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Complete amino acid sequence of Bombyx egg‐specific protein deduced from cDNA clone
Author(s) -
Inagaki Shyuichiro,
Yamashita Okitsugu
Publication year - 1989
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940100204
Subject(s) - biology , peptide sequence , amino acid , complementary dna , biochemistry , nucleic acid sequence , consensus sequence , signal peptide , protein sequencing , bombyx mori , microbiology and biotechnology , serine , sequence motif , homology (biology) , dna , gene , phosphorylation
Complementary (c)DNA coding for an insect yolk protein, the egg‐specific protein of the silkworm Bombyx mori was cloned and the nucleotide sequence determined. The sequence covers the entire coding region of 1,677 base pairs with 5′ and 3′ noncoding regions (21 and 115 base pairs, respectively). The deduced amino acid sequence of the egg‐specific protein consists of 559 amino acid residues. The NH 2 ‐terminal 18 amino acid sequence is enriched in hydrophobic amino acids and assumed to be a signal peptide. A sequence, Asn‐X‐Thr, a potential N‐linked glycosylation site, is found at positions 191 to 193. A serine‐rich domain is localized in the region from 63 to 90, in which phosphorylation takes place. Cys His motif in 405 to 415 is analogous to a proposed metal binding sequence. Lys 132 ‐Asn 133 and Arg 228 ‐Asp 229 are probably the sites cleaved by the egg‐specific protein protease that appears during embryogenesis. The derived amino acid sequence has no appreciable homology to other sequenced proteins.