##gff-version 3
Q9UG56	UniProtKB	Transit peptide	1	52	.	.	.	Note=Mitochondrion;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9UG56	UniProtKB	Chain	53	409	.	.	.	ID=PRO_0000435571;Note=Phosphatidylserine decarboxylase proenzyme%2C mitochondrial	
Q9UG56	UniProtKB	Chain	53	377	.	.	.	ID=PRO_0000029835;Note=Phosphatidylserine decarboxylase beta chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Chain	378	409	.	.	.	ID=PRO_0000029836;Note=Phosphatidylserine decarboxylase alpha chain;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Topological domain	53	63	.	.	.	Note=Mitochondrial matrix;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Transmembrane	64	82	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Topological domain	83	409	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Active site	191	191	.	.	.	Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Active site	267	267	.	.	.	Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Active site	378	378	.	.	.	Note=Charge relay system%3B for autoendoproteolytic cleavage activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Active site	378	378	.	.	.	Note=Schiff-base intermediate with substrate%3B via pyruvic acid%3B for decarboxylase activity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Site	377	378	.	.	.	Note=Cleavage (non-hydrolytic)%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Modified residue	378	378	.	.	.	Note=Pyruvic acid (Ser)%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03208	
Q9UG56	UniProtKB	Alternative sequence	1	107	.	.	.	ID=VSP_007540;Note=In isoform 2. MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWE->MMCQSEARQGPELRAAKWLHFPQLALRRRLGQLSCMSRPALKLRSWPLTVLYYLLPFGALRPLSRVGWRPVSR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
Q9UG56	UniProtKB	Natural variant	277	277	.	.	.	ID=VAR_084458;Note=In LIBF%3B loss of autocatalytic processing%3B decreased protein abundance%3B decreased phosphatidylserine decarboxylase activity%3B changed mitochondrion organization. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30858161;Dbxref=dbSNP:rs147371584,PMID:30858161	
Q9UG56	UniProtKB	Natural variant	300	300	.	.	.	ID=VAR_084459;Note=In LIBF%3B loss of autocatalytic processing%3B probably decreased phosphatidylserine decarboxylase activity%3B changed mitochondrion organization%3B patient-derived fibroblasts show fragmented mitochondrial morphology around the nucleus%3B decreased cell viability with increased CASP3 and CASP7 activation. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:30488656,ECO:0000269|PubMed:30858161;Dbxref=dbSNP:rs2072505076,PMID:30488656,PMID:30858161	
Q9UG56	UniProtKB	Mutagenesis	378	378	.	.	.	Note=Loss of autocatalytic processing. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30858161;Dbxref=PMID:30858161	
Q9UG56	UniProtKB	Region	36	103	.	.	.	Note=Necessary for localization to both lipid droplets and mitochondria;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33593792;Dbxref=PMID:33593792