title: Cloning and sequence analysis of cDNA for porcine beta-neo-endorphin/dynorphin precursor.
abstract: The primary structure of a precursor protein that contains beta-neo-endorphin, dynorphin and a third leucine-enkephalin sequence with a carboxyl extension has been deduced from the nucleotide sequence of cloned DNA complementary to the porcine hypothalamic mRNA encoding it. The three peptides are each bounded by Lys-Arg. This precursor protein, like adrenal preproenkephalin and the corticotropin/beta-lipotropin precursor, comprises multiple repetitive units and a cysteine-containing amino-terminal sequence preceded by a signal peptide.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis; D004262:DNA Restriction Enzymes; D004274:DNA, Recombinant; D004399:Dynorphins; D004723:Endorphins / Q000235:genetics*; D004743:Enkephalin, Leucine; D004745:Enkephalins / Q000235:genetics*; D007031:Hypothalamus; D011498:Protein Precursors / Q000235:genetics; D012333:RNA, Messenger / Q000032:analysis; D013552:Swine; D001615:beta-Endorphin / Q000031:analogs & derivatives*
chemical_list: D004274:DNA, Recombinant; D004723:Endorphins; D004745:Enkephalins; D011498:Protein Precursors; D012333:RNA, Messenger; D004743:Enkephalin, Leucine; D001615:beta-Endorphin; D004399:Dynorphins; C030719:beta-neo-endorphin; D004247:DNA; D004262:DNA Restriction Enzymes