Pycard
entrez
66824
canonical
uniprot
Q9EPB4
canonical
ensembl
ENSMUSG00000030793
resolver
ensp
ENSMUSP00000033056
resolver
enst
ENSMUST00000033056
resolver
genesymbol
Pycard
resolver
genesymbol_syn
Asc
resolver
uniprot
Q54AA2
resolver
uniprot
Q9D2W9
resolver
uniprot_entry
ASC_MOUSE
resolver
uniprot_entry
Q54AA2_MOUSE
resolver
uniprot_sec
Q9D2W9
resolver
amino_acid_sequence
MGRARDAILDALENLSGDELKKFKMKLLTVQLREGYGRIPRGALLQMDAIDLTDKLVSYYLESYGLELTMTVLRDMGLQELAEQLQTTKEESGAVAAAASVPAQSTARTGHFVDQHRQALIARVTEVDGVLDALHGSVLTEGQYQAVRAETTSQDKMRKLFSFVPSWNLTCKDSLLQALKEIHPYLVMDLEQS
uniprot
proteins
function
FUNCTION: Functions as a key mediator in apoptosis and inflammation (PubMed:32424362, PubMed:34678144). Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner (By similarity). Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3 (By similarity). Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP2, NLRP3, NLRP6 and AIM2) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines (PubMed:15190255, PubMed:15507117, PubMed:21892172, PubMed:22555457, PubMed:32424362, PubMed:34678144). Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death (By similarity). The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions (By similarity). Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization (By similarity). In the NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1 (By similarity). In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation (By similarity). May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation (By similarity). In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8 (PubMed:22555457). In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form (By similarity). Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways (By similarity). For regulation of NF-kappa-B activating and inhibiting functions have been reported (By similarity). Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK (By similarity). Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing (By similarity). Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA (PubMed:28314590). {ECO:0000250|UniProtKB:Q9ULZ3, ECO:0000269|PubMed:15190255, ECO:0000269|PubMed:15507117, ECO:0000269|PubMed:21892172, ECO:0000269|PubMed:22555457, ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:32424362, ECO:0000269|PubMed:34678144}.
uniprot
proteins
mass_dalton
21459
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9ULZ3}.; PTM: 'Lys-63'-linked polyubiquitination by TRAF3 is critical for speck formation and inflammasome activation (By similarity). 'Lys-63'-linked deubiquitinated by USP50; a crucial step for NLRP3-mediated inflammasome activation (By similarity). 'Lys-63'-linked polyubiquitination by PELI1 is also critical for speck formation and inflammasome activation (By similarity). Deubiquitinated by USP3 that cleaves 'Lys-48'-linked ubiquitin chains and strengthens its stability by blocking proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:Q9ULZ3}.
uniprot
proteins
pubmed
11139337
uniprot
proteins
pubmed
15190255
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15507117
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21892172
uniprot
proteins
pubmed
22555457
uniprot
proteins
pubmed
28314590
uniprot
proteins
pubmed
30487600
uniprot
proteins
pubmed
32424362
uniprot
proteins
pubmed
34471287
uniprot
proteins
pubmed
34678144
uniprot
proteins
sequence_length
193
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11139337, ECO:0000269|PubMed:21892172, ECO:0000269|PubMed:22555457}. Inflammasome {ECO:0000269|PubMed:32424362, ECO:0000269|PubMed:34678144}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9ULZ3}. Mitochondrion {ECO:0000250|UniProtKB:Q9ULZ3}. Nucleus {ECO:0000250|UniProtKB:Q9ULZ3}. Note=Upstream of caspase activation, a redistribution from the cytoplasm to the aggregates occurs. These appear as hollow, perinuclear spherical, ball-like structures. Upon NLRP3 inflammasome activation redistributes to the perinuclear space localizing to endoplasmic reticulum and mitochondria. Localized primarily to the nucleus in resting monocytes/macrophages and rapidly redistributed to the cytoplasm upon pathogen infection (By similarity). Localized to large cytoplasmic aggregate appearing as a speck containing AIM2, PYCARD, CASP8 and bacterial DNA after infection with Francisella tularensis (PubMed:22555457). {ECO:0000250|UniProtKB:Q9ULZ3, ECO:0000269|PubMed:22555457}.
uniprot
proteins