Dp. Cerretti et al., Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that show testis-specific gene expression, BIOC BIOP R, 263(3), 1999, pp. 810-815
Citations number
35
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Metalloproteinase-disintegrins (ADAMs) are type 1 transmembrane proteins th
at contain a unique domain structure including a zinc-binding metalloprotei
nase domain, We have isolated cDNAs encoding two novel members of this fami
ly, ADAM29 and ADAM30 which show testis-specific expression. Three forms of
ADAM29 were found that encode proteins of 820, 786 and 767 amino acids. Al
l 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 aci
ds, with the difference in the coding region occurring in the cytoplasmic d
omain. ADAM29 and ADAM30 map to human chromosome 4q34 and 1p11-13, respecti
vely. 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. (C) 1999 Ac
ademic Press.