Cysteine proteinase 1 (CP1), a cathepsin L-like enzyme expressed in the Drosophila melanogaster haemocyte cell line mbn-2.
We have isolated cDNA clones encoding the full-length Drosophila melanogaster cysteine proteinase 1 (CP1). The clones were isolated from the Drosophila melanogaster haemocytic mbn-2 cell line, where the gene is relatively strongly expressed, giving a transcript of 1.6 kb in size. We present the sequence encoding the full-length protein, and deduced the genomic organization of the gene by comparison to previously published genomic partial sequence data. Immunofluorescence shows that CP1 is localized in small granules, probably lysosomes, in mbn-2 cells. The data presented suggest a role for cysteine proteinase in immune functions in insects. It is likely to participate in the degradation of internalized material in phagocytic cells.
Tryselius
Y
Y
Department of Developmental Biology, Stockholm University, Sweden.
Hultmark
D
D
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D056668:Cathepsin L; D002403:Cathepsins / Q000235:genetics*; D002460:Cell Line; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D018076:DNA, Complementary; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000201:enzymology* / Q000235:genetics; D010450:Endopeptidases; D015870:Gene Expression; D017344:Genes, Insect; D006434:Hemocytes / Q000166:cytology / Q000201:enzymology; D019476:Insect Proteins / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D013347:Subcellular Fractions
D018076:DNA, Complementary; D029721:Drosophila Proteins; D019476:Insect Proteins; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; C106944:Cysteine proteinase-1, Drosophila; D056668:Cathepsin L