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http://purl.uniprot.org/citations/15132736http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15132736http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15132736http://www.w3.org/2000/01/rdf-schema#comment"The mollusc shell is a hard tissue consisting of calcium carbonate and organic matrices. The organic matrices are believed to play important roles in shell formation. In the present study, we extracted and purified a novel matrix protein, named Prismalin-14, from the acid-insoluble fraction of the prismatic layer of the shell of the Japanese pearl oyster (Pinctada fucata), and determined its whole amino acid sequence by a combination of amino acid sequence analysis and MS analysis of the intact protein and its enzymic digests. Prismalin-14 consisted of 105 amino acid residues, including PIYR repeats, a Gly/Tyr-rich region and N- and C-terminal Asp-rich regions. Prismalin-14 showed inhibitory activity on calcium carbonate precipitation and calcium-binding activity in vitro. The scanning electron microscopy images revealed that Prismalin-14 affected the crystallization of calcium carbonate in vitro. A cDNA encoding Prismalin-14 was cloned and its expression was analysed. The amino acid sequence deduced from the nucleotide sequence of Prismalin-14 cDNA was identical with that determined by peptide sequencing. Northern-blot analysis showed that a Prismalin-14 mRNA was expressed only at the mantle edge. In situ hybridization demonstrated that a Prismalin-14 mRNA was expressed strongly in the inner side of the outer fold of the mantle. These results suggest that Prismalin-14 is a framework protein that plays an important role in the regulation of calcification of the prismatic layer of the shell."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.org/dc/terms/identifier"doi:10.1042/bj20040319"xsd:string
http://purl.uniprot.org/citations/15132736http://purl.org/dc/terms/identifier"doi:10.1042/bj20040319"xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Inoue H."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Inoue H."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Kogure T."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Kogure T."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Suzuki M."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Suzuki M."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Ozaki N."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Ozaki N."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Nagasawa H."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Nagasawa H."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Tohse H."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Tohse H."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Murayama E."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/author"Murayama E."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/pages"205-213"xsd:string
http://purl.uniprot.org/citations/15132736http://purl.uniprot.org/core/pages"205-213"xsd:string