Isolation of a glycosylated form of the chicken eggshell protein ovocleidin and determination of the glycosylation site. Alternative glycosylation/phosphorylation at an N‐glycosylation sequon

FEBS Letters

Mann, Karlheinz¹ 

[1] Max-Planck-Institut für Biochemie, Am Klopferspitz 18, D-82152 Martinsried, Germany

关键词: Ovocleidin;    Eggshell;    Glycosylation;    Phosphorylation;   

DOI  :  10.1016/S0014-5793(99)01586-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Ovocleidin, a major protein of the avian eggshell calcified layer, occurs in the eggshell soluble organic matrix in at least two forms. The major form is a phosphoprotein with two phosphorylated serines (OC-17) which was sequenced recently. A minor form is a glycosylated protein with identical sequence and only one phosphorylated serine (OC-23). The site of glycosylation is Asn⁵⁹, the only asparagine in the amino acid sequence contained in the N-glycosylation site consensus sequence, N-A-S. Ser⁶¹, which is part of this site, is phosphorylated in OC-17 but not in OC-23 indicating that the two modifications are mutually exclusive. This is the first example of alternative glycosylation/phosphorylation occurring at an N-glycosylation site.

【 授权许可】

Unknown