| General information | | DisProt: | DP00491_C002 | | Name: | Beta-dystroglycan [cleavage product 2] | | Synonym(s): | DAG1_MOUSE
Beta-DG
cleavage product 2 of Dystroglycan
| | First appeared in release: | Release 3.2 (05/26/2006) | | UniProt: | Q62165 | | UniGene: | Mm.477413 | | SwissProt: | DAG1_MOUSE | | TrEMBL: | | | NCBI (GI): | 14916984 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 242 | | Percent disordered: | 40% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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SIVVEWTNNT LPLEPCPKEQ IIGLSRRIAD ENGKPRPAFS NALEPDFKAL SIAVTGSGSC - 60
RHLQFIPVAP PSPGSSAAPA TEVPDRDPEK SSEDDVYLHT VIPAVVVAAI LLIAGIIAMI - 120
CYRKKRKGKL TLEDQATFIK KGVPIIFADE LDDSKPPPSS SMPLILQEEK APLPPPEYPN - 180
QSMPETTPLN QDTVGEYTPL RDEDPNAPPY QPPPPFTAPM EGKGSRPKNM TPYRSPPPYV - 240
PP
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| Functional narrative |
Forms part of the dystrophin-associated protein complex (DAPC) which may link the cytoskeleton to the extracellular matrix. Interacts with AGR2 and AGR3, as well as SGCD. (UniProt). Beta-dystroglycan is cleavage product 2 of Dystroglycan, comprised of aa 652-893 of the polyprotein.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Beta-dystroglycan ectodomain | | Location: | 3 - 99 | | Length: | 97 | | Region sequence: |
VVEWTNNTLPLEPCPKEQIIGLSRRIADENGKPRPAFSNALEPDFKALSIAVTGSGSCRH
LQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVYLH | | Modification type: | Engineered
Fragment
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (pH: 6.5; CaCl2 1.25 mM; D2O 5 %; MgCl2 1 mM; NaCl 0.15 M; NaH2PO4 20 mM)
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7; Phosphate buffer 5 mM)
- Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (pH: 7; NaCl 0.1 M; phosphate buffer 10 mM)
| References:
- Boffi A, Bozzi M, Sciandra F, Woellner C, Bigotti MG, Ilari A, Brancaccio A. "Plasticity of secondary structure in the N-terminal region of beta-dystroglycan." Biochim Biophys Acta. 2001; 1546(1): 114-21. PubMed: 11257514
- Bozzi M, Bianchi M, Sciandra F, Paci M, Giardina B, Brancaccio A, Cicero DO. "Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan." Biochemistry. 2003; 42(46): 13717-24. PubMed: 14622018
| Comments:This protein is highly disordered, but steady-state NOE experiments indicate that the protein presents two regions of different mobility. The first one, between residues 659-722 of the polyprotein (N8-P71 of cleavage product 2), is characterized by a limited degree of mobility, whereas the C-terminal portion, containing about 30 amino acids, is highly flexible.
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| References |
- Williamson RA, Henry MD, Daniels KJ, Hrstka RF, Lee JC, Sunada Y, Ibraghimov-Beskrovnaya O, Campbell KP. "Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice." Hum Mol Genet. 1997; 6(6): 831-41. PubMed: 9175728
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| Comments |
Additional UniGene ID: Mm.7524
Previous entry DP00491 has been split into polyprotein (DP00491) and cleavage product
DP00491_C002. Disorder is characterized on the cleavage product.
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