The SEA module: A new extracellular domain associated with O- glycosylation

P. Bork, L. Patthy

Research output: Contribution to journalArticle

106 Citations (Scopus)

Abstract

Using a variety of homology search methods and multiple alignments, a new extracellular module was identified in (1) agrin, (2) enterokinase, (3) a 63- kDa sea urchin sperm protein, (4) perlecan, (5) the breast cancer marker MUCl (episialin), (6) the cell surface antigen 114/A10, and (7/8) two functionally uncharacterized, probably extracellular, Caenorhabditis elegans proteins. Despite the functional diversity of these adhesive proteins, a common denominator seems to be their existence in heavily glycosylated environments. In addition, the better characterized proteins mentioned above contain all O- glycosidic-linked carbohydrates such as heparan sulfate that contribute considerably to their molecular masses. The common module might regulate or assist binding to neighboring carbohydrate moieties.

Original languageEnglish
Pages (from-to)1421-1425
Number of pages5
JournalProtein Science
Volume4
Issue number7
Publication statusPublished - 1995

Fingerprint

Glycosylation
Caenorhabditis elegans Proteins
Agrin
Enteropeptidase
Carbohydrates
Mucin-1
Proteins
Heparitin Sulfate
Sea Urchins
antineoplaston A10
Molecular mass
Surface Antigens
Adhesives
Spermatozoa
Breast Neoplasms

Keywords

  • agrin
  • enterokinase
  • homology search
  • molecular evolution
  • perlecan
  • sperm protein

ASJC Scopus subject areas

  • Biochemistry

Cite this

The SEA module : A new extracellular domain associated with O- glycosylation. / Bork, P.; Patthy, L.

In: Protein Science, Vol. 4, No. 7, 1995, p. 1421-1425.

Research output: Contribution to journalArticle

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