The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin
Overlapping human erythroid alpha-spectrin cDNA clones were isolated from lambda gt11 libraries constructed from cDNAs of human fetal liver and erythroid bone marrow. The composite 8001-base pair (bp) cDNA nucleotide sequence contains 187-bp 5'- and 528-bp 3'-untranslated regions and has a...
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Published in | The Journal of biological chemistry Vol. 265; no. 8; pp. 4434 - 4443 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Biochemistry and Molecular Biology
15.03.1990
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Subjects | |
Online Access | Get full text |
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Summary: | Overlapping human erythroid alpha-spectrin cDNA clones were isolated from lambda gt11 libraries constructed from cDNAs of
human fetal liver and erythroid bone marrow. The composite 8001-base pair (bp) cDNA nucleotide sequence contains 187-bp 5'-
and 528-bp 3'-untranslated regions and has a single long open reading frame of 7287 bp that encodes a polypeptide of 2429
residues. As previously described (Speicher, D. W., and Marchesi, V. T. (1984) Nature 311, 177-180), spectrin is composed
largely of homologous 106-amino acid repeat units. From the amino acid sequence deduced from the cDNA, alpha-spectrin can
be divided into 22 segments. Segments 1-9 and 12-19 are homologous and can therefore be considered repeats; the average number
of identical residues in pairwise comparisons of these repeats is 22 out of 106, or 21%. Of these 17 repeats, 11 are exactly
106 amino acids in length, whereas five others differ from this length by a single residue. Segments 11, 20, and 21, although
less homologous, appear to be related to the more highly conserved repeat units. The very N-terminal 22 residues, segment
10, which is atypical both in length and sequence, and the C-terminal 150 residues in segment 22 appear to be unrelated to
the conserved repeat units. The sequence of the erythroid alpha-spectrin polypeptide chain is compared to that of human alpha-fodrin
and chicken alpha-actinin to which it is related. alpha-Spectrin is more distantly related to dystrophin. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)39583-3 |