|Ref Sequence Id||NP_776587.1|
|Amino Acid Lenth||895|
|Protein Existence Status||Reviewed: Experimental evidence at protein level|
|Protein Function||key signaling modulators of cellular architecture, and function during embryonic and post-natal development; play a role in basement membrane formation; role in epithelial morphogenesis in kidney, lung, and salivary gland|
|Biochemical Properties||integral component of the dystrophin glycoprotein complex; α- and ß-dystroglycan are obligate partners; In skeletal muscle, a-dystroglycan binds to the extracellular matrix component laminin α2-chain, whereas the intracellular domain of b-dystroglycan binds to the cytoskeletal protein dystrophin; a-dystroglycan binds laminin-1, agrin, and perlecan|
|Significance in milk||in mammary epithelial cell type DG is essential for receptor-facilitated laminin anchoring and assembly|
|PTMs||heterodimeric glycoprotein- undergoes N-linked and extensive O-linked glycosylation; contains a large mucin-like domain with a number of Ser or Thr residues, which are potential sites for O-glycosylation; Dystroglycan also contains four potential N-linked glycosylation sites, three in -dystroglycan and one in Glycosylated: -dystroglycan ; The O-linked glycoconjugates contain a fairly unique sugar linkage where mannose is directly coupled to serine or threonine in the dystroglycan peptide|
|Significance of PTMs||required for ligand binding and the reaction of monoclonal antibodies|
|Bibliography||1. Ervasti, J. M. and Campbell, K. P. (1993) ‘A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin’, The Journal of Cell Biology, 122(4), pp. 809–823. doi: 10.1083/jcb.122.4.809. |
2. Durbeej, M. and Campbell, K. P. (1999) ‘Biochemical characterization of the epithelial dystroglycan complex.’, The Journal of biological chemistry, 274(37), pp. 26609–16. doi: 10.1074/jbc.274.37.26609.
3. Weir, M. L. et al. (2006) ‘Dystroglycan loss disrupts polarity and beta-casein induction in mammary epithelial cells by perturbing laminin anchoring.’, Journal of cell science, 119(Pt 19), pp. 4047–58. doi: 10.1242/jcs.03103.
4. Ibraghimov-Beskrovnaya, O. et al. (1992) ‘Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix’, Nature, 355(6362), pp. 696–702. doi: 10.1038/355696a0.
5. Smalheiser, N. R. et al. (1998) ‘Structural analysis of sequences O-linked to mannose reveals a novel Lewis X structure in cranin (dystroglycan) purified from sheep brain.’, The Journal of biological chemistry, 273(37), pp. 23698–703. doi: 10.1074/jbc.273.37.23698.
6. Chiba, A. et al. (1997) ‘Structures of Sialylated O -Linked Oligosaccharides of Bovine Peripheral Nerve α-Dystroglycan’, Journal of Biological Chemistry, 272(4), pp. 2156–2162. doi: 10.1074/jbc.272.4.2156.