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http://purl.uniprot.org/citations/8198557http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8198557http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8198557http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/8198557http://www.w3.org/2000/01/rdf-schema#comment"In brain and many other tissues, type I inositol 1,4,5-trisphosphate (InsP3) 5-phosphatase is the major isoenzyme hydrolysing the calcium-mobilizing second messenger InsP3. This protein has been purified to apparent homogeneity from a crude soluble fraction of bovine brain, yielding a single major protein band with a molecular mass of 43 kDa after SDS/PAGE. This material was used to determine internal microsequences. A partial DNA sequence has been amplified by PCR by using degenerate primers deduced from two protein sequences (FKAKKYKKV and DENYKSQE). A cDNA clone (BVCT) was isolated by screening a dog thyroid cDNA library. The encoded protein of 412 amino acids has a calculated molecular mass of 47,681 Da. Peptide sequences generated from the bovine brain enzyme were found to be 96% conserved compared with the dog thyroid protein. When clone BVCT was expressed in Escherichia coli, the recombinant protein was shown to hydrolyse both InsP3 and inositol 1,3,4,5-tetrakisphosphate, with apparent Km values of 28 and 3 microM respectively. Enzyme activity was inhibited by EDTA and 2,3-bisphosphoglycerate, both inhibitors of native InsP3 5-phosphatase, but not by EGTA and LiCl, as previously shown for the bovine brain enzyme. Our data show the cloning of type I InsP3 5-phosphatase which, interestingly, does not share any significant sequence identity with the previously cloned type III isoenzyme."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.org/dc/terms/identifier"doi:10.1042/bj3000085"xsd:string
http://purl.uniprot.org/citations/8198557http://purl.org/dc/terms/identifier"doi:10.1042/bj3000085"xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"Moreau C."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"Moreau C."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"Erneux C."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"Erneux C."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"Lecocq R."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"Lecocq R."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"Vanweyenberg V."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"Vanweyenberg V."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"Verjans B."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"Verjans B."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"de Smedt F."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/author"de Smedt F."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/pages"85-90"xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/pages"85-90"xsd:string
http://purl.uniprot.org/citations/8198557http://purl.uniprot.org/core/title"Cloning and expression in Escherichia coli of a dog thyroid cDNA encoding a novel inositol 1,4,5-trisphosphate 5-phosphatase."xsd:string