Molecular cloning of human ABPL, an actin-binding protein homologue

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 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


  • Actins
  • Contractile Proteins
  • DNA, Complementary
  • FLNB protein, human
  • Filamins
  • Microfilament Proteins
  • Protein Isoforms