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http://purl.uniprot.org/citations/9990022http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9990022http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9990022http://www.w3.org/2000/01/rdf-schema#comment"Using reverse transcriptase-PCR and degenerate oligonucleotides derived from the active-site residues of subtilisin/kexin-like serine proteinases, we have identified a highly conserved and phylogenetically ancestral human, rat, and mouse type I membrane-bound proteinase called subtilisin/kexin-isozyme-1 (SKI-1). Computer databank searches reveal that human SKI-1 was cloned previously but with no identified function. In situ hybridization demonstrates that SKI-1 mRNA is present in most tissues and cells. Cleavage specificity studies show that SKI-1 generates a 28-kDa product from the 32-kDa brain-derived neurotrophic factor precursor, cleaving at an RGLT downward arrowSL bond. In the endoplasmic reticulum of either LoVo or HK293 cells, proSKI-1 is processed into two membrane-bound forms of SKI-1 (120 and 106 kDa) differing by the nature of their N-glycosylation. Late along the secretory pathway some of the membrane-bound enzyme is shed into the medium as a 98-kDa form. Immunocytochemical analysis of stably transfected HK293 cells shows that SKI-1 is present in the Golgi apparatus and within small punctate structures reminiscent of endosomes. In vitro studies suggest that SKI-1 is a Ca2+-dependent serine proteinase exhibiting a wide pH optimum for cleavage of pro-brain-derived neurotrophic factor."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.org/dc/terms/identifier"doi:10.1073/pnas.96.4.1321"xsd:string
http://purl.uniprot.org/citations/9990022http://purl.org/dc/terms/identifier"doi:10.1073/pnas.96.4.1321"xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Barale J.-C."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Barale J.-C."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Zhong M."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Zhong M."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Benjannet S."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Benjannet S."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Chretien M."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Chretien M."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Hamelin J."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Hamelin J."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Lazure C."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Lazure C."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Seidah N.G."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Seidah N.G."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Basak A."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Basak A."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Mowla S.J."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Mowla S.J."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Murphy R.A."xsd:string
http://purl.uniprot.org/citations/9990022http://purl.uniprot.org/core/author"Murphy R.A."xsd:string