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J. Biol. Chem., Vol. 265, Issue 36, 22075-22078, Dec, 1990
K Hatsuzawa, M Hosaka, T Nakagawa, M Nagase, A Shoda, K Murakami and K Nakayama
We have cloned and sequenced a mouse cDNA encoding the 793-residue amino
acid sequence of furin, which is a protein homologous to the yeast Kex2
protease. The entire sequence is 94% identical to that of human furin, and
it contains the 289-residue sequence of the subtilisin- like catalytic
domain. Within this region, 99, 64, and 53% of the amino acids are
identical to those of human furin, human PC2 (the other mammalian Kex2-like
protein), and yeast Kex2, respectively. It has been proposed that furin is
a mammalian prohormone processing enzyme which cleaves precursors at paired
basic amino acids, based on the fact that the Kex2 protease is responsible
for processing of alpha-mating factor and killer toxin precursors at
dibasic sites. However, Northern blot analysis has revealed that a furin
mRNA transcript is present in all tested mouse tissues and culture cell
lines, including those known not to process prohormones. Moreover, when
furin and a prohormone, prorenin, have been coexpressed in mammalian cells
by DNA transfection, no processing has been observed. These observations
fail to show a role for furin, a Kex2-like mammalian protease, in
prohormone processing.
Structure and expression of mouse furin, a yeast Kex2-related protease. Lack of processing of coexpressed prorenin in GH4C1 cells
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
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