Genomics, evolution and biological functions of the pacifastin peptide family: a conserved serine protease inhibitor family in arthropods.
The last decade, a new serine protease inhibitor family has been described in arthropods. Eight members were purified from the locusts Locusta migratoria (LMPI-1-2 and HI) and Schistocerca gregaria (SGPI-1-5). The light chain of the heterodimeric protease inhibitor pacifastin, from the freshwater crayfish Pacifastacus leniusculus, was found to be composed of nine consecutive inhibitory domains (PLDs). These domains share a pattern of six conserved cysteine residues (Cys-Xaa(9-12)-Cys-Asn-Xaa-Cys-Xaa-Cys-Xaa(2-3)-Gly-Xaa(3-6)-Cys-Thr-Xaa(3)-Cys) with the locust inhibitors. Via cDNA cloning, eight pacifastin-related precursors have been identified in locusts. Interestingly, additional pacifastin-related precursors have been identified in Diptera, Lepidoptera and Coleoptera utilising an in silico data mining approach.
Simonet
Gert
G
Laboratory for Developmental Physiology and Molecular Biology, Genomics and Proteomics, Zoological Institute, K.U. Leuven, B-3000, Leuven, Belgium. Gert.simonet@bio.kuleuven.ac.be
Claeys
Ilse
I
Franssens
Vanessa
V
De Loof
Arnold
A
Broeck
Jozef Vanden
JV
D000595:Amino Acid Sequence; D000818:Animals; D001181:Arthropods / Q000737:chemistry* / Q000235:genetics; D001483:Base Sequence; D017124:Conserved Sequence; D019143:Evolution, Molecular; D023281:Genomics; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D011506:Proteins; D015842:Serine Proteinase Inhibitors; C106709:pacifastin