Pathways & interactions
Caspase-like domain superfamily (IPR029030)
Short name: Caspase-like_dom_sf
- Peptidase C14, p20 domain (IPR001309)
- Gingipain (IPR001769)
- Uncharacterised conserved protein, caspase-like (IPR011189)
- Peptidase C14A, caspase catalytic domain (IPR015917)
- Caspase-8 (IPR033170)
- Caspase-14 (IPR033174)
- Mucosa-associated lymphoid tissue lymphoma translocation protein 1 (IPR033540)
- Caspase-6 (IPR037554)
This superfamily represents the caspase-like domain found in caspases, metacaspases and peptidases of the C25 family (gingipains).
Caspases (Cysteine-dependent ASPartyl-specific proteASE) are cysteine peptidases [PMID: 11517925]. 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) [PMID: 10578171, PMID: 10872455, PMID: 15077141]. 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) (EC:220.127.116.11), 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 [PMID: 15066636].
Metacaspases are arginine/lysine-specific, in contrast to caspases, which are aspartate-specific. They are found only in plants [PMID: 17998208, PMID: 23522353], fungi [PMID: 18355456] and lower eukaryotes, including the protozoa [PMID: 23506317]. While plant metacaspases have been shown to be involved in cell death pathways, in other organisms they have evolved alternative functions [PMID: 21949125].
Lys-gingipains are cysteine proteinases with a strong preference for substrates with Lys in the P1 position [PMID: 15576324].
- SSF52129 (SSF52129)