绵羊ACSL1基因编码蛋白结构及生物信息学分析

Analysis of Bioinformatics of ACSL1 Gene Encoding Protein in Sheep

为探究绵羊长链脂酰辅酶A合成酶1基因(ACSL1)编码蛋白的结构与功能,通过生物信息学分析对绵羊ACSL1蛋白的二、三级结构预测,分析其信号肽剪切位点、理化性质、亲/疏水性、亚细胞定位和蛋白互作网络通路。结果表明,ACSL1基因共编码699个氨基酸,理论分子量78.21 k D,理论等电点8.0,具有1个跨膜结构域,编码蛋白的不稳定系数33.23,主要分布在细胞质(26.1%)、线粒体(13%)和内质网(13%),无信号肽,是一种疏水性稳定蛋白。其蛋白结构主要以α螺旋和无规则卷曲为主,其中共有276个α螺旋(39.48%),148个β折叠(21.17%),217个无规则卷曲(31.04%),折叠缠绕后形成三级结构。绵羊ACSL1蛋白主要与FADS1、FADS2、ACOX1、ACOX2、LPL、MGLL、ELOVL6、ACADL等9个蛋白相关,可能处在同一信号通路,通过与疏水性蛋白结合后,在机体内调节其生物学功能。

The purpose of this study was to predict the structure and function of ACSL1 encoding protein in sheep,predicted ACSL1 protein secondary and tertiary structure,and analyzed the signal peptide splice site,physicochemical properties,hydrophilicity,subcellular localization and interactions between proteins network using lot of bioinformatics techniques software.The results showed that ACSL1 gene encoded 699 amino acid,the molecular weight of ACSL1 was 78.21 kDa,the theoretical pI was 8.0,and the instability index of ACSL1 protein was 33.23.It was a hydrophobic protein without signal peptide and was a stable protein with a transmembrane domain.The probability of distribution in cytoplasmic was 26.1%,and endoplasmic reticulum and mitochondrial were all 13%.The secondary structure of ACSL1 protein was mainly formed from alpha-helix and random coil,which had 276 alpha-helix(39.48%),148 extended strand(21.17%),217 random coil(31.04%),and the tertiary structure was formed after its folding and winding.ACSL1 protein was mainly related to 9 proteins including FADS1,FADS2,ACOX1,ACOX2,LPL,MGLL,ELOVL6,and ACADL,and might be in the same signaling pathway.After binding to hydrophobic proteins,it regulated their biological functions in the sheep body.