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Author Kovacic, R. T. ♦ Tizard, R. ♦ Cate, R. L. ♦ Frey, A. Z. ♦ Wallner, B. P.
Source United States Department of Energy Office of Scientific and Technical Information
Content type Text
Language English
Subject Keyword BASIC BIOLOGICAL SCIENCES ♦ ENZYME INHIBITORS ♦ AMINO ACID SEQUENCE ♦ GENES ♦ DNA SEQUENCING ♦ LIPASES ♦ MAN ♦ MEMBRANE PROTEINS ♦ PHOSPHOLIPIDS ♦ PHOSPHORUS 32 ♦ PROTEIN STRUCTURE ♦ RATS ♦ ANIMALS ♦ BETA DECAY RADIOISOTOPES ♦ BETA-MINUS DECAY RADIOISOTOPES ♦ CARBOXYLESTERASES ♦ DAYS LIVING RADIOISOTOPES ♦ ENZYMES ♦ ESTERASES ♦ ESTERS ♦ HYDROLASES ♦ ISOTOPES ♦ LIGHT NUCLEI ♦ LIPIDS ♦ MAMMALS ♦ MOLECULAR STRUCTURE ♦ NUCLEI ♦ ODD-ODD NUCLEI ♦ ORGANIC COMPOUNDS ♦ ORGANIC PHOSPHORUS COMPOUNDS ♦ PHOSPHORUS ISOTOPES ♦ PRIMATES ♦ PROTEINS ♦ RADIOISOTOPES ♦ RODENTS ♦ STRUCTURAL CHEMICAL ANALYSIS ♦ VERTEBRATES ♦ Biochemistry
Abstract Lipocortins (annexins) are a family of calcium-dependent phospholipid-binding proteins with phospholipase A{sub 2} inhibitory activity. The characteristic primary structure of members of this family consists of a core structure of four or eight repeated domains, which have been implicated in calcium-dependent phospholipid binding. In two lipocortins (1 and 2) a short amino-terminal sequence distinct from the core structure has potential regulatory functions which are dependent on its phosphorylation state. The authors isolated the rat and human lipocortin 1 genes and found that they both consist of 13 exons with a striking conservation of their exon-intron structure and their promoter and amino acid sequences. Both lipocortin I genes are at least 19 kbp in length with exons ranging from 57 to 123 bp interrupted by introns as large as 5 kbp. Each of the four repeat units of lipocortin 1 are encoded by two consecutive exons while individual exons code for the highly conserved putative calcium-binding domains. The promoter sequences in the rat and in human genes are highly conserved and contain nucleotide sequences characterized as enhancer sequences in other genes. The structure of the lipocortin 1 gene lends support to the hypothesis that the lipocortin genes arose by a duplication of a single domain.
ISSN 00062960
Educational Use Research
Learning Resource Type Article
Publisher Date 1991-09-17
Publisher Place United States
Journal Biochemistry
Volume Number 30
Issue Number 37


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