LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This entry represents the DG-type SEA domain.Dystroglycan (DG) is an integral membrane receptor linking the extracellular matrix (ECM) and cytoskeleton. Through widespread expression in a variety ofcell types, including muscle, neural and epithelial cells, DG plays diverse and important roles in cell functions from basement membrane assembly totissue morphogenesis and structural integrity. DG is encoded by a single gene and posttranslationally cleaved into two noncovalently associated subunits byautoproteolysis within a distinctive protein motif called an sea urchin- enterokinase-agrin (SEA) domain. The resulting heterodimeris composed of a transmembrane subunit that tethers to the cell surface an extracellular subunit bearing extensive O-linked glycosylation. O-linkedglycosylation of the extracellular DG subunit (alpha-DG) mediates binding to several ECM ligands, including laminins and perlecan. The cleavage of DGelicits a conspicuous change in its ligand-binding activity. Extensive work has demonstrated the importance of alpha-DG glycosylation for DG functions andhow altered alpha-DG glycosylation leads to receptor dysfunction with direct implications for human diseases. However, functions contained within the DGtransmembrane subunit (beta-DG), and the roles of this subunit in human disease, are poorly understood [, ]. The DG-type SEA domain forms thepeptidase S72 family. The ~120-residue DG-type SEA domain is predicted to display a four-stranded antiparallel beta sheet (beta1-beta4) backed by alpha helices (alpha1-alpha4).The cleavage occurs at a bend between the beta2 and beta3 sheets. The cleavage of the DG precursor requires the sequence GSIVV, where cleavage occurs betweenthe glycine and serine [ , ]. |
| Short Name | SEA_DG_dom |
