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The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed primarily of three or four glycoproteins with various functions during fertilization and preimplantation development. The nascent protein contains a N-terminal signal peptide sequence, a conserved ZP domain, a consensus furin cleavage site, and a C-terminal transmembrane domain. It is hypothesized that furin cleavage results in release of the mature protein from the plasma membrane for subsequent incorporation into the zona pellucida matrix. However, the requirement for furin cleavage in this process remains controversial based on mouse studies. Previously, this gene has been referred to as ZP1 or ZPB and thought to have similar functions as mouse Zp1. However, a human gene with higher similarity and chromosomal synteny to mouse Zp1 has been assigned the symbol ZP1 and this gene has beendomain:The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.,function:The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP4 may act as a sperm receptor.,PTM:Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.,similarity:Belongs to the ZP domain family. ZPB subfamily.,similarity:Contains 1 P-type (trefoil) domain.,similarity:Contains 1 ZP domain.,tissue specificity:Oocytes.,
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