| Primary Identifier | IPR033174 | Type | Family |
| Short Name | Caspase-14 |
| description | Caspase-14 (MEROPS identifier C14.018) is a cytoplasmic cysteine endopeptidase found only in cornifying tissues such as skin. It is found in epidermal keratinocytes and is involved in a tissue-specific form of senescence, leading to differentiation of keratinocytes to form the cornified cell layer [, ]. Caspase-14 is synthesized as a zymogen, but, unusually for a caspase, activation is not autocatalytic, and cleavage to produce the p20 and p10 subunits occurs in human caspase-14 at Ile152 []. Caspase-14 has a strict requirement for Asp in the P1 position, and positional scanning of substrates shows a preference for hydrophobic residues such as Trp or Tyr in P4 []. |
