CARD domain

CARDcaspase recruitment domainCARD motifcaspase activation and recruitment domaincaspase active recruitment domainscaspase recruitment domain (CARD)caspase-recruitment domain (CARD)
Caspase recruitment domains, or Caspase activation and recruitment domains (CARDs), are interaction motifs found in a wide array of proteins, typically those involved in processes relating to inflammation and apoptosis.wikipedia
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Death effector domain

DED
Other motifs in this class include the pyrin domain (PYD), death domain (DD), and death effector domain (DED), all of which also function primarily in regulation of apoptosis and inflammatory responses.
DED is a subfamily of the DD superfamily (other recogniazable domains in this superfamily are: caspase-recruitment domain (CARD), pyrin domain (PYD) and death domain (DD)).

Death fold

CARD domains are a subclass of protein motif known as the death fold, which features an arrangement of six to seven antiparallel alpha helices with a hydrophobic core and an outer face composed of charged residues.
Examples of death fold domains include the death domain (DD), death effector domain (DED), Caspase Recruitment Domain (CARD), and pyrin domain (PYD).

Death domain

DAPdeath domainsdeath-domain
Other motifs in this class include the pyrin domain (PYD), death domain (DD), and death effector domain (DED), all of which also function primarily in regulation of apoptosis and inflammatory responses.
DD is a subclass of protein motif known as the death fold and is related in sequence and structure to the death effector domain (DED) and the caspase recruitment domain (CARD), which work in similar pathways and show similar interaction properties.

Caspase

caspasesprocaspasescaspase cascade
CARD motifs are present on a number of proteins that promote apoptosis, primarily caspases 1,2,4,5,9, and 15 in mammals.
The pro-domain of the intrinsic initiator caspases and the inflammatory caspases contains a single death fold known as caspase recruitment domain (CARD), while the pro-domain of the extrinsic initiator caspases contains two death folds known as death effector domains (DED).

RIG-I

DDX58retinoic acid-inducible gene Iretinoic acid-inducible gene-1 (RIG-1)
Unlike NLRs, these proteins, termed RIG-I and MDA5, contain twin N-terminal CARD domains and C-terminal RNA helicase domains that directly interact with and process the double-stranded viral RNA.
RIG-I contains a RNA helicase-DEAD box motifs and a caspase recruitment domain (CARD).

NALP3

NLRP3CIAS1cryopyrin
Activating mutations in at least two related PYD-containing proteins, cryopyrin/CIAS-1 and pyrin/MEFV, have been linked to Muckle-Wells Syndrome and familial Mediterranean fever, respectively.
Proteins which contain the caspase recruitment domain, CARD, have been shown to be involved in inflammation and immune response.

Caspase-9

caspase 9CASP99
The N-terminal pro-domain is also called the long pro-domain and this contains the caspase activation domain (CARD) motif.

Short linear motif

motifinteraction motifsisland
Caspase recruitment domains, or Caspase activation and recruitment domains (CARDs), are interaction motifs found in a wide array of proteins, typically those involved in processes relating to inflammation and apoptosis.

Protein

proteinsproteinaceousstructural proteins
Caspase recruitment domains, or Caspase activation and recruitment domains (CARDs), are interaction motifs found in a wide array of proteins, typically those involved in processes relating to inflammation and apoptosis.

Inflammation

inflammatoryinflammatory responseinflamed
Caspase recruitment domains, or Caspase activation and recruitment domains (CARDs), are interaction motifs found in a wide array of proteins, typically those involved in processes relating to inflammation and apoptosis.

Apoptosis

apoptoticprogrammed cell deathcell death
Caspase recruitment domains, or Caspase activation and recruitment domains (CARDs), are interaction motifs found in a wide array of proteins, typically those involved in processes relating to inflammation and apoptosis.

Pyrin domain

PYDpyrinpyrin domain (PYD)
Other motifs in this class include the pyrin domain (PYD), death domain (DD), and death effector domain (DED), all of which also function primarily in regulation of apoptosis and inflammatory responses.

Toll-like receptor

Toll-like receptorsTLRToll
Ipaf-1 features an N-terminal CARD domain, a nucleotide-binding domain, and C-terminal leucine-rich repeats (LRRs), thought to function in a similar fashion to those found in Toll-like receptors.

RNA

ribonucleic aciddsRNAdouble-stranded RNA
Recently, a subset of CARD proteins has been shown to participate in recognition of intracellular double-stranded RNA, a common constituent of a number of viral genomes, including the para- and orthomyxoviridae and rhabdoviridae.

MDA5

IFIH1MDA-5Melanoma differentiation-associated antigen 5 (MDA5)
Unlike NLRs, these proteins, termed RIG-I and MDA5, contain twin N-terminal CARD domains and C-terminal RNA helicase domains that directly interact with and process the double-stranded viral RNA.

Helicase

DNA helicaseRNA helicasehelicases
Unlike NLRs, these proteins, termed RIG-I and MDA5, contain twin N-terminal CARD domains and C-terminal RNA helicase domains that directly interact with and process the double-stranded viral RNA.

Mitochondrial antiviral-signaling protein

MAVSVISAIPS-1
This processing makes the CARD domains available for interaction with the CARD motif of IPS-1/MAVS/VISA/Cardif, a downstream adapter anchored in the mitochondria.

CHUK

IKKAconserved helix-loop-helix ubiquitous kinaseIKBKA
Although the canonical IKK family members IKKa and IKKb are essential for virus-triggered NF-κB activation, the noncanonical IKK family members TBK1 and IKBKE are responsible for phosphorylating and activating IRF3 and IRF7 (Fitzgerald et al., 2003; Hemmi et al., 2004; Matsui et al., 2006).

IKK2

IKBKBIKK-βIKKB
Although the canonical IKK family members IKKa and IKKb are essential for virus-triggered NF-κB activation, the noncanonical IKK family members TBK1 and IKBKE are responsible for phosphorylating and activating IRF3 and IRF7 (Fitzgerald et al., 2003; Hemmi et al., 2004; Matsui et al., 2006).

NF-κB

NF-kBNF-kappaBNFκB
Although the canonical IKK family members IKKa and IKKb are essential for virus-triggered NF-κB activation, the noncanonical IKK family members TBK1 and IKBKE are responsible for phosphorylating and activating IRF3 and IRF7 (Fitzgerald et al., 2003; Hemmi et al., 2004; Matsui et al., 2006).

TANK-binding kinase 1

TBK1
Although the canonical IKK family members IKKa and IKKb are essential for virus-triggered NF-κB activation, the noncanonical IKK family members TBK1 and IKBKE are responsible for phosphorylating and activating IRF3 and IRF7 (Fitzgerald et al., 2003; Hemmi et al., 2004; Matsui et al., 2006).

IKBKE

IKK-εIKKε
Although the canonical IKK family members IKKa and IKKb are essential for virus-triggered NF-κB activation, the noncanonical IKK family members TBK1 and IKBKE are responsible for phosphorylating and activating IRF3 and IRF7 (Fitzgerald et al., 2003; Hemmi et al., 2004; Matsui et al., 2006).

Crohn's disease

Crohn’s diseaseCrohn diseaseCrohn
Gain-of-function mutations in the intracellular NOD2 protein has been linked to increased risk for Crohn's disease.

Muckle–Wells syndrome

Muckle-Wells SyndromeUrticaria-deafness-amyloidosis
Activating mutations in at least two related PYD-containing proteins, cryopyrin/CIAS-1 and pyrin/MEFV, have been linked to Muckle-Wells Syndrome and familial Mediterranean fever, respectively.

Familial Mediterranean fever

polyserositisMediterranean fever, familialPeriodic disease
Activating mutations in at least two related PYD-containing proteins, cryopyrin/CIAS-1 and pyrin/MEFV, have been linked to Muckle-Wells Syndrome and familial Mediterranean fever, respectively.