cDNA sequence of a Drosophila melanogaster gene, Dfur1, encoding a protein structurally related to the subtilisin‐like proprotein processing enzyme furin

Abstract

Screening a genomic library oT Drosophih rwhmgosrer DNA with a human_firrcDNA probe resulted in the isolation of DNA clones thaw apparently belonged to two different DNA regions of the Drosophikr genome. Subsequently. corresponding Drosophih cDNA ciones were isolated. Nucleotide sequence analysis indicated that these cDNA clones originated from two different genes. which were called Djitrl and Djirr2. From overlappihig Dfirl cDNA clones, a composite cDNA could be constructed and analysis of its nucleotide sequence revealed the coding sequence for a protein of 899 amino acid residues. This protein. designated Dfurinl. exhibited striking sequence homology to human furin and contained the same protein domains except for the cysteine-rich region. Furthermore. unlike human furin. Dfurinl possessed an extended amino-terminal region in which a potential transmembranc anchor was present.Subtilisin-like proprotein processing enzyme: Furin; DTurin I: Drosupllilcl rr~c/trr~ogcrs~er

Biosynthesis and secretion of insect lipoprotein: involvement of furin in cleavage of the apoB homolog, apolipophorin-II/I

“…In D. melanogaster, cleavage activity and homology have been demonstrated for the dfurin1 and dfurin2 gene products (30)(31)(32). Furthermore, a furin was cloned from the insect Sf9 cell line (24).…”

Sorting and processing of secretory proteins

“…[212], PC6A [213], PC6B [214] and PC5 [215] (Figure 3). These endoproteases were found in higher vertebrates, but homologous convertases have also been found in molluscs [216], Xenopus laevis [217], Drosophila melanogaster [218,219] and Hydra vulgaris [220]. These convertases have thus been well conserved throughout evolution.…”

Homology modelling of the catalytic domain of human furin

“…Asp46Ala, His87Ala, Asnl88Ala, Ser261Ala or Asp46Asn (Leduc et al, 1992). (Korner et al, 1991); Dm FURlDm FUR2, Drosophila melanogaster furin 1 (Roebroek et al, 1991 and furin 2 ; Ce BLIS, Caenorhabditis elegans blisterin (Peters, 1992); Ls PC2, Lymnea stagnalis PC2 (Smit et al, 1992); Hs PC2, human PC2 ; Hs PC13, human PC1/3 (Smeekens and Steiner, 1990); Mm PC4, mouse PC4 (Nakayama et el., 1992;Seidah et al, 1992); Hs PAC4, human PACE4 (Kiefer et al, 1991); Mm PC56, mouse PC5 (Lusson et al, 1993) and PC6 (Nakagawa et al, 1993); Hv PC3, Hydra vulgaris PC3-like protease (Chan et al, 1992); Y1 XPR6, Yarrowia Zipolytica XPR6 protease (Enderlin and Ogrydziak, 1994); K1 KEXl, Kluyveromyces lactis KEXl protease (Tanguy-Rougeau et al, 1988); Sc KEX2, Saccharomyces cerevisiae KEX2 protease (Mizuno et al, 1988). Residue numbering at the top corresponds to that of mature human furin (Hs FUR).…”