Rudimentary phosvitin domain in a minor chicken vitellogenin gene

• Published in: Biochemistry (Easton) 1989-03, Vol.28 (6), p.2572-2577
• Main Authors: Byrne, B M, de Jong, H, Fouchier, R A, Williams, D L, Gruber, M, Ab, G
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Blotting, Northern; Blotting, Southern; Chickens; Cloning, Molecular; Codon - genetics; Egg Proteins - genetics; Exons; Genes; Liver - metabolism; Molecular Sequence Data; Phosvitin - genetics; Restriction Mapping; Vitellogenins - genetics
• ISSN: 0006-2960
• DOI: 10.1021/bi00432a034

We have determined the nucleotide sequence and the derived amino acid sequence of the phosphoprotein-encoding region of the chicken vitellogenin III gene. The sequence of this minor vitellogenin could be aligned with exon 22 up to exon 27 of the previously sequenced major vitellogenin II gene (van het Schip et al., 1987). The exon 23 and 25 sequences are rich in serine codons (26% and 41%, respectively), and this region encodes at least one of the small egg yolk phosphoproteins. The major egg yolk phosphoprotein, phosvitin, is encoded by the analogous region in vitellogenin II. Comparison of the vitellogenin II and vitellogenin III sequences shows a great reduction in the size of the putative exon 23 of the latter (321 base pairs as opposed to 690). The number of serine codons is also drastically reduced from 124 in exon 23 of the vitellogenin II gene to 28 in vitellogenin III. The grouping of synonymous serine codons, as has hitherto been observed in sequenced vitellogenin phosphoproteins, has been maintained in vitellogenin III. A putative asparagine-linked N-glycosylation site which was conserved in the chicken vitellogenin II and the Xenopus laevis vitellogenin A2 gene, at the beginning of exon 23, is also present in vitellogenin III. The two chicken vitellogenins show a low conservation in the phosphoprotein-encoding region (average 33%, at the protein level) compared to that in the peripheral sequences (58% identity), which indicates that it is a rapidly evolving domain of the vertebrate vitellogenin gene.