We have isolated a new maternal gene called 4G2. 4G2 cDNA encodes a predicted protein of 501 amino acids, and its apparent molecular mass of 61 kDa was determined by SDS-PAGE of 4G2 recombinant protein expressed in E. coli or in vitro translated in rabbit reticulocyte lysate. Amino acid analysis of 4G2 revealed the RGD and LDV motif with a potential cell attachment activity. The open reading frames (ORF) also contained a consensus bipartite nuclear localization signal (NLS). There were number of expressed tag sequences (ESTs) from Drosophila, zebrafish, chicken, mouse, and human origin that encode a high degree of identity to the predicted 4G2 protein, thereby suggesting that 4G2 may constitute a novel gene family whose function has not been elucidated. We also present evidence that 4G2 transcript is maternally synthesized in stage IV oocyte, localized to animal hemisphere of egg, and zygotically reactivated in mid-neurula stage.