##gff-version 3
Q5SW96	UniProtKB	Chain	1	308	.	.	.	ID=PRO_0000064675;Note=Low density lipoprotein receptor adapter protein 1	
Q5SW96	UniProtKB	Domain	42	196	.	.	.	Note=PID;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00148	
Q5SW96	UniProtKB	Region	249	276	.	.	.	Note=AP-2 complex binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12221107;Dbxref=PMID:12221107	
Q5SW96	UniProtKB	Motif	212	216	.	.	.	Note=Clathrin box;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12221107;Dbxref=PMID:12221107	
Q5SW96	UniProtKB	Motif	257	266	.	.	.	Note=[DE]-X(1%2C2)-F-X-X-[FL]-X-X-X-R motif;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16516836;Dbxref=PMID:16516836	
Q5SW96	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
Q5SW96	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163	
Q5SW96	UniProtKB	Modified residue	186	186	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q5SW96	UniProtKB	Modified residue	202	202	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8C142	
Q5SW96	UniProtKB	Natural variant	56	56	.	.	.	ID=VAR_076925;Note=Found in patients with hypercholesterolemia%3B likely pathogenic. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20124734;Dbxref=dbSNP:rs752849346,PMID:20124734	
Q5SW96	UniProtKB	Natural variant	202	202	.	.	.	ID=VAR_023320;Note=In FHCL4%3B Lebanon%3B requires 2 nucleotide substitutions. S->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11326085;Dbxref=dbSNP:rs386629678,PMID:11326085	
Q5SW96	UniProtKB	Natural variant	202	202	.	.	.	ID=VAR_028403;Note=S->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11326085,ECO:0000269|PubMed:12417523,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:17974005,ECO:0000269|PubMed:20124734;Dbxref=dbSNP:rs6687605,PMID:11326085,PMID:12417523,PMID:15489334,PMID:17974005,PMID:20124734	
Q5SW96	UniProtKB	Mutagenesis	165	165	.	.	.	Note=Abolishes LDLR cytoplasmic tail binding. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12221107;Dbxref=PMID:12221107	
Q5SW96	UniProtKB	Mutagenesis	165	165	.	.	.	Note=Abolishes LDLR cytoplasmic tail binding. F->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12221107;Dbxref=PMID:12221107	
Q5SW96	UniProtKB	Mutagenesis	212	213	.	.	.	Note=Abolishes clathrin binding. LL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12221107;Dbxref=PMID:12221107	
Q5SW96	UniProtKB	Mutagenesis	214	214	.	.	.	Note=Abolishes clathrin binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12221107;Dbxref=PMID:12221107	
Q5SW96	UniProtKB	Mutagenesis	216	216	.	.	.	Note=Abolishes clathrin binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12221107;Dbxref=PMID:12221107	
Q5SW96	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Abolishes interaction with AP2B1. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16903783;Dbxref=PMID:16903783	
Q5SW96	UniProtKB	Mutagenesis	266	266	.	.	.	Note=Abolishes AP-2 complex binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12221107;Dbxref=PMID:12221107	
Q5SW96	UniProtKB	Helix	256	266	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G30