Primary structure of the brain alpha-spectrin.

摘要: We have determined the nucleotide sequence coding for chicken brain alpha-spectrin. It is derived both from cDNA and genomic sequences, comprises entire frame, 5' 3' untranslated terminates in poly(A)-tail. The deduced amino acid was used to map domain structure of protein. alpha-chain spectrin contains 22 segments which 20 correspond repeat human erythrocyte (Speicher, D. W., V. T. Marchesi. 1984. Nature (Lond.). 311:177-180.), typically made 106 residues. These homologous probably account flexible, rod-like spectrin. Secondary prediction suggests predominantly alpha-helical chain. Parts primary are excluded repetitive pattern they reside middle part its COOH terminus. Search homology other proteins showed presence following distinct structures these nonrepetitive regions: (a) COOH-terminal molecule that shows with alpha-actinin, (b) two typical EF-hand (i.e., Ca2+-binding) this region, (c) a close fulfills criteria calmodulin-binding site, (d) NH2-terminal segment several src-tyrosine kinases phospholipase C. regions good candidates carry some established as well yet unestablished functions Comparative analysis alpha-spectrin conserved across species boundaries Xenopus man, divergent spectrins.