The role of the SEA (sea urchin sperm protein, enterokinase and agrin) module in cleavage of membrane‐tethered mucins

@article{PalmaiPallag2005TheRO,
  title={The role of the SEA (sea urchin sperm protein, enterokinase and agrin) module in cleavage of membrane‐tethered mucins},
  author={Timea Palmai-Pallag and Naila Khodabukus and Leo Kinarsky and Shih-Hsing Leir and Simon A. Sherman and Michael A. Hollingsworth and Ann Harris},
  journal={The FEBS Journal},
  year={2005},
  volume={272}
}
The membrane‐tethered mucins are cell surface‐associated dimeric or multimeric molecules with extracellular, transmembrane and cytoplasmic portions, that arise from cleavage of the primary polypeptide chain. Following the first cleavage, which may be cotranslational, the subunits remain closely associated through undefined noncovalent interactions. These mucins all share a common structural motif, the SEA module that is found in many other membrane‐associated proteins that are released from the… 
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Expansion of divergent SEA domains in cell surface proteins and nucleoporin 54
  • J. Pei, N. Grishin
  • Biology
    Protein science : a publication of the Protein Society
  • 2017
TLDR
By comparative sequence and structural analyses, dystroglycan‐like proteins with SEA domains are identified in Capsaspora owczarzaki of the Filasterea group, one of the closest single‐cell relatives of metazoans.
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TLDR
This work shows that the SEA domain of the human MUC1 transmembrane mucin undergoes a novel type of autoproteolysis, which is catalyzed by conformational stress and the conserved serine hydroxyl.
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TLDR
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High-resolution structure of intramolecularly proteolyzed human mucin-1 SEA domain.
Contribution of the conservative cleavage motif to posttranslational processing of the carboxyl terminal domain of rodent Muc3
TLDR
The present study demonstrates how the conservative cleavage motif LS1KGS2IV1V2 contributes to posttranslational processing through mutagenesis of each residue in the LS1 k GS2V2 motif.
Activity of recombinant cysteine-rich domain proteins derived from the membrane-bound MUC17/Muc3 family mucins.
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Mapping the protein domain structures of the respiratory mucins: a mucin proteome coverage study.
TLDR
The proteome coverage of the mucins responsible for the maintenance and protection of the airway epithelia was investigated, and 43 cleavage sites from 10 different domains of M UC5B and MUC5AC were identified, indicating potential exposure to proteolytic and/or "spontaneous cleavages".
Mucin-like proteins in Drosophila development
TLDR
A new mechanism in organ development, whereby the extent of lumen volume expansion can be regulated by the accumulation of single glycoprotein is revealed, which is essential for epithelial organ development in Drosophila.
Role of N-glycosylation of the SEA module of rodent Muc3 in posttranslational processing of its carboxy-terminal domain.
TLDR
The proteolytic cleavage of the rodent Muc3 SEA module was not affected when it lacked only one, two, or three N-glycans, but was partially inhibited when lacking four, five, and six N- glycans.
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References

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TLDR
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TLDR
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  • Biology
    Protein science : a publication of the Protein Society
  • 1995
TLDR
Using a variety of homology search methods and multiple alignments, a new extracellular module was identified in agrin, enterokinase, and a 63‐kDa sea urchin sperm protein, which contain all O‐glycosidiclinked carbohydrates such as heparan sulfate that contribute considerably to their molecular masses.
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TLDR
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TLDR
It is hypothesize that all membrane resident proteins containing such a “SEA” module will undergo cleavage, thereby generating a receptor–ligand alliance and could well lead to the rational design and identification of molecules that, by binding to one of the cleaved partners, will act either as agonists or antagonists, alter signal transduction and, hence, cellular behavior.
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TLDR
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TLDR
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TLDR
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