| Type: | Domain | Name: | CARD domain |
| Description: | The caspase recruitment domain (CARD domain) is a homotypic protein interaction module composed of a bundle of six alpha-helices. CARD is related in sequence and structure to the death domain (DD, see ) and the death effector domain (DED, see ), which work in similar pathways and show similar interaction properties []. The CARD domain typically associates with other CARD-containing proteins, forming either dimers or trimers. CARD domains can be found in isolation, or in combination with other domains. Domains associated with CARD include: NACHT () (in Nal1 and Bir1), NB-ARC () (in Apaf-1), pyrin/dapin domains () (in Nal1), leucine-rich repeats () (in Nal1), WD repeats () (in Apaf1), Src homology domains (), PDZ (), RING, kinase and DD domains [].CARD-containing proteins are involved in apoptosis through their regulation of caspases that contain CARDs in their N-terminal pro-domains, including human caspases 1, 2, 9, 11 and 12 []. CARD-containing proteins are also involved in inflammation through their regulation of NF-kappaB []. The mechanisms by which CARDs activate caspases and NF-kappaB involve the assembly of multi-protein complexes, which can facilitate dimerisation or serve as scaffolds on which proteases and kinases are assembled and activated. | Short Name: | CARD |
