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http://purl.uniprot.org/citations/10684806http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10684806http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10684806http://www.w3.org/2000/01/rdf-schema#comment"It has been suggested that proteins of molecular size 56-58 kDa play an important role in bovine ovarian follicular development and oocyte maturation. A polyclonal antibody was raised against a 56-to 58-kDa protein band purified from bovine granulosa cells and was used to screen granulosa or luteal cell cDNA expression libraries. This work resulted in the identification of a cDNA encoding for a protein of 60.1 kDa with a signal peptide of 13 residues. The bovine 60.1-kDa protein shared an overall 86.7% and 81.8% identity with, respectively, the human 80K-H protein and the mouse putative beta subunit of glucosidase II (beta-GII), and was named vacuolar system-associated protein-60 (VASAP-60). Marked differences in sequence identity were noted in a putative molecular adapter domain containing a tandem D and E amino acid stretch flanked by proline-rich sequences presenting the minimal PXXP SH3 motif. VASAP-60 was shown to be unglycosylated using endoglycosidase H treatment and was found mainly in a cellular membrane fraction of bovine corpus luteum. VASAP-60 was localized in a rat hepatic Golgi/endosome fraction and in wheat germ agglutinin (WGA) affinity chromatographic eluates, thereby suggesting the presence of interactions with membrane glycoproteins. A polyclonal antibody was raised against the putative adapter domain of the recombinant VASAP-60; this was shown to recognize a major 88-kDa and two minor 58-kDa and 50-kDa proteins, suggesting that the major 88-kDa protein band represents the complete VASAP-60 protein whereas the 58-kDa and the 50-kDa bands represent its proteolytic fragments. Northern blot analysis demonstrated the presence of a single 2.3-kilobase transcript in all the bovine tissues analyzed with variation in the steady state level between tissues. Immunohistochemical observations showed that VASAP-60 was widely distributed in bovine tissues and was localized in pericytoplasmic and perinuclear membranes. In epithelial cells, the staining presented a basolateral or apical polarity associated with intracellular vacuoles. In conclusion, we have characterized a novel acidic membrane protein, associated with organelles of the vacuolar system, that is widely and histospecifically expressed in bovine tissues. VASAP-60 represents either the bovine ortholog or a new family member of the previously characterized human 80K-H and murine beta-GII proteins. Our results suggest that VASAP-60 presents characteristics of a molecular adaptor protein with functions in membrane-trafficking events."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.org/dc/terms/identifier"doi:10.1095/biolreprod62.3.642"xsd:string
http://purl.uniprot.org/citations/10684806http://purl.org/dc/terms/identifier"doi:10.1095/biolreprod62.3.642"xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Lussier J.G."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Lussier J.G."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Silversides D.W."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Silversides D.W."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Brule S."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Brule S."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Beckers J.-F.M.P."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Beckers J.-F.M.P."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Faure R."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Faure R."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Rabahi F."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/author"Rabahi F."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/name"Biol. Reprod."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/name"Biol. Reprod."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/pages"642-654"xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/pages"642-654"xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/title"Vacuolar system-associated protein-60: a protein characterized from bovine granulosa and luteal cells that is associated with intracellular vesicles and related to human 80K-H and murine beta-glucosidase II."xsd:string
http://purl.uniprot.org/citations/10684806http://purl.uniprot.org/core/title"Vacuolar system-associated protein-60: a protein characterized from bovine granulosa and luteal cells that is associated with intracellular vesicles and related to human 80K-H and murine beta-glucosidase II."xsd:string
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