Abstract:
:A cDNA for parafusin, an evolutionarily conserved phosphoglycoprotein involved in exocytosis, has been cloned and sequenced from a unicellular eukaryote, Paramecium tetraurelia. A Paramecium cDNA library was screened with an oligonucleotide probe synthesized to an internal amino acid sequence of isolated parafusin. The insert was 3 kb long with an open reading frame of 1.75 kb. Data base searches of the deduced amino acid sequence showed that Paramecium parafusin had a 50.7% sequence identity to rabbit muscle phosphoglucomutase, although no detectable phosphoglucomutase activity has been detected in isolated parafusin. The deduced parafusin amino acid sequence had four inserts and two deletions, which might confer on the protein specific functions in signal transduction events related to exocytosis. Furthermore, searches for potential phosphorylation sites showed the presence of a protein kinase C site (KDFSFR) specific to parafusin. Southern blot analysis with probes specific for parafusin and phosphoglucomutase suggested that these proteins were products of different genes. We propose that parafusin and phosphoglucomutase are members of a superfamily that conserve homologies important for the tertiary structure of the molecules.
journal_name
Proc Natl Acad Sci U S Aauthors
Subramanian SV,Wyroba E,Andersen AP,Satir BHdoi
10.1073/pnas.91.21.9832subject
Has Abstractpub_date
1994-10-11 00:00:00pages
9832-6issue
21eissn
0027-8424issn
1091-6490journal_volume
91pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:2000-08-29 00:00:00
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:2013-06-11 00:00:00