Q2LKV5
uniprot
Q2LKV5
canonical
activity_regulation
ACTIVITY REGULATION: In contrast to allele 1, does not undergo autocatalytic cleavage within the FIIND domain and its mode of activation remains unclear (PubMed:32558991). In contrast to alleles 1 and 2, allele 3 is not activated by Val-boroPro (Talabostat, PT-100) (PubMed:31383852). Not activated by cleavage by B.anthracis lethal toxin (LT) endopeptidase (PubMed:16429160, PubMed:23230290, PubMed:31383852). Not activated by metabolic inhibitors, such as 2-deoxy-D-glucose and sodium azide (PubMed:23230290). {ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:23230290, ECO:0000269|PubMed:31383852, ECO:0000303|PubMed:32558991}.
uniprot
proteins
amino_acid_sequence
MEESPPKQKSNTKVAQHEGQQDLNTTRHMNVELKHRPKLERHLKLGMIPVVYMKQREEILYPAQSLKEENLIQNFTSLPLLQKLYPKDPENMVRKSWASCIPEEGGHMINIQDLFGPNIGTQKEPQLVIIEGAAGIGKSTLARLVKRAWKEGQLYRDHFQHVFFFSCRELAQCKKLSLAELIAQGQEVPTAPINQILSHPEKLLFILDGIDEPAWVLADQNPELCLHWSQRQPVHTLLGSLLGKSILPEAFFLLTTRTTALQKFIPSLPMPCQVEVLGFSGIERENYFYKYFANQRHAITAFMMVESNPVLLTLCEVPWVCWLVCTCLKKQMEQGRVLSLKSQTTTALCLKYPSLTIPDKHRRTQVKALCSLAAEGIWKRRTLFSESDLCKQGLDEDAVATFLKTGVLQKQASSLSYSFAHLCLQEFFAAISCILEDSEERHGNMEMDRIVETLVERYGRQNLFEAPTVRFLFGLLGKEGVKGMEKLFSCSLHGKTKLKLLWHILGKSQPHQPSCLGLLHCLYENQDMELLTHVMHDLQGTIVPGPNDIAHTVLQTNVKQLVVQTDMELMVATFCIQFYCHVRTLQLNMEKQQGYALTSPRMVLYRWTPITNASWEILFYNLKFTRNLEGLDLSGNSLRYSVVQSLCNTLRYPGCQLKTLWLVKCGLTSRYCSLLASVLSAHSSLTELYLQLNDLGDDGVRMLCEGLRNPVCNLSILWLDLSSLSAQVITELRTLEEKNPKLYIRSIWMPHMMVPTENMDEEAILTTFKQQRQESGDKPMEILGTEEDFWGPTGPVATELVDRVRNLYRVQLPMAGSYHCPSTGLHFVVTRAVTIEIEFCAWSQFLDKTPLQQSHMVVGPLFDIKAEQGAVTAVYLPHFVSLKDTEASTFDFKVAHFQEHGIVLETPDRVKPGYTVLKNPSFSPMGDVLRIIPADRHFIPITSITLIYYRLNLEEVTLHLYLVPSDCTIQKAIDDEEMKFQFVRINKPPPVDNLFIGSRYIVSGSENLEITPKELELCYRSSKEFQLFSEIYVGNMGSEIKLQIKNKKHMRLIWEALLKPGDLRPALPRIAQALKDAPSLLHFMDQHREQLVARVTSVDPLLDKLHGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVMDLLEKSGGVSLGS
uniprot
proteins
function
FUNCTION: May act as the sensor component of the Nlrp1b inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). May act as a recognition receptor (PRR), which recognizes specific pathogens and other damage-associated signals and forms an inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1b inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). Contrary to Nlrp1b allele 1, allele 3 is not activated by Bacillus anthracis lethal toxin (PubMed:16429160, PubMed:19651869, PubMed:23230290). The absence of autocatalytic cleavage within the FIIND domain, which regulates activation in other alleles, suggests that allele 3 may be non-functional (PubMed:31383852). {ECO:0000250|UniProtKB:Q2LKW6, ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:19651869, ECO:0000269|PubMed:23230290, ECO:0000269|PubMed:31383852}.
uniprot
proteins
mass_dalton
133631
uniprot
proteins
mutagenesis
MUTAGEN 927; /note="D->V: Restores autocatalytic cleavage, as observed in allele 1, but not response to anthrax lethal toxin (LT), nor to metabolic inhibitors. Restores autocatalytic cleavage and IL1B release in response to LT; when associated with A-935 and N-965."; /evidence="ECO:0000269|PubMed:22536155, ECO:0000269|PubMed:23230290"; MUTAGEN 935; /note="D->A: No effect; when associated with N-965. Restores autocatalytic cleavage and IL1B release in response to anthrax lethal toxin; when associated with V-927 and N-965."; /evidence="ECO:0000269|PubMed:22536155"; MUTAGEN 965; /note="S->N: Restores autocatalytic cleavage, as observed in allele 1, and produces constitutive IL1B release; when associated with V-927 and A-935."; /evidence="ECO:0000269|PubMed:22536155
uniprot
proteins
post_translational_modification
PTM: In contrast to allele 1 and 2, not able to mediate autocatalytic cleavage. {ECO:0000269|PubMed:22536155, ECO:0000269|PubMed:31383852}.
uniprot
proteins
protein_family
NLRP family
uniprot
proteins
pubmed
16429160
uniprot
proteins
pubmed
19651869
uniprot
proteins
pubmed
22536155
uniprot
proteins
pubmed
23230290
uniprot
proteins
pubmed
23506131
uniprot
proteins
pubmed
31383852
uniprot
proteins
pubmed
32558991
uniprot
proteins
sequence_length
1172
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q2LKW6}.
uniprot
proteins