Xie Z, Xu W, Davie E W, Chung D W
Department of Biochemistry, University of Washington, Seattle, Washington, 98195, USA.
Biochem Biophys Res Commun. 1998 Oct 29;251(3):914-9. doi: 10.1006/bbrc.1998.9506.
Based on two partial cDNA sequences, a full-length cDNA sequence for an actin-binding like protein previously named ABPL has been isolated and characterized. ABPL is homologous to the human actin-binding proteins ABP-280 and ABP-278. The predicted sequence for ABPL is 2,705 amino acids in length with a calculated molecular mass of 289 kDa. It contains an amino terminal actin-binding domain followed by 24 tandem repeats of approximately 96 amino acids. Two hinge regions, Hinge I and Hinge II, were located prior to repeats 16 and 24, respectively. An isoform of ABPL lacking Hinge I, with a calculated molecular mass of 286 kDa, was also identified by the reverse transcriptase PCR (RT-PCR) method. A comparison with genomic sequences indicated the isoform resulted from alternative RNA splicing. ABPL has a unique insertion sequence of 82 amino acids in repeat 20 that was not present in the other two homologues and has a tissue distribution that was also different from the other two homologues.
基于两个部分cDNA序列，一个先前命名为ABPL的肌动蛋白结合样蛋白的全长cDNA序列已被分离和鉴定。ABPL与人肌动蛋白结合蛋白ABP - 280和ABP - 278同源。ABPL的预测序列长度为2705个氨基酸，计算分子量为289 kDa。它包含一个氨基末端肌动蛋白结合结构域，随后是24个约96个氨基酸的串联重复序列。两个铰链区，铰链I和铰链II，分别位于重复序列16和24之前。通过逆转录聚合酶链反应（RT-PCR）方法也鉴定出一种缺少铰链I的ABPL同工型，其计算分子量为286 kDa。与基因组序列的比较表明，该同工型是由选择性RNA剪接产生的。ABPL在重复序列20中有一个独特的82个氨基酸的插入序列，这在其他两个同源物中不存在，并且其组织分布也与其他两个同源物不同。
