Cloning and sequence analysis of hypothalamic cDNA encoding Xenopus preproneuropeptide Y.
Neuropeptide Y (NPY) consists of 36 amino acids and it constitutes one of the most conserved neuropeptides. Here we report the complete sequence of the first amphibian NPY precursor by cloning of a hypothalamic cDNA encoding Xenopus laevis preproNPY. The overall amino acid sequence identity between Xenopus and other known NPY precursor proteins ranges from 59% (fish) to 82% (chicken); a low degree of identity was found for the signal peptide sequence (32-75%) and for the carboxy-terminal peptide of NPY (CPON; 43-73%), while the NPY peptide sequence itself constitutes the most highly-conserved region (89-100%) within the preproNPY structure.
van Riel
M C
MC
Department of Animal Physiology, University of Nijmegen, The Netherlands.
Tuinhof
R
R
Roubos
E W
EW
Martens
G J
GJ
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D008969:Molecular Sequence Data; D009478:Neuropeptide Y / Q000737:chemistry / Q000235:genetics*; D021382:Protein Sorting Signals / Q000737:chemistry; D016415:Sequence Alignment; D014982:Xenopus laevis / Q000235:genetics*
D009478:Neuropeptide Y; D021382:Protein Sorting Signals; D004247:DNA