TY - JOUR
T1 - Cloning of Metalloprotease Genes in the Carpet Viper (Echis pyramidurm leakeyi): Further Members of the Metalloprotease/Disintegrin Gene Family: Further Members of the Metalloprotease/Disintegrin Gene Family
AU - Paine, Mark
AU - Moura‐Da‐Silva, Ana M.
AU - Theakston, R. David G.
AU - Crampton, Julian M.
PY - 1994/9/1
Y1 - 1994/9/1
N2 - The genes coding for two metalloproteases, EcH‐I and EcH‐II, have been cloned from an Echis pyramidum leakeyi venom gland cDNA library. The cDNA sequences predict two zymogen molecules with strong amino acid sequence similarity and the same domain structure present in other members of the viper metalloprotease/disintegrin gene family. EcH‐I and EcH‐II contain pro‐protein, enzyme and disintegrin domains. Analysis of the cDNAs coding for EcH‐I, EcH‐II, jararhagin, trigramin and Ht‐e reveals a strong similarity, particularly in the untranslated regions and regions coding for the pro‐peptide. Comparison of EcH‐I and EcH‐II with venom metalloproteases, mammalian matrix‐degrading metalloproteases, sperm proteins, and a potential tumour suppressor gene highlights the presence of a number of motifs with potential functional significance.
AB - The genes coding for two metalloproteases, EcH‐I and EcH‐II, have been cloned from an Echis pyramidum leakeyi venom gland cDNA library. The cDNA sequences predict two zymogen molecules with strong amino acid sequence similarity and the same domain structure present in other members of the viper metalloprotease/disintegrin gene family. EcH‐I and EcH‐II contain pro‐protein, enzyme and disintegrin domains. Analysis of the cDNAs coding for EcH‐I, EcH‐II, jararhagin, trigramin and Ht‐e reveals a strong similarity, particularly in the untranslated regions and regions coding for the pro‐peptide. Comparison of EcH‐I and EcH‐II with venom metalloproteases, mammalian matrix‐degrading metalloproteases, sperm proteins, and a potential tumour suppressor gene highlights the presence of a number of motifs with potential functional significance.
U2 - 10.1111/j.1432-1033.1994.00483.x
DO - 10.1111/j.1432-1033.1994.00483.x
M3 - Article
SN - 1742-464X
VL - 224
SP - 483
EP - 488
JO - FEBS Journal
JF - FEBS Journal
IS - 2
ER -