##gff-version 3
Q9H444	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|Ref.6,ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
Q9H444	UniProtKB	Chain	2	224	.	.	.	ID=PRO_0000211489;Note=Charged multivesicular body protein 4b	
Q9H444	UniProtKB	Region	1	23	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9H444	UniProtKB	Region	185	224	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9H444	UniProtKB	Coiled coil	23	183	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H444	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|Ref.6,ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
Q9H444	UniProtKB	Modified residue	6	6	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861	
Q9H444	UniProtKB	Modified residue	114	114	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861	
Q9H444	UniProtKB	Modified residue	184	184	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231	
Q9H444	UniProtKB	Modified residue	223	223	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692;Dbxref=PMID:20068231,PMID:21406692	
Q9H444	UniProtKB	Natural variant	129	129	.	.	.	ID=VAR_037579;Note=In CTRCT31. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17701905;Dbxref=dbSNP:rs118203965,PMID:17701905	
Q9H444	UniProtKB	Natural variant	161	161	.	.	.	ID=VAR_037580;Note=In CTRCT31. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17701905;Dbxref=dbSNP:rs118203966,PMID:17701905	
Q9H444	UniProtKB	Mutagenesis	54	54	.	.	.	Note=No loss of interaction with CC2D1B and forms a disulfide bond locking the protein in its folded closed conformation when exposed to oxidizing conditions%3B when associated with C-180. A->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33349255;Dbxref=PMID:33349255	
Q9H444	UniProtKB	Mutagenesis	180	180	.	.	.	Note=No loss of interaction with CC2D1B and forms a disulfide bond locking the protein in its folded closed conformation when exposed to oxidizing conditions%3B when associated with C-54. L->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33349255;Dbxref=PMID:33349255	
Q9H444	UniProtKB	Helix	23	57	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ABM	
Q9H444	UniProtKB	Helix	62	96	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ABM	
Q9H444	UniProtKB	Helix	209	212	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3C3Q	
Q9H444	UniProtKB	Helix	213	221	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5MK2