SEADomain found in sea urchin sperm protein, enterokinase, agrin
|SMART accession number:||SM00200|
|Description:||Proposed function of regulating or binding carbohydrate sidechains.|
|Interpro abstract (IPR000082):|
The SEA domain has been named after the first three proteins in which it was identified (Sperm protein, Enterokinase and Agrin). The SEA domain has around 120 residues, it is an extracellular domain whose function is not known. It is found in one or two copies in mosaic extracellular or transmembrane proteins. The SEA domain is closely associated with regions receiving extensive O-glycosylation. It has been proposed that carbohydrates are required to stabilise SEA domains and protect them against proteolytic degradation and that the extent of substitution may control proteolytic processing [(PUBMED:7670383), (PUBMED:9762901)].
The SEA domain contains an about 80-residue conserved region and an about 40-residue segment that separates the conserved region from the subsequent C-terminal domains. Secondary structure predictions and circular dichroism suggest an alternating conformation of beta sheets and alpha helices for the SEA domain [(PUBMED:7670383), (PUBMED:9030729)].
Some proteins known to contain a SEA domain include:
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