The E3-11.6K protein of adenovirus is an Asn-glycosylated integral membrane protein that localizes to the nuclear membrane.
The E3-11.6K protein of adenovirus is an Asn-glycosylated integral membrane protein that localizes to the nuclear membrane.
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DOI：
10.1016/0042-6822(92)90250-s
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发表时间：
1992-12
期刊：
影响因子：
3.7
通讯作者：
A. Scaria;A. Tollefson;S. K. Saha;W. Wold
中科院分区：
文献类型：
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作者：
A. Scaria;A. Tollefson;S. K. Saha;W. Wold
腺病毒2（Ad 2）的11，600 MW（101个氨基酸; 11.6K）蛋白是一种功能未知的蛋白质，在感染的早期阶段合成量很低，但在晚期阶段合成量非常高。11.6K蛋白迁移为三个主要的弥散带组。14 K、21 K和31 K的蛋白质，表明11.6K经历了翻译后修饰。我们在这里表明，11.6K是Asn-糖基化与复杂的（endo H-抗性）寡糖和11.6K是一个完整的膜蛋白。免疫荧光显示，11.6K最初与内质网和高尔基体相关，最终定位于核膜。预测11.6K蛋白在残基41-62处具有单个信号锚定序列，并且在残基14处仅具有一个潜在的Asn连接的糖基化位点;因此，11.6K必须在膜中定向，其NH 2-末端在管腔中，其COOH-末端在细胞质中。11.6 K的信号锚和糖基化特征在Ad 2和Ad 5（C组）以及Ad 3和Ad 7（B组）中被保留，但是11.6 K的序列在这些血清型中比大多数其他腺病毒蛋白质的序列更加多样化。
The 11,600 MW (101 amino acids; 11.6K) protein of adenovirus 2 (Ad2) is a protein of unknown function which is synthesized in low amounts during early stages of infection but in very high amounts at late stages. The 11.6K protein migrates as three major groupings of diffuse bands of ca. 14K, 21 K, and 31 K on SDS-PAGE, indicating that 11.6K undergoes post-translational modification. We show here that 11.6K is Asn-glycosylated with complex (endo H-resistant) oligosaccharides and that 11.6K is an integral membrane protein. Immunofluorescence indicated that 11.6K initially is associated with the endoplasmic reticulum and Golgi apparatus and that it ultimately localizes to the nuclear membrane. The 11.6K protein is predicted to have a single signal-anchor sequence at residues 41–62 and only one potential Asn-linked glycosylation site at residue 14; thus, 11.6K must be oriented in the membranes with its NH2-terminus in the lumen and its COOH-terminus in the cytoplasm. The signal-anchor and glycosylation features of 11.6K are preserved in Ad2 and Ad5 (group C), and in Ad3 and Ad7 (group B), but the sequence of 11.6K is more diverged among these serotypes than is the sequence of most other adenovirus proteins.