{PDOC00492} {PS00569; MYELIN_MBP} {BEGIN} ********************************** * Myelin basic protein signature * ********************************** Myelin basic protein (MBP) [1,2] is an important hydrophilic protein which may function to maintain proper structure of myelin. MBP interacts with myelin lipids both electrostatically and by hydrophobic interactions. In mammals various forms of MBP exist which are produced by the alternative splicing of a single gene; these forms differ by the presence or the absence of short (10 to 20 residues) peptides in various internal locations in the sequence. The major form of MBP is generally a protein of about 18.5 Kd (170 residues). MBP is the target of many post-translational modifications: it is N-terminally acetylated, methylated on an arginine residue, phosphorylated by various serine/threonine protein-kinases, and deamidated on some glutamine residues. As a signature pattern for MBP we selected the best conserved part of the protein, a perfectly conserved heptapeptide. -Consensus pattern: V-V-H-F-F-K-N -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 1991 / First entry. [ 1] Deber C.M., Reynolds S.J. "Central nervous system myelin: structure, function, and pathology." Clin. Biochem. 24:113-134(1991). PubMed=1710177 [ 2] Inouye H., Kirschner D.A. "Folding and function of the myelin proteins from primary sequence data." J. Neurosci. Res. 28:1-17(1991). PubMed=1710279 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}