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The SEA module: A new extracellular domain associated with O ‐glycosylation
Author(s) -
Bork Peer,
Patthy Laszlo
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040716
Subject(s) - glycosylation , extracellular , glycoprotein , biology , caenorhabditis elegans , heparan sulfate , biochemistry , microbiology and biotechnology , chemistry , computational biology , gene , cell
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.