意大利蜜蜂Akt1的蛋白序列特征和结构域分析  

Bioinformatics analysis of serine/threonine protein kinases Akt1 in Apis mellifera ligustica

作　　者：李桂林 冯颖 张新怡 张呈豪 夏文丽 王姝威 赵航 LI Guilin;FENG Ying;ZHANG Xinyi;ZHANG Chenghao;XIA Wenli;WANG Shuwei;ZHAO Hang(School of Life Sciences,Qufu Normal University,273165,Qufu,Shandong,PRC)

机构地区：[1]曲阜师范大学生命科学学院,山东省曲阜市273165

出　　处：《曲阜师范大学学报(自然科学版)》2025年第2期93-98,共6页Journal of Qufu Normal University(Natural Science)

基　　金：国家自然科学基金(32202739);曲阜师范大学科研启动基金.

摘　　要：丝氨酸/苏氨酸蛋白激酶已被证明是反转录病毒癌基因v-akt的编码产物,所以又被称为Akt.Akt有3个亚型,分别是Akt1、Akt2和Akt3.研究表明,Akt1与精神分裂症、生物的生长发育等有关.该文利用生物信息学软件分析意大利蜜蜂Akt1蛋白的序列和结构特征.结果表明,意大利蜜蜂Akt1是一种存在于细胞质中并由544个氨基酸残基组成的带负电的稳定的亲水蛋白.Akt1有4个结构域,不具有跨膜结构域.另外,Akt1一共具有60个可能的磷酸化修饰位点,33个潜在的O-连接的糖基化修饰位点和1个N-连接的糖基化修饰位点.该研究可为进一步研究意大利蜜蜂Akt1的功能提供理论依据.Serine/threonine protein kinases have been shown to encode the retroviral oncogene v-akt,so they are also known as Akt.There are three subtypes of Akt,including Akt1,Akt2 and Akt3.Akt1 is related to schizophrenia,biological growth and development.The purpose of this study was to analyze the sequence and structural characteristics of Akt1 in Apis mellifera ligustica by using bioinformatics softwares.The results showed that Apis mellifera ligustica Akt1 was a negatively charged and stable hydrophilic protein that was composed of 544 amino acid residues in the cytoplasm.Akt1 has 4 domains and does not possess transmembrane domains.Besides,Akt1 has a total of 60 possible phosphorylation sites,33 potential O-glycosylation sites and 1 N-glycosylation site.This study can provide theoretical basis for further study on the structure and function of Apis melliana ligustica Akt1.

关 键 词：生物信息学 意大利蜜蜂 结构特征 AKT1 

分 类 号：Q966[生物学—昆虫学]