CARD domain
IPR001315
Definition
The caspase recruitment domain (CARD domain) is a homotypic protein interaction module composed of a bundle of six α-helices. CARD is related in sequence and structure to the death domain (DD, see [interpro:IPR000488]) and the death effector domain (DED, see [interpro:IPR001875]), which work in similar pathways and show similar interaction properties PMID: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 ([interpro:IPR007111]) (in Nal1 and Bir1), NB-ARC ([interpro:IPR002182]) (in Apaf-1), pyrin/dapin domains ([interpro:IPR004020]) (in Nal1), leucine-rich repeats ([interpro:IPR001611]) (in Nal1), WD repeats ([interpro:IPR001680]) (in Apaf1), Src homology domains ([interpro:IPR001452]), PDZ ([interpro:IPR001478]), RING, kinase and DD domains PMID: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 [[cite:PMID:9175472], [cite:PMID:22065589]]. CARD-containing proteins are also involved in inflammation through their regulation of NF-kappaB PMID: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.
28 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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