##gff-version 3
Q9H300	UniProtKB	Transit peptide	1	52	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14732705;Dbxref=PMID:14732705	
Q9H300	UniProtKB	Chain	53	379	.	.	.	ID=PRO_0000027386;Note=Presenilin-associated rhomboid-like protein%2C mitochondrial	
Q9H300	UniProtKB	Peptide	53	77	.	.	.	ID=PRO_0000027387;Note=P-beta;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14732705;Dbxref=PMID:14732705	
Q9H300	UniProtKB	Topological domain	53	101	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Transmembrane	102	121	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Topological domain	122	167	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Transmembrane	168	187	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Topological domain	188	207	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Transmembrane	208	230	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Topological domain	231	244	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Transmembrane	245	262	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Topological domain	263	272	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Transmembrane	273	289	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Topological domain	290	295	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Transmembrane	296	318	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Topological domain	319	332	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Transmembrane	333	354	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Topological domain	355	379	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H300	UniProtKB	Active site	277	277	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9H300	UniProtKB	Active site	335	335	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9H300	UniProtKB	Modified residue	65	65	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17116872;Dbxref=PMID:17116872	
Q9H300	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17116872;Dbxref=PMID:17116872	
Q9H300	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17116872;Dbxref=PMID:17116872	
Q9H300	UniProtKB	Alternative sequence	203	253	.	.	.	ID=VSP_013310;Note=In isoform 2. KVLCSPMLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAG->S;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
Q9H300	UniProtKB	Natural variant	137	137	.	.	.	ID=VAR_029801;Note=A->G;Dbxref=dbSNP:rs4912470	
Q9H300	UniProtKB	Natural variant	262	262	.	.	.	ID=VAR_021578;Note=V->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12214059,ECO:0000269|Ref.3;Dbxref=dbSNP:rs3732581,PMID:12214059	
Q9H300	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Strongly reduces the beta cleavage%3B when associated with D-69 and D-70. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17116872;Dbxref=PMID:17116872	
Q9H300	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Strongly reduces the beta cleavage%3B when associated with D-65 and D-70. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17116872;Dbxref=PMID:17116872	
Q9H300	UniProtKB	Mutagenesis	70	70	.	.	.	Note=Strongly reduces the beta cleavage%3B when associated with D-65 and D-69. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17116872;Dbxref=PMID:17116872	
Q9H300	UniProtKB	Mutagenesis	76	76	.	.	.	Note=Abolishes the beta cleavage. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14732705;Dbxref=PMID:14732705	
Q9H300	UniProtKB	Mutagenesis	76	76	.	.	.	Note=Abolishes the beta cleavage. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14732705;Dbxref=PMID:14732705	
Q9H300	UniProtKB	Mutagenesis	77	77	.	.	.	Note=Abolishes the beta cleavage. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14732705;Dbxref=PMID:14732705	
Q9H300	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Abolishes the beta cleavage. A->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14732705;Dbxref=PMID:14732705	
Q9H300	UniProtKB	Mutagenesis	79	79	.	.	.	Note=Abolishes the beta cleavage. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14732705;Dbxref=PMID:14732705	
Q9H300	UniProtKB	Mutagenesis	277	277	.	.	.	Note=Loss of cleavage of CLPB%2C DIABLO%2C STARD7 and TTC19. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28288130;Dbxref=PMID:28288130	
Q9H300	UniProtKB	Mutagenesis	277	277	.	.	.	Note=Loss of PGAM5 cleavage. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22915595;Dbxref=PMID:22915595	
Q9H300	UniProtKB	Mutagenesis	335	335	.	.	.	Note=Loss of PGAM5 cleavage. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22915595;Dbxref=PMID:22915595