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http://purl.uniprot.org/citations/17317927http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17317927http://www.w3.org/2000/01/rdf-schema#comment"Carboxypeptidase Y (CPY) inhibitor (I(C)) and its homologous protein (I(C)h) are thought to be members of the phosphatidylethanolamine-binding protein (PEBP) family of Saccharomyces cerevisiae. The biochemical characterization of I(C) and its inhibition mode toward CPY were recently reported, but I(C)h has not been characterized. The molecular mass of I(C)h was determined to be 22,033.7. The N-terminal Met1 was cleaved and the amino group of Ser2 was acetylated. I(C)h is folded as a monomeric beta-protein and is devoid of disulfide bonds. It has no inhibitory activity toward CPY, and it does not form a complex with CPY. I(C)h was exclusively expressed in the early log phase, whereas I(C) was expressed in the logarithmic and stationary phase. The intracellular localization of I(C)h was different from that of I(C). These findings provide insights into the physiological functions of I(C)h."xsd:string
http://purl.uniprot.org/citations/17317927http://purl.org/dc/terms/identifier"doi:10.1271/bbb.60528"xsd:string
http://purl.uniprot.org/citations/17317927http://purl.uniprot.org/core/author"Fukada H."xsd:string
http://purl.uniprot.org/citations/17317927http://purl.uniprot.org/core/author"Kato M."xsd:string
http://purl.uniprot.org/citations/17317927http://purl.uniprot.org/core/author"Ueda M."xsd:string
http://purl.uniprot.org/citations/17317927http://purl.uniprot.org/core/author"Nagayama M."xsd:string
http://purl.uniprot.org/citations/17317927http://purl.uniprot.org/core/author"Mima J."xsd:string
http://purl.uniprot.org/citations/17317927http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17317927http://purl.uniprot.org/core/name"Biosci Biotechnol Biochem"xsd:string
http://purl.uniprot.org/citations/17317927http://purl.uniprot.org/core/pages"472-480"xsd:string
http://purl.uniprot.org/citations/17317927http://purl.uniprot.org/core/title"Biochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC."xsd:string
http://purl.uniprot.org/citations/17317927http://purl.uniprot.org/core/volume"71"xsd:string
http://purl.uniprot.org/citations/17317927http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17317927
http://purl.uniprot.org/citations/17317927http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17317927
http://purl.uniprot.org/uniprot/P14306#attribution-7714E1990ED3F863ABD7F6DAA40B6E6Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/17317927
http://purl.uniprot.org/uniprot/Q06252#attribution-7714E1990ED3F863ABD7F6DAA40B6E6Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/17317927
http://purl.uniprot.org/uniprot/#_Q06252-mappedCitation-17317927http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17317927
http://purl.uniprot.org/uniprot/#_P14306-mappedCitation-17317927http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17317927
http://purl.uniprot.org/uniprot/P14306http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17317927
http://purl.uniprot.org/uniprot/Q06252http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17317927