P43527
uniprot
P43527
canonical
amino_acid_sequence
MADKVLRAKRKQFINSVSVGTINGLLDELLEKRVLNQEEMDTIKLANITVMEKARDLCDHVTKKGPRASQMFITYICNEDCYLAEILELQSGPSAETVFVTEDSKGGHPFSSETKEKLNKEGGAFPGPSGSLKFCPLEIAQKLWKENHSEIYPIMKTPTRTRLALIICNTDFQHLSRRVGADVDLREMKLLLQDLGYTVKVKENLTALEMTKELKEFAACPEHKTSDSTFLVFMSHGLQEGICGITYSNEVADILKVDTIFQMMNTLKCPSLKDKPKVIIIQACRGEKQGVVLLKDSVGNSEEGFLTDAIFEDDGIKKAHIEKDFIAFCSSTPDNVSWRHPVRGSLFIESLIKHMKEYAWSCDLEDIFRKVRFSFEQPDSRLQMPTTERVTLTKRFYLFPGH
uniprot
proteins
ec_number
3.4.22.36
uniprot
proteins
function
FUNCTION: Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides. Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a pro-inflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes. Cleaves a tetrapeptide after an Asp residue at position P1. Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD. In contrast to cleavage of interleukin IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part. Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive. In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly. {ECO:0000250|UniProtKB:P29466}.
uniprot
proteins
mass_dalton
45576
uniprot
proteins
post_translational_modification
PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism. {ECO:0000250|UniProtKB:P29466}.; PTM: Ubiquitinated via 'Lys-11'-linked polyubiquitination. Deubiquitinated by USP8. {ECO:0000250|UniProtKB:P29466}.
uniprot
proteins
protein_family
Peptidase C14A family
uniprot
proteins
pubmed
7588240
uniprot
proteins
pubmed
7780029
uniprot
proteins
sequence_length
402
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29466}. Cell membrane {ECO:0000250|UniProtKB:P29466}.
uniprot
proteins