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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1994-5-20
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pubmed:databankReference | |
pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
343
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27-31
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8163012-Amino Acid Sequence,
pubmed-meshheading:8163012-Animals,
pubmed-meshheading:8163012-Base Sequence,
pubmed-meshheading:8163012-DNA, Complementary,
pubmed-meshheading:8163012-Furin,
pubmed-meshheading:8163012-Humans,
pubmed-meshheading:8163012-Lymnaea,
pubmed-meshheading:8163012-Molecular Sequence Data,
pubmed-meshheading:8163012-Sequence Alignment,
pubmed-meshheading:8163012-Serine Endopeptidases,
pubmed-meshheading:8163012-Subtilisins
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pubmed:year |
1994
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pubmed:articleTitle |
Structural characterization of a Lymnaea putative endoprotease related to human furin.
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pubmed:affiliation |
Graduate School Neurosciences Amsterdam, Research Institute Neurosciences Vrije Universiteit, Faculty of Biology, The Netherlands.
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pubmed:publicationType |
Journal Article
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