##gff-version 3
Q9JIZ9	UniProtKB	Chain	1	296	.	.	.	ID=PRO_0000100790;Note=Phospholipid scramblase 3	
Q9JIZ9	UniProtKB	Topological domain	1	266	.	.	.	Note=Mitochondrial intermembrane;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6QBQ4	
Q9JIZ9	UniProtKB	Transmembrane	267	283	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JIZ9	UniProtKB	Region	1	58	.	.	.	Note=Proline-rich domain (PRD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O15162	
Q9JIZ9	UniProtKB	Region	1	45	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9JIZ9	UniProtKB	Motif	7	15	.	.	.	Note=SH3-binding 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JIZ9	UniProtKB	Motif	15	18	.	.	.	Note=PPxY motif;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JIZ9	UniProtKB	Motif	21	27	.	.	.	Note=SH3-binding 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JIZ9	UniProtKB	Motif	66	71	.	.	.	Note=SH3-binding 3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JIZ9	UniProtKB	Compositional bias	8	45	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9JIZ9	UniProtKB	Lipidation	159	159	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21785166;Dbxref=PMID:21785166	
Q9JIZ9	UniProtKB	Lipidation	161	161	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21785166;Dbxref=PMID:21785166	
Q9JIZ9	UniProtKB	Lipidation	163	163	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21785166;Dbxref=PMID:21785166	
Q9JIZ9	UniProtKB	Lipidation	164	164	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21785166;Dbxref=PMID:21785166	
Q9JIZ9	UniProtKB	Lipidation	166	166	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21785166;Dbxref=PMID:21785166	
Q9JIZ9	UniProtKB	Mutagenesis	159	159	.	.	.	Note=Complete loss of palmitoylation%2C mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function%3B when associated with A-161%2C A-163%2C A-164 and A-166. Partial loss of palmitoylation%3B when associated with A-161. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21785166;Dbxref=PMID:21785166	
Q9JIZ9	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Complete loss of palmitoylation%2C mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function%3B when associated with A-159%2C A-163%2C A-164 and A-166. Partial loss of palmitoylation%3B when associated with A-159. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21785166;Dbxref=PMID:21785166	
Q9JIZ9	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Complete loss of palmitoylation%2C mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function%3B when associated with A-159%2C A-161%2C A-164 and A-166. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21785166;Dbxref=PMID:21785166	
Q9JIZ9	UniProtKB	Mutagenesis	164	164	.	.	.	Note=Complete loss of palmitoylation%2C mislocalization from mitochondrial membrane and reduced apoptotic function%3B when associated with A-159%2C A-161%2C A-163 and A-166. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21785166;Dbxref=PMID:21785166	
Q9JIZ9	UniProtKB	Mutagenesis	166	166	.	.	.	Note=Complete loss of palmitoylation%2C mislocalization from mitochondrial membrane to nucleus and reduced apoptotic function%3B when associated with A-159%2C A-161%2C A-163 and A-164. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21785166;Dbxref=PMID:21785166