The SEA module: a new extracellular domain associated with O-glycosylation.
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 MUCI (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.
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Max-Delbrück-Center for Molecular Medicine, Berlin-Buch, Germany.
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D018171:Agrin / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D000954:Antigens, Surface / Q000737:chemistry; D017173:Caenorhabditis elegans / Q000737:chemistry; D004765:Enteropeptidase / Q000737:chemistry; D004815:Epidermal Growth Factor; D006031:Glycosylation; D019812:Heparan Sulfate Proteoglycans; D006497:Heparan Sulfate / Q000737:chemistry; D006801:Humans; D008297:Male; D008562:Membrane Glycoproteins / Q000737:chemistry; D008969:Molecular Sequence Data; D018396:Mucin-1; D009077:Mucins / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D011509:Proteoglycans / Q000737:chemistry; D012617:Sea Urchins / Q000737:chemistry; D016415:Sequence Alignment; D013094:Spermatozoa / Q000737:chemistry
D018171:Agrin; D000954:Antigens, Surface; D004765:Enteropeptidase; D004815:Epidermal Growth Factor; D019812:Heparan Sulfate Proteoglycans; D006497:Heparan Sulfate; D008562:Membrane Glycoproteins; D018396:Mucin-1; D009077:Mucins; D011506:Proteins; D011509:Proteoglycans; C063487:Ly64 protein, mouse; C071927:perlecan