A hatching enzyme substrate in the Xenopus laevis egg envelope is a high molecular weight ZPA homolog.
The Xenopus laevis egg envelope is composed of six or more glycoproteins, three of which have been cloned and identified as the mammalian homologs ZPA (ZP2), ZPB (ZP1) and ZPC (ZP3). The remaining glycoproteins are a triplet of high molecular weight components that are selectively hydrolyzed by the hatching enzyme. We have isolated one of these proteins and cloned its cDNA. The mRNA for the protein was found to be expressed only in early stage oocytes, as are other envelope components. From the deduced amino acid sequence, it was indicated to be a secreted glycoprotein with a characteristic ZP domain in the C-terminal half of the molecule. The N-terminal half was unrelated to any known glycoprotein. Comparative sequence analysis of the ZP domain indicated that it was derived from an ancestor of ZPA and ZPB, with the greatest identity to ZPA. This envelope component has been designated ZPAX.
Lindsay
L L
LL
Section of Molecular & Cellular Biology, University of California, Davis, California 95616, USA. llindsay@ucdavis.edu
Wallace
M A
MA
Hedrick
J L
JL
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005260:Female; D017403:In Situ Hybridization; D008969:Molecular Sequence Data; D009865:Oocytes / Q000737:chemistry / Q000166:cytology*; D010053:Ovary / Q000166:cytology; D016415:Sequence Alignment; D014982:Xenopus laevis; D015044:Zona Pellucida / Q000737:chemistry*