Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that show testis-specific gene expression

Biochem Biophys Res Commun. 1999 Oct 5;263(3):810-5. doi: 10.1006/bbrc.1999.1322.

Abstract

Metalloproteinase-disintegrins (ADAMs) are type 1 transmembrane proteins that contain a unique domain structure including a zinc-binding metalloproteinase domain. We have isolated cDNAs encoding two novel members of this family, ADAM29 and ADAM30 which show testis-specific expression. Three forms of ADAM29 were found that encode proteins of 820, 786 and 767 amino acids. All of the amino acid differences are located in the cytoplasmic domain. Two forms of ADAM30 were isolated that encode proteins of 790 and 781 amino acids, with the difference in the coding region occurring in the cytoplasmic domain. ADAM29 and ADAM30 map to human chromosome 4q34 and 1p11-13, respectively. An ancestral analysis of all known mammalian ADAMs indicates that the zinc-binding motif in the catalytic domain arose once in a common ancestor and was subsequently lost by those members lacking this motif.

MeSH terms

  • ADAM Proteins
  • Amino Acid Sequence
  • Animals
  • Cell Membrane / metabolism
  • Chromosome Mapping*
  • Chromosomes, Human
  • Cloning, Molecular
  • Cytoplasm / metabolism
  • DNA, Complementary*
  • Disintegrins / chemistry
  • Disintegrins / metabolism*
  • Evolution, Molecular
  • Female
  • Gene Library
  • Humans
  • Male
  • Mammals
  • Membrane Proteins / genetics
  • Membrane Proteins / isolation & purification
  • Metalloendopeptidases / chemistry
  • Metalloendopeptidases / genetics*
  • Metalloendopeptidases / isolation & purification
  • Mice
  • Molecular Sequence Data
  • Organ Specificity
  • Phylogeny
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Testis / metabolism*

Substances

  • DNA, Complementary
  • Disintegrins
  • Membrane Proteins
  • Recombinant Proteins
  • ADAM Proteins
  • ADAM29 protein, human
  • ADAM30 protein, human
  • Metalloendopeptidases