##gff-version 3
P99999	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:13933734,ECO:0000269|PubMed:14063298;Dbxref=PMID:13933734,PMID:14063298	
P99999	UniProtKB	Chain	2	105	.	.	.	ID=PRO_0000108218;Note=Cytochrome c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00433	
P99999	UniProtKB	Binding site	15	15	.	.	.	Note=Covalent;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00433,ECO:0000269|PubMed:23150584;Dbxref=PMID:23150584	
P99999	UniProtKB	Binding site	18	18	.	.	.	Note=Covalent;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00433,ECO:0000269|PubMed:23150584;Dbxref=PMID:23150584	
P99999	UniProtKB	Binding site	19	19	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00433,ECO:0000269|PubMed:23150584;Dbxref=PMID:23150584	
P99999	UniProtKB	Binding site	81	81	.	.	.	Note=Axial binding residue	
P99999	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylglycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:13933734;Dbxref=PMID:13933734	
P99999	UniProtKB	Modified residue	49	49	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62894	
P99999	UniProtKB	Modified residue	56	56	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62897	
P99999	UniProtKB	Modified residue	73	73	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62897	
P99999	UniProtKB	Modified residue	73	73	.	.	.	Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62897	
P99999	UniProtKB	Modified residue	98	98	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62894	
P99999	UniProtKB	Modified residue	100	100	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62897	
P99999	UniProtKB	Natural variant	42	42	.	.	.	ID=VAR_044450;Note=In THC4%3B increases the pro-apoptotic function by triggering caspase activation more efficiently than wild-type%3B does not affect the redox function. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18345000;Dbxref=dbSNP:rs121918552,PMID:18345000	
P99999	UniProtKB	Natural variant	56	56	.	.	.	ID=VAR_048850;Note=K->R;Dbxref=dbSNP:rs11548795	
P99999	UniProtKB	Natural variant	66	66	.	.	.	ID=VAR_002204;Note=M->L	
P99999	UniProtKB	Mutagenesis	6	6	.	.	.	Note=No effect on covalent heme attachment. K->A%2CD%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23150584;Dbxref=PMID:23150584	
P99999	UniProtKB	Mutagenesis	11	11	.	.	.	Note=Decreased covalent heme attachment. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23150584;Dbxref=PMID:23150584	
P99999	UniProtKB	Mutagenesis	11	11	.	.	.	Note=No effect on covalent heme attachment. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23150584;Dbxref=PMID:23150584	
P99999	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Decreased covalent heme attachment. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23150584;Dbxref=PMID:23150584	
P99999	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Decreased covalent heme attachment. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23150584;Dbxref=PMID:23150584	
P99999	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Loss of covalent heme attachment. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23150584;Dbxref=PMID:23150584	
P99999	UniProtKB	Sequence conflict	18	18	.	.	.	Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P99999	UniProtKB	Sequence conflict	41	41	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P99999	UniProtKB	Helix	4	14	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TY3	
P99999	UniProtKB	Turn	15	18	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TY3	
P99999	UniProtKB	Beta strand	23	25	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J3S	
P99999	UniProtKB	Beta strand	28	30	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J3S	
P99999	UniProtKB	Turn	36	38	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J3S	
P99999	UniProtKB	Beta strand	39	42	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2N9I	
P99999	UniProtKB	Helix	51	55	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TY3	
P99999	UniProtKB	Beta strand	56	58	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2N3Y	
P99999	UniProtKB	Helix	62	70	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TY3	
P99999	UniProtKB	Helix	72	75	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TY3	
P99999	UniProtKB	Beta strand	76	78	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2N3Y	
P99999	UniProtKB	Helix	89	102	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TY3