Structural characterization of a Lymnaea putative endoprotease related to human furin. Smit, A. B., Spijker, S., Nagle, G. T., Knock, S. L., Kurosky, A., & Geraerts, W. P. FEBS Letters, 343(1):27–31, Elsevier, apr, 1994. ![Structural characterization of a Lymnaea putative endoprotease related to human furin [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex A number of peptides have been identified in the central nervous system of the freshwater snail, Lymnaea stagnalis, that function as hormones and neurotransmitters/neuromodulators. These peptides are typically proteolytically processed from larger prohormones mostly at sites composed of single or multiple basic amino acid residues. Previously we demonstrated a diversity of putative prohormone convertases that may be involved in prohormone processing in the Lymnaea brain. In the present report, we have characterized a cDNA clone encoding a putative endoprotease of 837 amino acids. The primary structure of the endoprotease (Lfur2) was comparable to that of human furin and contained a putative catalytic domain, a Cys-rich domain, and a transmembrane region. The catalytic domain of Lfur2 demonstrated about 70% residue identity when compared with human furin, PACE4 and Drosophila Dfur1 and dKLIP-1. The Lfur2 gene was expressed in the central nervous system as well as various peripheral tissues of Lymnaea. © 1994.
@article{pop00286,
abstract = {A number of peptides have been identified in the central nervous system of the freshwater snail, Lymnaea stagnalis, that function as hormones and neurotransmitters/neuromodulators. These peptides are typically proteolytically processed from larger prohormones mostly at sites composed of single or multiple basic amino acid residues. Previously we demonstrated a diversity of putative prohormone convertases that may be involved in prohormone processing in the Lymnaea brain. In the present report, we have characterized a cDNA clone encoding a putative endoprotease of 837 amino acids. The primary structure of the endoprotease (Lfur2) was comparable to that of human furin and contained a putative catalytic domain, a Cys-rich domain, and a transmembrane region. The catalytic domain of Lfur2 demonstrated about 70{\%} residue identity when compared with human furin, PACE4 and Drosophila Dfur1 and dKLIP-1. The Lfur2 gene was expressed in the central nervous system as well as various peripheral tissues of Lymnaea. {\textcopyright} 1994.},
annote = {Query date: 2020-06-29 13:05:30},
author = {Smit, August B. and Spijker, Sabine and Nagle, Gregg T. and Knock, Susan L. and Kurosky, Alexander and Geraerts, Wijnand P.M.},
doi = {10.1016/0014-5793(94)80600-4},
issn = {00145793},
journal = {FEBS Letters},
keywords = {Central nervous system,Furin-related endoprotease,Lymnaeastagnalis,Mollusc,Polymerase chain reaction,cDNA cloning},
month = {apr},
number = {1},
pages = {27--31},
publisher = {Elsevier},
title = {{Structural characterization of a Lymnaea putative endoprotease related to human furin}},
url = {https://www.sciencedirect.com/science/article/pii/0014579394806004 http://doi.wiley.com/10.1016/0014-5793{\%}2894{\%}2980600-4},
volume = {343},
year = {1994}
}
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The primary structure of the endoprotease (Lfur2) was comparable to that of human furin and contained a putative catalytic domain, a Cys-rich domain, and a transmembrane region. The catalytic domain of Lfur2 demonstrated about 70% residue identity when compared with human furin, PACE4 and Drosophila Dfur1 and dKLIP-1. 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