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XB-ART-22821
Biochem Biophys Res Commun 1993 Feb 15;1903:948-51.
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Cloning and sequence analysis of hypothalamic cDNA encoding Xenopus preproneuropeptide Y.

van Riel MC , Tuinhof R , Roubos EW , Martens GJ .


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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.

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Species referenced: Xenopus laevis
Genes referenced: npy