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PROSITE documentation PDOC00699

Ependymins signatures





Description

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.

Expert(s) to contact by email:

Hoffmann W.
Apostolopoulos J.

Last update:

December 2001 / Patterns and text revised.

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Technical section

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

EPENDYMIN_1, PS00898; Ependymins signature 1  (PATTERN)

EPENDYMIN_2, PS00899; Ependymins signature 2  (PATTERN)


References

1AuthorsHoffmann W.
TitleEpendymins and their potential role in neuroplasticity and regeneration: calcium-binding meningeal glycoproteins of the cerebrospinal fluid and extracellular matrix.
SourceInt. J. Biochem. 26:607-619(1994).
PubMed ID8005346

2AuthorsShashoua V.E.
TitleEpendymin, a brain extracellular glycoprotein, and CNS plasticity.
SourceAnn. N.Y. Acad. Sci. 627:94-114(1991).
PubMed ID1831964

3AuthorsMueller-Schmid A. Ganss B. Gorr T. Hoffmann W.
SourceJ. Mol. Evol. 36:578-585(1993).

4AuthorsHoffmann W. Schwarz H.
TitleEpendymins: meningeal-derived extracellular matrix proteins at the blood-brain barrier.
SourceInt. Rev. Cytol. 165:121-158(1996).
PubMed ID8900958

5AuthorsGans B. Hoffmann W.
SourceEur. J. Biochem. 217:275-280(1993).

6AuthorsApostolopoulos 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.
TitleIdentification and characterization of a novel family of mammalian ependymin-related proteins (MERPs) in hematopoietic, nonhematopoietic, and malignant tissues.
SourceDNA Cell Biol. 20:625-635(2001).
PubMed ID11749721
DOI10.1089/104454901753340613



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