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. 1972 Feb;69(2):431–434. doi: 10.1073/pnas.69.2.431

Evolution of Neurophysin Proteins: The Partial Sequence of Bovine Neurophysin-I

J D Capra *, J M Kehoe *, D Kotelchuck †, R Walter †, E Breslow ‡
PMCID: PMC426473  PMID: 4501123

Abstract

The sequence of the first 50 amino-acid residues of bovine neurophysin-I was determined. A comparison of this sequence with that of the 97-residue bovine neurophysin-II and the 92-residue porcine neurophysin-I molecules reveals a high degree of homology among these proteins. It is suggested that the binding site of neurophysin proteins for neurohypophyseal hormones is located in the middle portion of these molecules, where their sequences are virtually identical. The sequence data, as well as the occurrence of at least two neurophysins in both the pig and the cow, suggest that each species inherited at least two structural genes controlling the synthesis of these proteins. The most striking finding in the study was the observation of internal sequence homologies within the neurophysins. This result implies that these molecules arose by way of a series of partial gene duplications of a primitive gene that coded for a smaller ancestral protein.

Keywords: vasopressin, oxytocin, carrier proteins, automated amino-acid-sequence analysis, homology, protein evolution

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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