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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1988-3-11
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2415530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2422556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2936963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2942542,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2948495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2948959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2948960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2952539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2953951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2981869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-2988123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-3013422,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-3013423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-3020049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-3156212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-3702991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-3818645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-6105043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-6231954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-6233137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-6236813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-6310323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-6326095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-6376118,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2963335-7108955
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
664-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2963335-Amino Acid Sequence,
pubmed-meshheading:2963335-Annexins,
pubmed-meshheading:2963335-Base Sequence,
pubmed-meshheading:2963335-Calcium-Binding Proteins,
pubmed-meshheading:2963335-DNA,
pubmed-meshheading:2963335-Glycoproteins,
pubmed-meshheading:2963335-Humans,
pubmed-meshheading:2963335-Molecular Sequence Data,
pubmed-meshheading:2963335-Multigene Family,
pubmed-meshheading:2963335-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:2963335-Sequence Homology, Nucleic Acid
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pubmed:year |
1988
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pubmed:articleTitle |
Human 67-kDa calelectrin contains a duplication of four repeats found in 35-kDa lipocortins.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Molecular Genetics, University of Texas Health Science Center, Dallas 75235.
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pubmed:publicationType |
Journal Article,
Comparative Study
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