Search by BoMiProt ID - Bomi263


Primary Information

BoMiProt ID Bomi263
Protein Name Dystroglycan
Organism Bos taurus
Uniprot IdO18738
Milk FractionWhey
Ref Sequence Id NP_776587.1
Amino Acid Lenth 895
Molecular Weight 97321
Fasta Sequence https://www.uniprot.org/uniprot/O18738.fasta
Gene Name DAG1
Gene Id 281439
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

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.