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{
"metadata": {
"accession": "PS51699",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR030398",
"hierarchy": null,
"name": {
"name": "DG-type SEA domain profile",
"short": "SEA_DG"
},
"description": [
{
"text": "<p>Dystroglycan (DG) is an integral membrane receptor linking the extracellular\nmatrix (ECM) and cytoskeleton. Through widespread expression in a variety of\ncell types, including muscle, neural and epithelial cells, DG plays diverse\nand important roles in cell functions from basement membrane assembly to\ntissue morphogenesis and structural integrity. DG is encoded by a single gene\nand posttranslationally cleaved into two noncovalently associated subunits by\nautoproteolysis within a distinctive protein motif called an sea urchin-\nenterokinase-agrin (SEA) domain. The resulting heterodimer\nis composed of a transmembrane subunit that tethers to the cell surface an\nextracellular subunit bearing extensive O-linked glycosylation. O-linked\nglycosylation of the extracellular DG subunit (alpha-DG) mediates binding to\nseveral ECM ligands, including laminins and perlecan. The cleavage of DG\nelicits a conspicuous change in its ligand-binding activity. Extensive work\nhas demonstrated the importance of alpha-DG glycosylation for DG functions and\nhow altered alpha-DG glycosylation leads to receptor dysfunction with direct\nimplications for human diseases. However, functions contained within the DG\ntransmembrane subunit (beta-DG), and the roles of this subunit in human\ndisease, are poorly understood [[cite:PUB00072578]][[cite:PUB00072579]]. The DG-type SEA domain forms the\npeptidase S72 family [E1].\n\nThe ~120-residue DG-type SEA domain is predicted to display a four-stranded\nantiparallel beta sheet (beta1-beta4) backed by alpha helices (alpha1-alpha4).\nThe cleavage occurs at a bend between the beta2 and beta3 sheets. The cleavage\nof the DG precursor requires the sequence GSIVV, where cleavage occurs between\nthe glycine and serine [[cite:PUB00072578]][[cite:PUB00072579]].\n\nThe profile we developed covers the entire DG-type SEA domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00072579": {
"PMID": 18764929,
"ISBN": null,
"volume": "9",
"issue": "12",
"year": 2008,
"title": "Nuclear translocation of beta-dystroglycan reveals a distinctive trafficking pattern of autoproteolyzed mucins.",
"URL": null,
"raw_pages": "2063-72",
"medline_journal": "Traffic",
"ISO_journal": "Traffic",
"authors": [
"Oppizzi ML",
"Akhavan A",
"Singh M",
"Fata JE",
"Muschler JL."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1600-0854.2008.00822.x"
},
"PUB00072578": {
"PMID": 17905726,
"ISBN": null,
"volume": "22",
"issue": "2",
"year": 2008,
"title": "SEA domain proteolysis determines the functional composition of dystroglycan.",
"URL": null,
"raw_pages": "612-21",
"medline_journal": "FASEB J",
"ISO_journal": "FASEB J.",
"authors": [
"Akhavan A",
"Crivelli SN",
"Singh M",
"Lingappa VR",
"Muschler JL."
],
"DOI_URL": "http://dx.doi.org/10.1096/fj.07-8354com"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 2674,
"pathways": 0,
"proteins": 2092,
"proteomes": 1135,
"sets": 0,
"structural_models": {
"alphafold": 1730,
"bfvd": 0
},
"structures": 3,
"taxa": 3921
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
