Structural characterization of a Lymnaea putative endoprotease related to human furin.
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 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.
Smit
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AB
Graduate School Neurosciences Amsterdam, Research Institute Neurosciences Vrije Universiteit, Faculty of Biology, The Netherlands.
Spijker
S
S
Nagle
G T
GT
Knock
S L
SL
Kurosky
A
A
Geraerts
W P
WP
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary; D045683:Furin; D006801:Humans; D008195:Lymnaea / Q000201:enzymology*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics; D013381:Subtilisins / Q000737:chemistry*
D018076:DNA, Complementary; C086863:Lymnaea furin2; D012697:Serine Endopeptidases; D013381:Subtilisins; D045683:Furin