##gff-version 3
P56818	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P56818	UniProtKB	Propeptide	22	45	.	.	.	ID=PRO_0000025941;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P56818	UniProtKB	Chain	46	501	.	.	.	ID=PRO_0000025942;Note=Beta-secretase 1	
P56818	UniProtKB	Topological domain	22	457	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P56818	UniProtKB	Transmembrane	458	478	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P56818	UniProtKB	Topological domain	479	501	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P56818	UniProtKB	Domain	75	416	.	.	.	Note=Peptidase A1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01103	
P56818	UniProtKB	Region	39	58	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P56818	UniProtKB	Region	479	501	.	.	.	Note=Interaction with RTN3;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P56818	UniProtKB	Motif	496	500	.	.	.	Note=DXXLL;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56817	
P56818	UniProtKB	Compositional bias	43	58	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P56818	UniProtKB	Active site	93	93	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
P56818	UniProtKB	Active site	289	289	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10094	
P56818	UniProtKB	Modified residue	126	126	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56817	
P56818	UniProtKB	Modified residue	275	275	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56817	
P56818	UniProtKB	Modified residue	279	279	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56817	
P56818	UniProtKB	Modified residue	285	285	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56817	
P56818	UniProtKB	Modified residue	299	299	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56817	
P56818	UniProtKB	Modified residue	300	300	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56817	
P56818	UniProtKB	Modified residue	307	307	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56817	
P56818	UniProtKB	Modified residue	498	498	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P56818	UniProtKB	Lipidation	474	474	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19074428;Dbxref=PMID:19074428	
P56818	UniProtKB	Lipidation	478	478	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19074428;Dbxref=PMID:19074428	
P56818	UniProtKB	Lipidation	482	482	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19074428;Dbxref=PMID:19074428	
P56818	UniProtKB	Lipidation	485	485	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19074428;Dbxref=PMID:19074428	
P56818	UniProtKB	Glycosylation	153	153	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26467158;Dbxref=PMID:26467158	
P56818	UniProtKB	Glycosylation	172	172	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26467158;Dbxref=PMID:26467158	
P56818	UniProtKB	Glycosylation	223	223	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26467158;Dbxref=PMID:26467158	
P56818	UniProtKB	Glycosylation	354	354	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26467158;Dbxref=PMID:26467158	
P56818	UniProtKB	Disulfide bond	216	420	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P56818	UniProtKB	Disulfide bond	278	443	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P56818	UniProtKB	Disulfide bond	330	380	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P56818	UniProtKB	Cross-link	501	501	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P56817	
P56818	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Loss of catalytic activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29325091;Dbxref=PMID:29325091	
P56818	UniProtKB	Mutagenesis	153	153	.	.	.	Note=Decreases bisecting N-acetylglucosamine levels. Almost abolishes bisecting N-acetylglucosamine levels but has no effect on surface expression%3B when associated with S-223. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26467158;Dbxref=PMID:26467158	
P56818	UniProtKB	Mutagenesis	172	172	.	.	.	Note=Slightly decreases bisecting N-acetylglucosamine levels. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26467158;Dbxref=PMID:26467158	
P56818	UniProtKB	Mutagenesis	223	223	.	.	.	Note=Decreases bisecting N-acetylglucosamine levels. Almost abolishes bisecting N-acetylglucosamine levels but has no effect on surface expression%3B when associated with S-153. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26467158;Dbxref=PMID:26467158	
P56818	UniProtKB	Mutagenesis	354	354	.	.	.	Note=Slightly decreases bisecting N-acetylglucosamine levels. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26467158;Dbxref=PMID:26467158	
P56818	UniProtKB	Mutagenesis	474	474	.	.	.	Note=Completely abolishes S-palmitoylation%3B when associated with A-478%3B A-482 and A-485. Doesn't affect trans-Golgi network and endosome localization%3B when associated with A-478%3B A-482 and A-485. Reduces membrane raft association%3B when associated with A-478%3B A-482 and A-485. Doesn't affect APP processing%3B when associated with A-478%3B A-482 and A-485. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19074428;Dbxref=PMID:19074428	
P56818	UniProtKB	Mutagenesis	478	478	.	.	.	Note=Significantly reduces S-palmitoylation%3B when associated with A-482 and A-485. Completely abolishes S-palmitoylation%3B when associated with A-474%3B A-482 and A-485. Doesn't affect trans-Golgi network and endosome localization%3B when associated with A-474%3B A-482 and A-485. Reduces membrane raft association%3B when associated with A-474%3B A-482 and A-485. Doesn't affect APP processing%3B when associated with A-474%3B A-482 and A-485. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19074428;Dbxref=PMID:19074428	
P56818	UniProtKB	Mutagenesis	482	482	.	.	.	Note=Significantly reduces S-palmitoylation%3B when associated with A-478 and A-485. Completely abolishes S-palmitoylation%3B when associated with A-474%3B A-478 and A-485. Doesn't affect trans-Golgi network and endosome localization%3B when associated with A-474%3B A-478 and A-485. Reduces membrane raft association%3B when associated with A-474%3B A-478 and A-485. Doesn't affect APP processing%3B when associated with A-474%3B A-478 and A-485. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19074428;Dbxref=PMID:19074428	
P56818	UniProtKB	Mutagenesis	485	485	.	.	.	Note=Significantly reduces S-palmitoylation%3B when associated with A-478 and A-482. Completely abolishes S-palmitoylation%3B when associated with A-474%3B A-478 and A-482. Doesn't affect trans-Golgi network and endosome localization%3B when associated with A-474%3B A-478 and A-482. Reduces membrane raft association%3B when associated with A-474%3B A-478 and A-482. Doesn't affect APP processing%3B when associated with A-474%3B A-478 and A-482. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19074428;Dbxref=PMID:19074428