CARDCaspase recruitment domain
|SMART accession number:||SM00114|
|Description:||Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.|
|Interpro abstract (IPR001315):|
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 IPR000488) and the death effector domain (DED, see IPR001875), which work in similar pathways and show similar interaction properties [(PUBMED:11504623)]. 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 (IPR007111) (in Nal1 and Bir1), NB-ARC (IPR002182) (in Apaf-1), pyrin/dapin domains (IPR004020) (in Nal1), leucine-rich repeats (in Nal1), WD repeats (IPR001680) (in Apaf1), Src homology domains (IPR001452), PDZ (IPR001478), RING, kinase and DD domains [(PUBMED:15226512)].
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 [(PUBMED:9175472)]. CARD-containing proteins are also involved in inflammation through their regulation of NF-kappaB [(PUBMED:12101092)]. 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.
|GO process:||regulation of apoptotic process (GO:0042981)|
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