##gff-version 3
Q8C129	UniProtKB	Chain	1	1025	.	.	.	ID=PRO_0000278198;Note=Leucyl-cystinyl aminopeptidase	
Q8C129	UniProtKB	Topological domain	1	109	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Transmembrane	110	131	.	.	.	Note=Helical%3B Signal-anchor for type II membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Topological domain	132	1025	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Region	96	101	.	.	.	Note=Tankyrase binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8C129	UniProtKB	Motif	53	54	.	.	.	Note=Dileucine internalization motif;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Motif	76	77	.	.	.	Note=Dileucine internalization motif;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Active site	465	465	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
Q8C129	UniProtKB	Binding site	295	295	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8C129	UniProtKB	Binding site	428	432	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8C129	UniProtKB	Binding site	464	464	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
Q8C129	UniProtKB	Binding site	468	468	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
Q8C129	UniProtKB	Binding site	487	487	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
Q8C129	UniProtKB	Site	549	549	.	.	.	Note=Transition state stabilizer;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q8C129	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UIQ6	
Q8C129	UniProtKB	Modified residue	70	70	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19144319;Dbxref=PMID:19144319	
Q8C129	UniProtKB	Modified residue	80	80	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19144319,ECO:0007744|PubMed:21183079;Dbxref=PMID:19144319,PMID:21183079	
Q8C129	UniProtKB	Modified residue	91	91	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19144319;Dbxref=PMID:19144319	
Q8C129	UniProtKB	Glycosylation	145	145	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	184	184	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	215	215	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	256	256	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	266	266	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	368	368	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	374	374	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	447	447	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
Q8C129	UniProtKB	Glycosylation	525	525	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	578	578	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	664	664	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	682	682	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19349973;Dbxref=PMID:19349973	
Q8C129	UniProtKB	Glycosylation	695	695	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	758	758	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	834	834	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	850	850	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q8C129	UniProtKB	Glycosylation	989	989	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255