The SEA module: A new extracellular domain associated with O‐glycosylation
Open Access
- 1 July 1995
- journal article
- for the-record
- Published by Wiley in Protein Science
- Vol. 4 (7), 1421-1425
- https://doi.org/10.1002/pro.5560040716
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 MUC1 (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-glycosidiclinked carbohydrates such as heparan sulfate that contribute considerably to their molecular masses. The common module might regulate or assist binding to neighboring carbohydrate moieties.Keywords
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