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• W2013700778 abstract "Neuropeptides containing the C-terminal sequence Arg-Phe-NH2 are an important group of hormones mediating or modulating neuronal communication. Arg-Phe-NH2 peptides are abundant in evolutionarily old nervous systems such as those of coelenterates, the lowest animal group having a nervous system. Here, we have cloned the precursor protein for the anthozoan neuropeptide Antho-RFamide (< Glu-Gly-Arg-Phe-NH2) from the sea pansy Renilla köllikeri. This precursor contains 36 copies of immature Antho-RFamide (Gln-Gly-Arg-Phe-Gly) and two additional putative neuropeptide sequences, which are regularly distributed over the precursor protein. Of the 36 Antho-RFamide sequences, 29 copies are separated by the five amino acid spacer sequence Arg-Glu/Gly-Asn/Ser/Asp-Glu/Lys-Glu. This implicates processing at single Arg and single Glu residues. Endoproteolytic cleavage at the C-terminal side of paired or single basic residues is a well known initial step in the maturation of precursor proteins. Cleavage at the C-terminal side of acidic residues, however, is unusual and must be catalyzed by a new type of processing enzyme. This processing enzyme is most likely to be an endoprotease, because the simplest way to generate Antho-RFamide is by endoproteolytic cleavage at the C-terminal side of Glu residues. The enzyme could also be an aminopeptidase, but in this case other proteases must be involved. As a possible alternative, one single unspecific aminopeptidase could cleave at Glu, Asp, Gly, Asn, Ser, and possibly also at other residues, and thus liberate all Antho-RFamide sequences. The processing of one precursor molecule probably yields 38 neuropeptides.(ABSTRACT TRUNCATED AT 250 WORDS)" @default.
• W2013700778 created "2016-06-24" @default.
• W2013700778 creator A5036928003 @default.
• W2013700778 creator A5043006822 @default.
• W2013700778 date "2008-06-28" @default.
• W2013700778 modified "2023-09-26" @default.
• W2013700778 title "Primary Structure of the Precursor for the Anthozoan Neuropeptide Antho-RFamide from Renilla köllikeri: Evidence for Unusual Processing Enzymes" @default.
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• W2013700778 doi "https://doi.org/10.1046/j.1471-4159.1994.62031214.x" @default.
• W2013700778 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7906718" @default.
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