Molecular cloning and sequence analysis of cDNA encoding flavoridin, a disintegrin from the venom of Trimeresurus flavoviridis.
We isolated a cDNA of 2001bp encoding the full-length precursor of flavoridin, which is one of the four disintegrins in the venom of Trimeresurus flavoviridis, and analyzed the cDNA nucleotide sequence. The deduced amino acid sequence of the open reading frame consisted of a pro-domain (190 residues), a metalloproteinase domain (205 residues), a spacer domain (18 residues) and a disintegrin (flavoridin) domain (70 residues), thus indicating that the flavoridin precursor belongs to the P-II class of snake venom metalloproteinases. The unknown metalloproteinase domain shared strong sequence similarity with HR2a (71.2% identity) and H(2)-proteinase (74.1% identity), a low molecular mass hemorrhagic metalloproteinase and a non-hemorrhagic metalloproteinase in the same snake venom, respectively.
Kishimoto
Masaaki
M
Institute of Medicinal Chemistry, Hoshi University, 2-4-41 Ebara Shinagawaku, Tokyo 142-8501, Japan.
Takahashi
Tomoko
T
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003435:Crotalid Venoms / Q000737:chemistry*; D018076:DNA, Complementary / Q000235:genetics*; D036341:Intercellular Signaling Peptides and Proteins; D008666:Metalloendopeptidases / Q000235:genetics; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics* / Q000302:isolation & purification; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D017841:Trimeresurus
D003435:Crotalid Venoms; D018076:DNA, Complementary; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; C029748:Trimeresurus venoms; C069044:flavoridin protein, Trimeresurus; D008666:Metalloendopeptidases