Abstract
A full-length cDNA of 595 bp was isolated froma human fetal brain cDNA library. It contains an openreading frame encoding 153 amino acids, with an 18-bp5′UTR and a 118-bp 3′UTR in which there isan atypicalpolyadenylation signal (ATTAAA). The calculatedmolecular weight of the deduced protein is 17.3 kU. Thepredicted isoelectric point is 4.89. On account of itshigh homology to mouse neuronal protein NP15.6(81.2% identity), the deduced protein was namedneuronal protein 17.3 (NP17.3). When its secondarystructure was examined by the GGBSM program of PCGENEsoftware, it was found that 32.6 and 15.0% of itsamino acids are involved in formingalpha-helices and beta-sheets, respectively. Examinedwith the PESTFIND program, a typical PEST region foundin rapidly degraded proteins was found between residue48and residue 68.
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Cui, Y., Yu, L., Gong, R. et al. Cloning and Tissue Expressional Characterization of a Full-Length cDNA Encoding Human Neuronal Protein P17.3. Biochem Genet 37, 175–185 (1999). https://doi.org/10.1023/A:1018734605214
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DOI: https://doi.org/10.1023/A:1018734605214