##gff-version 3
P29452	UniProtKB	Propeptide	1	118	.	.	.	ID=PRO_0000004525;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29452	UniProtKB	Chain	119	296	.	.	.	ID=PRO_0000004526;Note=Caspase-1 subunit p20;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:32109412;Dbxref=PMID:32109412	
P29452	UniProtKB	Propeptide	297	314	.	.	.	ID=PRO_0000004527;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29452	UniProtKB	Chain	315	402	.	.	.	ID=PRO_0000004528;Note=Caspase-1 subunit p10;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:32109412;Dbxref=PMID:32109412	
P29452	UniProtKB	Domain	1	91	.	.	.	Note=CARD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00046	
P29452	UniProtKB	Region	98	125	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P29452	UniProtKB	Compositional bias	108	122	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P29452	UniProtKB	Active site	236	236	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29466	
P29452	UniProtKB	Active site	284	284	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21147462;Dbxref=PMID:21147462	
P29452	UniProtKB	Site	103	104	.	.	.	Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21147462;Dbxref=PMID:21147462	
P29452	UniProtKB	Site	122	123	.	.	.	Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21147462;Dbxref=PMID:21147462	
P29452	UniProtKB	Modified residue	301	301	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P29452	UniProtKB	Modified residue	343	343	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
P29452	UniProtKB	Mutagenesis	102	122	.	.	.	Note=Prevents autoprocessing. EDSKGGHPSSSETKEEQNKED->AASKGGHPSSSATKAAQNKAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32109412;Dbxref=PMID:32109412	
P29452	UniProtKB	Mutagenesis	103	103	.	.	.	Note=In C71 mutant%3B abolished cleavage and ability to generate caspase-1 subunits%3B abolished ability to process inflammatory cytokine interleukin-1 beta (IL1B) and ability to induce programmed cell death%3B when associated with N-122 and 296-N--N-314. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21147462;Dbxref=PMID:21147462	
P29452	UniProtKB	Mutagenesis	122	122	.	.	.	Note=In C71 mutant%3B abolished cleavage and ability to generate caspase-1 subunits%3B abolished ability to process inflammatory cytokine interleukin-1 beta (IL1B) and ability to induce programmed cell death%3B when associated with N-103 and 296-N--N-314. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21147462;Dbxref=PMID:21147462	
P29452	UniProtKB	Mutagenesis	284	284	.	.	.	Note=Loss of protease activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21147462;Dbxref=PMID:21147462	
P29452	UniProtKB	Mutagenesis	296	314	.	.	.	Note=In C71 mutant%3B abolished cleavage and ability to generate caspase-1 subunits%3B abolished ability to process inflammatory cytokine interleukin-1 beta (IL1B) and ability to induce programmed cell death%3B when associated with N-103 and N-122. DSVRDSEEDFLTDAIFEDD->NSVRDSEEDFLTNAIFENN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21147462;Dbxref=PMID:21147462	
P29452	UniProtKB	Mutagenesis	296	314	.	.	.	Note=In C60 mutant%3B impaired cleavage and ability to generate caspase-1 subunits p10 and p20%3B abolished ability to process inflammatory cytokine interleukin-1 beta (IL1B) without affecting ability to induce programmed cell death. DSVRDSEEDFLTDAIFEDD->NSVRNSEENFLTNAIFENN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21147462;Dbxref=PMID:21147462	
P29452	UniProtKB	Mutagenesis	296	296	.	.	.	Note=In C47 mutant%3B does not affect ability to mediate inflammatory response%3B when associated with 313-N-N-314. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21147462;Dbxref=PMID:21147462	
P29452	UniProtKB	Mutagenesis	313	314	.	.	.	Note=In C47 mutant%3B does not affect ability to mediate inflammatory response and cell death%3B when associated with N-296. DD->NN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21147462;Dbxref=PMID:21147462	
P29452	UniProtKB	Mutagenesis	316	316	.	.	.	Note=Mediates autoprocessing but are unable to mediate cleavage of Gasdermin-D (GSDMD). I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32109412;Dbxref=PMID:32109412	
P29452	UniProtKB	Sequence conflict	3	6	.	.	.	Note=DKIL->V;Ontology_term=ECO:0000305;evidence=ECO:0000305