v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This entry represents the caspase activation and recruitment domain (CARD) found in a group of proteins, including ASC (apoptosis-associated speck-like protein containing a CARD), caspase recruitment domain-containing protein 8 (CARD8) and NALP1 (CARD7, NLRP1). CARD domain containing proteins are known to be important in the signalling pathways for apoptosis, inflammation and host-defense mechanisms [ ]. ASC is an adaptor molecule that mediates inflammatory and apoptotic signals. It has been found to recruit caspase-1 to several members of the nucleotide-binding domain and leucine-rich repeat (LRR)-containing proteins (NLRs), which functions as cytoplasmic sensors for invading bacteria and viruses in cells [ ]. The inflammasome is a cytosolic complex that functions to specifically recruit and activate a downstream protease called caspase-1 (CASP1). NLRP1 is a sensor component of the NLRP1 inflammasome, which plays a crucial role in innate immunity and inflammation. It has been linked to a number of human pathologies, such as vitiligo, rheumatoid arthritis, and Crohn disease [ ].CARD8 (also known as CARDINAL) regulates caspase-1 activation and apoptosis [ ] and participates in NFkappaB activation []. It is part of the inflammasome, which is responsible for the activation of caspases 1 and 5, leading to the processing and secretion of the pro-inflammatory cytokines IL-1beta and IL-18 []. |
| Short Name | CARD8/ASC/NALP1_CARD |