We report the cloning and sequencing of cDNA encoding a chicken filamin protein. The 2,567 amino acid protein contains an NH2-terminal 267 amino acid actin-binding domain followed by a series of 24 repeating units that are each approximately 95 amino acids in length. The overall primary structure of filamin closely resembles that of human actin-binding protein (ABP). However, filamin lacks a 24-amino-acid insertion prior to repeat 16 that is contained within ABP. This region of human ABP is a site of calpain cleavage and is thought to confer flexibility on the molecule. Hence, it is possible that the properties of actin gels formed with either human ABP or filamin reflect the presence or absence of this insertion. Filamin is encoded within a multi-promoter transcription unit. A downstream filamin promoter (Fill) resembles those of certain housekeeping genes and has a putative binding site for the transcription factor E2F. Thus, transcription from this promoter may be linked to the cell cycle. A second filamin promoter (Fi12) is located at least 8 kilobases upstream from the Fill promoter. This structural arrangement suggests that regulation of filamin gene expression is likely to be complex.
|Original language||English (US)|
|Number of pages||10|
|Journal||Journal of Biological Chemistry|
|State||Published - 1993|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology