Poult. Sci.
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Poultry Science, Vol 82, Issue 2, 242-250
Copyright © 2003 by Poultry Science Association


Articles

Cloning and characterization of HEP21, a new member of the uPAR/Ly6 protein superfamily predominantly expressed in hen egg white

F Nau, C Guerin-Dubiard, C Desert, J Gautron, S Bouton, J Gribonval, and S Lagarrigue

UMR INRA-ENSAR 1055 Physico-chimie et Technologie des Ovoproduits, Pole d'Enseignement Superieur et de Recherche Agronomique de Rennes, 65 rue de Saint-Brieuc CS 84215-35042 Rennes cedex, France. nau@agrorennes.educagri.fr

Using two-dimensional (2D)-PAGE, partial protein internal sequencing, and PCR with degenerate primers, we cloned a novel cDNA named HEP21 from hen egg white. The 0.5-kb cDNA encodes a 106 amino acid protein with a cysteine spacing pattern suggesting that HEP21 is a new member of the uPAR/CD59/Ly-6/ snake neurotoxin superfamily. The closest homology of HEP21 is to mouse Ly-6C. Unlike most members of this protein family, HEP21 is not glycosylphosphatidylinositol (GPI)-anchored but is a secreted protein, as indicated by its localization and the presence of a signal peptide in its sequence. Moreover, HEP21 appears as an original member of this protein superfamily because it is predominantly expressed in a tissue, i.e., the oviduct, and especially the magnum where the egg white components are secreted.


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