##gff-version 3
P97864	UniProtKB	Propeptide	1	23	.	.	.	ID=PRO_0000004624;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18667412;Dbxref=PMID:18667412	
P97864	UniProtKB	Chain	24	198	.	.	.	ID=PRO_0000004625;Note=Caspase-7 subunit p20;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18667412;Dbxref=PMID:18667412	
P97864	UniProtKB	Propeptide	199	206	.	.	.	ID=PRO_0000004626;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18667412;Dbxref=PMID:18667412	
P97864	UniProtKB	Chain	207	303	.	.	.	ID=PRO_0000004627;Note=Caspase-7 subunit p11;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Region	1	26	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P97864	UniProtKB	Region	38	41	.	.	.	Note=Exosite;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Region	76	87	.	.	.	Note=Loop L1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Region	187	196	.	.	.	Note=Loop L2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Region	226	238	.	.	.	Note=Loop L3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Region	274	288	.	.	.	Note=Loop L4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Active site	144	144	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29466	
P97864	UniProtKB	Active site	186	186	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Site	36	37	.	.	.	Note=Cleavage%3B by CAPN1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Site	45	46	.	.	.	Note=Cleavage%3B by CAPN1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Site	47	48	.	.	.	Note=Cleavage%3B by CAPN1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Site	187	187	.	.	.	Note=Involved in allosteric regulation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Site	223	223	.	.	.	Note=Involved in allosteric regulation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17242355;Dbxref=PMID:17242355	
P97864	UniProtKB	Modified residue	30	30	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Modified residue	173	173	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Modified residue	239	239	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55210	
P97864	UniProtKB	Mutagenesis	23	23	.	.	.	Note=Abolished cleavage and activation%3B when associated with A-198. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18667412;Dbxref=PMID:18667412	
P97864	UniProtKB	Mutagenesis	198	198	.	.	.	Note=Abolished cleavage and activation%3B when associated with A-23. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18667412;Dbxref=PMID:18667412	
P97864	UniProtKB	Sequence conflict	10	11	.	.	.	Note=EL->DW;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P97864	UniProtKB	Sequence conflict	45	45	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P97864	UniProtKB	Sequence conflict	48	49	.	.	.	Note=VR->RQ;Ontology_term=ECO:0000305;evidence=ECO:0000305