Structure and maturation process of pro-opiomelanocortin: a model for other neuropeptides.
Pro-opiomelanocortin has a signal peptide of 26 amino acids which is very hydrophobic like the other signal peptides. The large precursor has two forms which differ in their carbohydrate content. The presence of pairs of amino acids at the proposed sites of cleavage to release ACTH, beta-MSH and endorphin is a feature described in 1967 for beta-MSH and the C-terminal fragment which is now known as beta-endorphin. It is proposed that other neuropeptides will be biosynthesized through a similar type of processing.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000096:biosynthesis; D000818:Animals; D004589:Electrophoresis, Disc; D008297:Male; D008715:Methionine / Q000378:metabolism; D010455:Peptides / Q000302:isolation & purification; D010649:Phenylalanine / Q000378:metabolism; D010902:Pituitary Gland / Q000166:cytology / Q000378:metabolism*; D010908:Pituitary Hormones, Anterior / Q000378:metabolism*; D011333:Pro-Opiomelanocortin; D011498:Protein Precursors / Q000378:metabolism*; D051381:Rats
D000596:Amino Acids; D010455:Peptides; D010908:Pituitary Hormones, Anterior; D011498:Protein Precursors; D010649:Phenylalanine; D011333:Pro-Opiomelanocortin; D008715:Methionine