##gff-version 3
Q9Z2D3	UniProtKB	Chain	1	512	.	.	.	ID=PRO_0000148179;Note=Gasdermin-E	
Q9Z2D3	UniProtKB	Chain	1	270	.	.	.	ID=PRO_0000442749;Note=Gasdermin-E%2C N-terminal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443	
Q9Z2D3	UniProtKB	Chain	271	499	.	.	.	ID=PRO_0000442750;Note=Gasdermin-E%2C C-terminal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443	
Q9Z2D3	UniProtKB	Region	1	56	.	.	.	Note=Membrane targeting domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443	
Q9Z2D3	UniProtKB	Site	270	271	.	.	.	Note=Cleavage%3B by CASP3 or granzyme B;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443	
Q9Z2D3	UniProtKB	Modified residue	45	45	.	.	.	Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443	
Q9Z2D3	UniProtKB	Modified residue	156	156	.	.	.	Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443	
Q9Z2D3	UniProtKB	Modified residue	168	168	.	.	.	Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443	
Q9Z2D3	UniProtKB	Modified residue	180	180	.	.	.	Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443	
Q9Z2D3	UniProtKB	Modified residue	235	235	.	.	.	Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443	
Q9Z2D3	UniProtKB	Modified residue	411	411	.	.	.	Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443	
Q9Z2D3	UniProtKB	Modified residue	420	420	.	.	.	Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60443