Isolation of a cDNA encoding a Kex2-like endoprotease with homology to furin from the nematode Caenorhabditis elegans.
A cDNA was isolated from the nematode Caenorhabditis elegans that encodes an endoprotease which is a member of the Kex2 family of serine endoproteases. Degenerate oligonucleotide primers were designed based on conserved regions within the active sites of known Kex2-like endoproteases, and were used for reverse transcription-polymerase chain reaction (RT-PCR) of poly(A)+RNA isolated from C. elegans. A PCR product was isolated that had homology to the active sites of known furin endoproteases, and was used as a probe to screen a C. elegans cDNA library. A Kex2-like endoprotease (CelfurPC) which encoded a 692-amino-acid pre-proendoprotease, was identified. The deduced amino acid sequence for the catalytic domain of CelfurPC is homologous to the known Kex2-like endoproteases, with strongest structural homology to the furin/PACE4 family. However, all furins and PACE4 proteins contain a characteristic cysteine-rich domain, and all furins contain a transmembrane domain, neither of which is present in the CelfurPC protein. CelfurPC may thus represent a new class of Kex2-like endoprotease.
Gómez-Saladín
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Department of Physiology and Biophysics, University of Miami School of Medicine, FL 33101, USA.
Luebke
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Wilson
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Dickerson
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017173:Caenorhabditis elegans / Q000201:enzymology / Q000235:genetics*; D018076:DNA, Complementary / Q000235:genetics* / Q000302:isolation & purification; D045683:Furin; D008969:Molecular Sequence Data; D043484:Proprotein Convertases; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013381:Subtilisins / Q000235:genetics*
D018076:DNA, Complementary; D029701:Saccharomyces cerevisiae Proteins; D043484:Proprotein Convertases; D013381:Subtilisins; C058751:KEX2 protein, S cerevisiae; D045683:Furin