The molecular cloning of the complementary deoxyribonucleic acid for bovine vitamin D-dependent calcium-binding protein

Structure of the full-length protein and evidence for homologies with other calcium-binding proteins of the troponin-C superfamily of proteins

Rajiv Kumar, Eric D Wieben, S. J. Beecher

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

We have cloned the cDNA for bovine intestinal vitamin D-dependent calcium-binding protein and, based on the sequence of the DNA, have deduced the structure of the full-length protein. The sequence of the cDNA clone predicts a protein comprised of 78 amino acids with a mol wt of 8788. The mRNA for the protein in bovine duodenum is about 500-600 bases in length. The protein sequence of bovine intestinal calcium-binding protein is 87% homologous with the sequence of porcine intestinal vitamin D-dependent calcium-binding protein and 81% homologous with the sequence of rat intestinal vitamin D-dependent calcium-binding protein. Hydrophilicity plots of the proteins noted above show that despite differences in amino acid sequence the proteins have similar patterns. In addition, the predicted secondary structure of the proteins is similar. Bovine intestinal calcium-binding protein shows 48.6% homology with the α-chain and 38.2% homology with the β-chain of bovine S-100 protein and a similar high degree of homology with the β-chain of human S-100 protein. The protein also demonstrates 36-43% homology with parvalbumin α and β from various species and with troponin-C. There is some homology with the 28K vitamin D-dependent calcium-binding proteins. Vitamin D-dependent bovine intestinal calcium-binding protein is closely related to other mammalian intestinal calcium-binding proteins and to the S-100 proteins, parvalbumins, and troponin-C.

Original languageEnglish (US)
Pages (from-to)427-432
Number of pages6
JournalMolecular Endocrinology
Volume3
Issue number2
StatePublished - 1989

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S100 Calcium Binding Protein G
Troponin C
Calcium-Binding Proteins
Molecular Cloning
Protein C
DNA
S100 Proteins
Proteins
Parvalbumins
Sequence Homology
Complementary DNA
Secondary Protein Structure
Protein S
Hydrophobic and Hydrophilic Interactions
Duodenum
Vitamin D
Amino Acid Sequence
Swine
Clone Cells
Amino Acids

ASJC Scopus subject areas

  • Molecular Biology
  • Endocrinology, Diabetes and Metabolism

Cite this

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title = "The molecular cloning of the complementary deoxyribonucleic acid for bovine vitamin D-dependent calcium-binding protein: Structure of the full-length protein and evidence for homologies with other calcium-binding proteins of the troponin-C superfamily of proteins",
abstract = "We have cloned the cDNA for bovine intestinal vitamin D-dependent calcium-binding protein and, based on the sequence of the DNA, have deduced the structure of the full-length protein. The sequence of the cDNA clone predicts a protein comprised of 78 amino acids with a mol wt of 8788. The mRNA for the protein in bovine duodenum is about 500-600 bases in length. The protein sequence of bovine intestinal calcium-binding protein is 87{\%} homologous with the sequence of porcine intestinal vitamin D-dependent calcium-binding protein and 81{\%} homologous with the sequence of rat intestinal vitamin D-dependent calcium-binding protein. Hydrophilicity plots of the proteins noted above show that despite differences in amino acid sequence the proteins have similar patterns. In addition, the predicted secondary structure of the proteins is similar. Bovine intestinal calcium-binding protein shows 48.6{\%} homology with the α-chain and 38.2{\%} homology with the β-chain of bovine S-100 protein and a similar high degree of homology with the β-chain of human S-100 protein. The protein also demonstrates 36-43{\%} homology with parvalbumin α and β from various species and with troponin-C. There is some homology with the 28K vitamin D-dependent calcium-binding proteins. Vitamin D-dependent bovine intestinal calcium-binding protein is closely related to other mammalian intestinal calcium-binding proteins and to the S-100 proteins, parvalbumins, and troponin-C.",
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AB - We have cloned the cDNA for bovine intestinal vitamin D-dependent calcium-binding protein and, based on the sequence of the DNA, have deduced the structure of the full-length protein. The sequence of the cDNA clone predicts a protein comprised of 78 amino acids with a mol wt of 8788. The mRNA for the protein in bovine duodenum is about 500-600 bases in length. The protein sequence of bovine intestinal calcium-binding protein is 87% homologous with the sequence of porcine intestinal vitamin D-dependent calcium-binding protein and 81% homologous with the sequence of rat intestinal vitamin D-dependent calcium-binding protein. Hydrophilicity plots of the proteins noted above show that despite differences in amino acid sequence the proteins have similar patterns. In addition, the predicted secondary structure of the proteins is similar. Bovine intestinal calcium-binding protein shows 48.6% homology with the α-chain and 38.2% homology with the β-chain of bovine S-100 protein and a similar high degree of homology with the β-chain of human S-100 protein. The protein also demonstrates 36-43% homology with parvalbumin α and β from various species and with troponin-C. There is some homology with the 28K vitamin D-dependent calcium-binding proteins. Vitamin D-dependent bovine intestinal calcium-binding protein is closely related to other mammalian intestinal calcium-binding proteins and to the S-100 proteins, parvalbumins, and troponin-C.

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