##gff-version 3
Q9H6L5	UniProtKB	Chain	1	497	.	.	.	ID=PRO_0000288466;Note=Reticulophagy regulator 1	
Q9H6L5	UniProtKB	Topological domain	1	59	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26040720;Dbxref=PMID:26040720	
Q9H6L5	UniProtKB	Transmembrane	60	80	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H6L5	UniProtKB	Topological domain	81	95	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9H6L5	UniProtKB	Transmembrane	96	116	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H6L5	UniProtKB	Topological domain	117	118	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9H6L5	UniProtKB	Transmembrane	119	139	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H6L5	UniProtKB	Topological domain	140	208	.	.	.	Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9H6L5	UniProtKB	Transmembrane	209	229	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9H6L5	UniProtKB	Topological domain	230	497	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26040720;Dbxref=PMID:26040720	
Q9H6L5	UniProtKB	Region	1	51	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9H6L5	UniProtKB	Region	84	233	.	.	.	Note=Reticulon homology domain;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26040720;Dbxref=PMID:26040720	
Q9H6L5	UniProtKB	Region	319	365	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9H6L5	UniProtKB	Region	377	396	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9H6L5	UniProtKB	Region	436	455	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9H6L5	UniProtKB	Region	468	497	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9H6L5	UniProtKB	Motif	453	458	.	.	.	Note=LIR motif;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:26040720;Dbxref=PMID:26040720	
Q9H6L5	UniProtKB	Compositional bias	20	34	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9H6L5	UniProtKB	Compositional bias	468	490	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9H6L5	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31930741;Dbxref=PMID:31930741	
Q9H6L5	UniProtKB	Modified residue	151	151	.	.	.	Note=Phosphoserine%3B by CAMK2B;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31930741;Dbxref=PMID:31930741	
Q9H6L5	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31930741;Dbxref=PMID:31930741	
Q9H6L5	UniProtKB	Alternative sequence	1	141	.	.	.	ID=VSP_025685;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:14702039,PMID:15489334	
Q9H6L5	UniProtKB	Alternative sequence	142	152	.	.	.	ID=VSP_025686;Note=In isoform 2. RGAQLWRSLSE->MPEGEDFGPGK;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:14702039,PMID:15489334	
Q9H6L5	UniProtKB	Natural variant	216	216	.	.	.	ID=VAR_068477;Note=Found in a patient with HSAN2B%3B uncertain significance%3B dramatically enhances homooligomerization which results in aberrant endoplasmic reticulum scission and excessive reticulophagy%3B induces sensory neuron death in vitro. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22302274;Dbxref=dbSNP:rs1579584286,PMID:22302274	
Q9H6L5	UniProtKB	Natural variant	379	379	.	.	.	ID=VAR_032422;Note=Q->E;Dbxref=dbSNP:rs34432513	
Q9H6L5	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Reduces self-association. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31930741;Dbxref=PMID:31930741	
Q9H6L5	UniProtKB	Mutagenesis	149	149	.	.	.	Note=Phosphomimetic mutant which enhances self-association. Enhanced membrane scission activity%3B when associated with D-151 and D-153. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31930741;Dbxref=PMID:31930741	
Q9H6L5	UniProtKB	Mutagenesis	151	151	.	.	.	Note=Abolishes phosphorylation and reduces self-association. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31930741;Dbxref=PMID:31930741	
Q9H6L5	UniProtKB	Mutagenesis	151	151	.	.	.	Note=Phosphomimetic mutant which enhances self-association. Enhanced membrane scission activity%3B when associated with D-149 and D-153. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31930741;Dbxref=PMID:31930741	
Q9H6L5	UniProtKB	Mutagenesis	153	153	.	.	.	Note=Reduces self-association. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31930741;Dbxref=PMID:31930741	
Q9H6L5	UniProtKB	Mutagenesis	153	153	.	.	.	Note=Phosphomimetic mutant which enhances self-association. Enhanced membrane scission activity%3B when associated with D-149 and D-151. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31930741;Dbxref=PMID:31930741	
Q9H6L5	UniProtKB	Mutagenesis	453	458	.	.	.	Note=Abolishes interaction with ATG8 family proteins. DDFELL->AAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26040720;Dbxref=PMID:26040720	
Q9H6L5	UniProtKB	Mutagenesis	455	458	.	.	.	Note=Abolishes interaction with ATG8 family proteins and reduces endoplasmic reticulum branching. FELL->AELA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34338405;Dbxref=PMID:34338405	
Q9H6L5	UniProtKB	Mutagenesis	456	456	.	.	.	Note=Severely impaired binding to GABARAP. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34854256;Dbxref=PMID:34854256	
Q9H6L5	UniProtKB	Mutagenesis	462	462	.	.	.	Note=Severely impaired binding to GABARAP. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34854256;Dbxref=PMID:34854256	
Q9H6L5	UniProtKB	Mutagenesis	463	463	.	.	.	Note=Mildly weakened binding to GABARAP. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34854256;Dbxref=PMID:34854256	
Q9H6L5	UniProtKB	Mutagenesis	466	466	.	.	.	Note=Mildly weakened binding to GABARAP. I->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34854256;Dbxref=PMID:34854256	
Q9H6L5	UniProtKB	Sequence conflict	382	382	.	.	.	Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9H6L5	UniProtKB	Helix	461	465	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7BRQ