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

T. C. Sudhof, C. A. Slaughter, I. leznicki, P. Barjon, G. A. Reynolds

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

The 67-kDa calelectrin is the largest member of a family of Ca2+-binding proteins that associate with membranes and phospholipids in a Ca2+-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 Ca2+-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.

Original languageEnglish (US)
Pages (from-to)664-668
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number3
DOIs
StatePublished - Jan 1 1988

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Annexin A6
Annexins
Proteins
Phospholipids
Annexin A2
Annexin A1
Oligonucleotide Probes
Gene Library
DNA Sequence Analysis
Retina
Carrier Proteins
Amino Acids
Peptides
Membranes
Genes

ASJC Scopus subject areas

  • General

Cite this

Human 67-kDa calelectrin contains a duplication of four repeats found in 35-kDa lipocortins. / Sudhof, T. C.; Slaughter, C. A.; leznicki, I.; Barjon, P.; Reynolds, G. A.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, No. 3, 01.01.1988, p. 664-668.

Research output: Contribution to journalArticle

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AU - Reynolds, G. A.

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AB - The 67-kDa calelectrin is the largest member of a family of Ca2+-binding proteins that associate with membranes and phospholipids in a Ca2+-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 Ca2+-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.

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