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作 者:耿荣庆[1,2] 陈玉林[1] 王兰萍[2] 杨朝霞[1] 姜维[1] 刘敏[1] 曹春娜[1]
机构地区:[1]西北农林科技大学动物科技学院,陕西杨凌712100 [2]盐城师范学院生命科学与技术学院,江苏盐城224051
出 处:《华北农学报》2012年第1期1-4,共4页Acta Agriculturae Boreali-Sinica
基 金:国家自然科学基金(31101684)
摘 要:对绒山羊和绵羊KAP1.4基因的编码区进行克隆与分析,在此基础上预测了KAP1.4蛋白的分子结构,为研究毛(绒)用性状的分子基础提供资料。结果表明,克隆测序获得绒山羊、绵羊KAP1.4基因编码区序列长度为579bp和549 bp,分别编码192个氨基酸和182个氨基酸。生物信息学分析表明,绒山羊和绵羊KAP1.4蛋白的基本理化特性方面无明显差异,属于非跨膜蛋白,信号肽的长度和裂解点相同,都具有1个蛋白激酶C磷酸化位点、3个酪蛋白激酶Ⅱ磷酸化位点和6个N端酰基化位点;蛋白的二级结构由β折叠、β转角和无规则卷曲构成。三级结构预测显示,绒山羊与绵羊KAP1.4蛋白在空间三维结构上存在显著差异,将会进一步影响其功能的发挥并成为调控产毛(绒)性状的影响因子。The objectives of this study were to clone and analysis the coding region of KAPI. 4 gene and to pre- dict KAPI. 4 protein structure in order to provide basic molecular data for the study of wool and cashmere traits. The result showed that the coding region of KAP1.4 gene in cashmere goat and sheep was 579,549 bp long and espec- tively encoded 192 amino acids, 182 amino acids. Bioinformatic analysis showed that there was no significant differ- ence in the basic physical and chemical characteristics of KAP1. 4 protein of cashmere goat and sheep. They was a non-transmembrane protein and possessed the same length and the signal peptide cleavage point, having a protein kinase C phosphorylation site,three casein kinase Ⅱ phosphorylation sites and six N-terminal acylation sites. The protein secondary structure was constructed by β-sheet, β turn and random coil. Tertiary structure prediction showed that there were significant differences of three-dimensional structure in space between cashmere goat and sheep KAP1. 4 protein. It would further affect the function and become an impact factor on the regulation of wool or cash- mere traits.
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