##gff-version 3
O75381	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|Ref.8,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22814378,ECO:0007744|PubMed:25944712;Dbxref=PMID:19413330,PMID:22814378,PMID:25944712	
O75381	UniProtKB	Chain	2	377	.	.	.	ID=PRO_0000058325;Note=Peroxisomal membrane protein PEX14	
O75381	UniProtKB	Topological domain	2	108	.	.	.	Note=Peroxisomal matrix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q642G4	
O75381	UniProtKB	Transmembrane	109	126	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O75381	UniProtKB	Topological domain	127	377	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q642G4	
O75381	UniProtKB	Region	1	24	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O75381	UniProtKB	Region	230	377	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O75381	UniProtKB	Compositional bias	1	21	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O75381	UniProtKB	Compositional bias	244	282	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O75381	UniProtKB	Compositional bias	319	338	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O75381	UniProtKB	Compositional bias	339	377	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O75381	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|Ref.8,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22814378,ECO:0007744|PubMed:25944712;Dbxref=PMID:19413330,PMID:22814378,PMID:25944712	
O75381	UniProtKB	Modified residue	34	34	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861	
O75381	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
O75381	UniProtKB	Modified residue	282	282	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q642G4	
O75381	UniProtKB	Modified residue	335	335	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17081983;Dbxref=PMID:17081983	
O75381	UniProtKB	Alternative sequence	58	100	.	.	.	ID=VSP_037021;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
O75381	UniProtKB	Natural variant	117	117	.	.	.	ID=VAR_051269;Note=A->S;Dbxref=dbSNP:rs12061667	
O75381	UniProtKB	Natural variant	150	150	.	.	.	ID=VAR_051270;Note=A->S;Dbxref=dbSNP:rs11539793	
O75381	UniProtKB	Natural variant	320	320	.	.	.	ID=VAR_051271;Note=R->K;Dbxref=dbSNP:rs12070353	
O75381	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Reduced interaction with PEX19%2C minor effect on interaction with PEX5. F->A%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19197237;Dbxref=PMID:19197237	
O75381	UniProtKB	Mutagenesis	56	56	.	.	.	Note=Reduced interaction with PEX19%2C minor effect on interaction with PEX5. K->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19197237;Dbxref=PMID:19197237	
O75381	UniProtKB	Sequence conflict	319	319	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O75381	UniProtKB	Beta strand	19	22	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4BXU	
O75381	UniProtKB	Helix	26	36	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W84	
O75381	UniProtKB	Helix	41	43	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W84	
O75381	UniProtKB	Helix	46	55	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W84	
O75381	UniProtKB	Helix	60	70	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2W84