K. Sritunyalucksana et al., Molecular cloning and characterization of prophenoloxidase in the black tiger shrimp, Penaeus monodon, DEV COMP IM, 23(3), 1999, pp. 179-186
A cDNA encoding shrimp, Penaeus monodon, prophenoloxidase (proPO) was obtai
ned bi screening a hemocyte library by plaque hybridization using a proPO c
DNA fragment from freshwater crayfish, Pacifastacus leniusculus. as a probe
. The 3.002 bp cDNA contains an open reading frame of 2,121 bp and a 881 bp
3'-unsaturated region. The molecular mass of the deduced amino acid sequen
ce (688 amino acids) is 78.700 Da with an estimated pi of 5.8. Two putative
copper binding sites are present and they have a highly conserved sequence
around these sites. No signal peptide was detected in the shrimp proPO, as
has been previously shown to be the case for all arthropod proPOs cloned s
o far. The cleavage site of rymogen activation is likely to be between Arg
44 and Val 45. A tentative complement-like motif (GCGWPQHM) is also present
. Shrimp proPO mRNA is synthesized in the hemocytes and not in the hepatopa
ncreas. Comparison of amino acid sequences showed that shrimp proPO is more
closely related to another crustacean proPO, namely crayfish, than to the
insect proPOs. (C) 1999 Elsevier Science Ltd. All rights reserved.