The formation of the mollusk nacre layer involves the assembly and organization of mineral nanoparticles into fracture-toughened mesoscale-sized aragonite tablets that possess intracrystalline nanoporosities. At least one nacre protein family， known as the framework proteome， is strategically located as part of a macromolecular coating around each nacre tablet and is believed to participate in tablet formation. Here， we report new studies of a recombinant form (rPif97) of a unique Japanese pearl oyster (Pinctada fucata) nacre framework biomineralization protein， Pif97. This unique protein possesses both a von Willlebrand factor type A domain (vWA， F23-Y161) and a Peritrophin A chitin-binding domain (PAC， E234-D298). rPif97 self-associates or aggregates to form amorphous protein phases that organize both amorphous and single-crystal calcium carbonate nanoparticles in vitro. Further， in the presence of nucleating calcite crystals， rPif97 protein phases deposit onto these crystals and become occluded over time， forming nanochambers within the crystal interior. The formation of these mineral-modifying amorphous protein phases is linked to the presence of intrinsic disorder and amyloid-like cross-β-strand aggregation-prone regions， and three-dimensional modeling indicates that both the vWA and PAC domains are accessible for intermolecular interactions. Thus， the vWA- and PAC-containing Pif97 protein exhibits key functionalities that would allow its participation in mollusk nacre layer tablet assembly and porosity formation.