Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain.
Gelsolin is representative of a class of actin-modulating proteins found in lower eukaryotes to mammals, which sever actin filaments. Gelsolin found in the cytoplasm of cells is functionally similar to a mammalian plasma protein of similar size, originally called ADF or brevin. Human plasma and rabbit macrophage gelsolins differ by the presence of a 25-amino-acid residue extension on plasma gelsolin which appears to account for the difference in relative molecular mass (Mr) between the proteins as assessed by SDS-polyacrylamide gel electrophoresis (PAGE), 93,000 (93K) and 90K, respectively. Here we report the isolation of full-length human plasma gelsolin complementary DNA clones from a HepG2 library. The inferred amino-acid sequence reveals the presence of a signal peptide, a long tandem repeat that matches the actin-binding domains of gelsolin, a tetrapeptide present in actin and extended regions of identical sequence with rabbit macrophage gelsolin. Southern blot analysis indicates that a single gene in the haploid genome encodes both protein forms.
D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins / Q000097:blood / Q000235:genetics*; D003593:Cytoplasm / Q000378:metabolism; D004247:DNA; D018260:Gelsolin; D005796:Genes; D006801:Humans; D008840:Microfilament Proteins / Q000097:blood / Q000235:genetics*; D012091:Repetitive Sequences, Nucleic Acid; D012689:Sequence Homology, Nucleic Acid
D002135:Calcium-Binding Proteins; D018260:Gelsolin; D008840:Microfilament Proteins; D004247:DNA