
     "Ependymin, a brain extracellular glycoprotein, and CNS plasticity."
     Ann. N.Y. Acad. Sci. 627:94-114(1991).
     PubMed=1831964
[ 3] Mueller-Schmid A., Ganss B., Gorr T., Hoffmann W.
     J. Mol. Evol. 36:578-585(1993).
[ 4] Hoffmann W., Schwarz H.
     "Ependymins: meningeal-derived extracellular matrix proteins at the
     blood-brain barrier."
     Int. Rev. Cytol. 165:121-158(1996).
     PubMed=8900958
[ 5] Gans B., Hoffmann W.
     Eur. J. Biochem. 217:275-280(1993).
[ 6] Apostolopoulos J., Sparrow R.L., McLeod J.L., Collier F.M.,
     Darcy P.K., Slater H.R., Ngu C., Gregorio-King C.C., Kirkland M.A.
     "Identification and characterization of a novel family of mammalian
     ependymin-related proteins (MERPs) in hematopoietic, nonhematopoietic,
     and malignant tissues."
     DNA Cell Biol. 20:625-635(2001).
     PubMed=11749721; DOI=10.1089/104454901753340613

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