Peptidase C14, caspase domain
IPR011600
Definition
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 PMID:22761449. 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) [[cite:PMID:10578171], [cite:PMID:10872455], [cite: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:3.4.22.36]), 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 [[cite:PMID:17998208], [cite: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.
14 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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