title: From the spectrin gene to the assembly of the membrane skeleton.
abstract: The complete nucleotide sequence coding for the chicken brain alpha-spectrin was determined. It comprises the entire coding frame, 5'- and 3'-untranslated sequences terminating in a poly(A)-tail. The deduced amino acid sequence shows that the alpha-chain contains 22 segments, 20 of which correspond to the typical 106 residue repeat of the human erythrocyte spectrin. Some segments non-homologous to the repeat structure reside in the middle and COOH-terminal regions. Sequence comparisons with other proteins show that these segments evidently harbour some structural and functional features such as: homology to alpha-actinin and dystrophin, two typical EF-hand structures (calcium-binding) and a putative calmodulin-binding site in the COOH-terminus and a sequence homologous to various src-tyrosine kinases and to phospholipase C in the middle of the molecule. Comparison of our sequence with other partial alpha-spectrin sequences shows that alpha-spectrin is well conserved in different species and that the human erythrocyte alpha-spectrin is divergent.
authors.affiliation: Department of Medical Chemistry, University of Helsinki, Finland.
authors.forename: V M
authors.initials: VM
authors.lastname: Wasenius
authors.forename: M
authors.initials: M
authors.lastname: Saraste
authors.forename: V P
authors.initials: VP
authors.lastname: Lehto
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D001921:Brain / Q000378:metabolism*; D002462:Cell Membrane / Q000502:physiology; D002645:Chickens; D003599:Cytoskeleton / Q000502:physiology*; D004247:DNA / Q000032:analysis; D004912:Erythrocytes / Q000378:metabolism; D006801:Humans; D008957:Models, Genetic; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013049:Spectrin / Q000235:genetics*; D013329:Structure-Activity Relationship
chemical_list: D013049:Spectrin; D004247:DNA