InterPro : IPR011600

Name  Peptidase C14, caspase domain Short Name  Pept_C14_caspase
Type  Domain Description  This domain can be found in caspases (MEROPS family C12A) and metacaspases (MEROPS family C14B). Metacaspases adopt a caspase fold, with active site loops arranged similarly as other caspases [].Caspases (Cysteine-dependent ASPartyl-specific proteASE) are cysteine peptidases []. They are tightly regulated proteins that require zymogen activation to become active, and once active can be regulated by caspase inhibitors. Caspases are mainly involved in mediating cell death (apoptosis) [, , ]. They have two main roles within the apoptosis cascade: as initiators that trigger the cell death process, and as effectors of the process itself. Caspases can have roles other than in apoptosis, such as caspase-1 (interleukin-1 beta convertase) (), which is involved in the inflammatory process. The activation of apoptosis can sometimes lead to caspase-1 activation, providing a link between apoptosis and inflammation, such as during the targeting of infected cells. Caspases may also be involved in cell differentiation [].Metacaspases are arginine/lysine-specific, in contrast to caspases, which are aspartate-specific. They are found only in plants [, ], fungi []and lower eukaryotes, including the protozoa []. While plant metacaspases have been shown to be involved in cell death pathways, in other organisms they have evolved alternative functions [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



1 Child Features

Id Name Short Name Type
IPR015917 Peptidase C14A, caspase precursor p45, core Pept_C14A_p45_core Domain

3 Contains

Id Name Short Name Type
IPR002138 Peptidase C14, caspase non-catalytic subunit p10 Pept_C14_p10 Domain
IPR001309 Peptidase C14, ICE, catalytic subunit p20 Pept_C14_ICE_p20 Domain
IPR016129 Peptidase C14, ICE, catalytic subunit p20, active site Pept_C14_ICE_p20_AS Active_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR029030 Caspase-like domain Caspase-like_dom Domain

11 Publications

First Author Title Year Journal Volume Pages
Barrett AJ Evolutionary lines of cysteine peptidases. 2001 Biol Chem 382 727-33
Salvesen GS Caspase activation - stepping on the gas or releasing the brakes? Lessons from humans and flies. 2004 Oncogene 23 2774-84
Abraham MC Death without caspases, caspases without death. 2004 Trends Cell Biol 14 184-93
Nicholson DW Caspase structure, proteolytic substrates, and function during apoptotic cell death. 1999 Cell Death Differ 6 1028-42
Earnshaw WC Mammalian caspases: structure, activation, substrates, and functions during apoptosis. 1999 Annu Rev Biochem 68 383-424
Wong AH Crystal structure of the yeast metacaspase Yca1. 2012 J Biol Chem 287 29251-9
Kim SM A pepper (Capsicum annuum L.) metacaspase 9 (Camc9) plays a role in pathogen-induced cell death in plants. 2013 Mol Plant Pathol 14 557-66
He R Metacaspase-8 modulates programmed cell death induced by ultraviolet light and H2O2 in Arabidopsis. 2008 J Biol Chem 283 774-83
Mazzoni C Caspase-dependent apoptosis in yeast. 2008 Biochim Biophys Acta 1783 1320-7
Machado MF Substrate specificity and the effect of calcium on Trypanosoma brucei metacaspase 2. 2013 FEBS J 280 2608-21
Proto WR Trypanosoma brucei metacaspase 4 is a pseudopeptidase and a virulence factor. 2011 J Biol Chem 286 39914-25

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)