| Primary Identifier | IPR033153 | Type | Family |
| Short Name | SPE-4 |
| description | SPE-4 peptidase (MEROPS identifier A22.012) is an intramembrane, aspartic endopeptidase characterized from Caenorhabditis elegans. Swapping the active site domain of presenilin 1 with SPE-4 resulted in a protein that could process the beta-amyloid protein precursor but not Notch, and the difference in substrate recognition was shown by site-directed mutagenesis to depend on the nature of a residue in the GxGD motif that includes the active site aspartic acid []. SPE-4 is essential for the activation of sperm cells, and in a naturally occurring mutant known as hc196, spermatocytes are defective, and spermatids are activated prematurely []. |
