Summary: SEA domain
SEA domain Provide feedback
Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain .
Kitamoto Y, Yuan X, Wu Q, McCourt DW, Sadler JE; , Proc Natl Acad Sci U S A 1994;91:7588-7592.: Enterokinase, the initiator of intestinal digestion, is a mosaic protease composed of a distinctive assortment of domains. PUBMED:8052624 EPMC:8052624
Maeda T, Inoue M, Koshiba S, Yabuki T, Aoki M, Nunokawa E, Seki E, Matsuda T, Motoda Y, Kobayashi A, Hiroyasu F, Shirouzu M, Terada T, Hayami N, Ishizuka Y, Shinya N, Tatsuguchi A, Yoshida M, Hirota H, Matsuo Y, Tani K, Arakawa T, Carninci P, Kawai J, Hay, J Biol Chem 2004;279:13174-13182.: Solution structure of the SEA domain from the murine homologue of ovarian cancer antigen CA125 (MUC16). PUBMED:14764598 EPMC:14764598
External database links
This tab holds annotation information from the InterPro database.
InterPro entry 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:
- Vertebrate agrin, an heparan sulfate proteoglycan of the basal lamina of the neuromuscular junction. It is responsible for the clustering of acetylcholine receptors (AChRs) and other proteins at the neuromuscular junction.
- Mammalian enterokinase. It catalyses the conversion of trypsinogen to trypsin which in turn activates other proenzymes, including chymotrypsinogen, procarboxypeptidases, and proelastases.
- 63 kDa sea urchin sperm protein (SP63). It might mediate sperm-egg or sperm-matrix interactions.
- Animal perlecan, a heparan sulfate containing proteoglycan found in all basement membranes. It interacts with other basement membrane components such as laminin and collagen type IV and serves as an attachment substrate for cells.
- Some vertebrate epithelial mucins. They form a family of secreted and cell surface glycoproteins expressed by epithelial tissues and implicated in epithelial cell protection, adhesion modulation and signaling.
- Mammalian cell surface antigen 114/A10, an integral transmembrane protein that is highly expressed in hematopoietic progenitor cells and IL-3-dependent cell lines.
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Number in seed:||247|
|Number in full:||2431|
|Average length of the domain:||97.60 aa|
|Average identity of full alignment:||17 %|
|Average coverage of the sequence by the domain:||14.20 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the SEA domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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