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Human 67-kDa calelectrin contains a duplication of four repeats found in 35-kDa lipocortins

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
The 67-kDa calelectrin is the largest number of a family of Ca/sup 2 +/-binding proteins that associate with membranes and phospholipids in a Ca/sup 2 +/-dependent manner. Oligonucleotide probes based on peptide sequences obtained from purified bovine 67-kDa calelectrin were used to screen a human retina cDNA library, and the complete primary structure of human 67-kDa calelectrin was deduced by DNA sequence analysis. The protein consists of eight 68-amino acid repeats separated by linking sequences of variable lengths. It is highly similar to the human lipocortin I and II sequences, each of which contains four such repeats. The amino termini of the three proteins show no sequence similarity; however, in the repeated regions the proteins are 42-45% identical in sequence. Analysis of the 16 repeats from the three proteins provides insights into the structural basis for Ca/sup 2 +/-dependent phospholipid binding. These data place the calelectrins and the lipocortins into the same gene family and suggest that these proteins have similar functions and have evolved from a common ancestor.
Research Organization:
Howard Hughes Medical Institute, Dallas, TX (USA)
OSTI ID:
6619112
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 85:3; ISSN PNASA
Country of Publication:
United States
Language:
English