Molecular Cloning of Human ABPL, an Actin-Binding Protein Homologue

• Published in: Biochemical and biophysical research communications Vol. 251; no. 3; pp. 914 - 919
• Main Authors: Xie, Zhi-wei, Xu, Wen-feng, Davie, Earl W., Chung, Dominic W.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 29.10.1998
• Subjects: Actins - metabolism; Alternative Splicing; Amino Acid Sequence; Cloning, Molecular; Contractile Proteins - genetics; DNA, Complementary - genetics; Filamins; Humans; Microfilament Proteins - genetics; Molecular Sequence Data; Protein Binding; Protein Isoforms - genetics; Sequence Homology, Amino Acid
• ISSN: 0006-291X; 1090-2104
• 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.