Primary Information |
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BoMiProt ID | Bomi263 |
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Protein Name | Dystroglycan |
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Organism | Bos taurus |
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Uniprot ID | O18738 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_776587.1 |
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Aminoacid Length | 895 |
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Molecular Weight | 97321 |
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FASTA Sequence |
Download |
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Gene Name | DAG1 |
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Gene ID | 281439 |
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Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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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. Dystroglycan functions as part of a synaptic partner recognition complex that is required early for CCK+ interneuron development in the forebrain. |
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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 |
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Significance in milk | in mammary epithelial cell type DG is essential
for receptor-facilitated laminin anchoring and assembly |
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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 |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | 164-172,323-362,381-462,484-490,726-746,827-841 |
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DisProt Annotation | |
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TM Helix Prediction | 1TMH;(753-775) |
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Significance of PTMs | required for
ligand binding and the reaction of monoclonal antibodies |
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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. 7.Miller DS, Wright KM. Neuronal Dystroglycan regulates postnatal development of CCK/cannabinoid receptor-1 interneurons. Neural Dev. 2021 Aug 6;16(1):4. doi: 10.1186/s13064-021-00153-1. PMID: 34362433; PMCID: PMC8349015. |