Molecular Biology and Evolution, Vol 14, 266-276, Copyright © 1997 by Society for Molecular Biology and Evolution
G Durstewitz and NB Terwilliger
The complete cDNA sequence and protein reading frame of a developmentally
regulated hemocyanin subunit in the Dungeness crab (Cancer magister) is
presented. The protein sequence is aligned with 18 potentially homologous
hemocyanin-type proteins displaying apparent sequence similarities.
Functional domains are identified, and a comparison of predicted
hydrophilicities, surface probabilities, and regional backbone
flexibilities provides evidence for a remarkable degree of structural
conservation among the proteins surveyed. Parsimony analysis of the protein
sequence alignment identifies four monophyletic groups on the arthropodan
branch of the hemocyanin gene tree: crustacean hemocyanins, insect
hexamerins, chelicerate hemocyanins, and arthropodan prophenoloxidases.
They form a monophyletic group relative to molluscan hemocyanins and
nonarthropodan tyrosinases. Arthropodan prophenoloxidases, although
functionally similar to tyrosinases, appear to belong to the arthropodan
hexamer- type hemolymph proteins as opposed to molluscan hemocyanins and
tyrosinases.
ORIGINAL ARTICLE
cDNA cloning of a developmentally regulated hemocyanin subunit in the crustacean Cancer magister and phylogenetic analysis of the hemocyanin gene family
Oregon Institute of Marine Biology, Charleston, Oregon 97420, USA.
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