##gff-version 3 P30533 UniProtKB Signal peptide 1 34 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P30533 UniProtKB Chain 35 357 . . . ID=PRO_0000020724;Note=Alpha-2-macroglobulin receptor-associated protein P30533 UniProtKB Region 32 52 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P30533 UniProtKB Region 237 353 . . . Note=LDL receptor binding;Ontology_term=ECO:0000255;evidence=ECO:0000255 P30533 UniProtKB Coiled coil 219 310 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P30533 UniProtKB Motif 354 357 . . . Note=Prevents secretion from ER;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7774585;Dbxref=PMID:7774585 P30533 UniProtKB Compositional bias 36 52 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P30533 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99068 P30533 UniProtKB Modified residue 135 135 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P55302 P30533 UniProtKB Modified residue 248 248 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P30533 UniProtKB Glycosylation 268 268 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19159218;Dbxref=PMID:19159218 P30533 UniProtKB Natural variant 114 114 . . . ID=VAR_050660;Note=N->S;Dbxref=dbSNP:rs2228158 P30533 UniProtKB Natural variant 311 311 . . . ID=VAR_011821;Note=V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9782079;Dbxref=dbSNP:rs1800493,PMID:9782079 P30533 UniProtKB Mutagenesis 283 283 . . . Note=Strongly reduced interaction with LRP1%3B when associated with A-291%3B A-293%3B A-302%3B A-307 and A-341. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678114;Dbxref=PMID:16678114 P30533 UniProtKB Mutagenesis 290 290 . . . Note=Reduces competition with MAPT for binding to LRP1%3B when associated with A-304. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32296178;Dbxref=PMID:32296178 P30533 UniProtKB Mutagenesis 291 291 . . . Note=Strongly reduced interaction with LRP1%3B when associated with A-283%3B A-293%3B A-302%3B A-307 and A-341. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678114;Dbxref=PMID:16678114 P30533 UniProtKB Mutagenesis 293 293 . . . Note=Strongly reduced interaction with LRP1%3B when associated with A-283%3B A-291%3B A-302%3B A-307 and A-341. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678114;Dbxref=PMID:16678114 P30533 UniProtKB Mutagenesis 302 302 . . . Note=Strongly reduced interaction with LRP1%3B when associated with A-283%3B A-291%3B A-293%3B A-307 and A-341. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678114;Dbxref=PMID:16678114 P30533 UniProtKB Mutagenesis 304 304 . . . Note=Reduces competition with MAPT for binding to LRP1%3B when associated with A-290. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32296178;Dbxref=PMID:32296178 P30533 UniProtKB Mutagenesis 307 307 . . . Note=Strongly reduced interaction with LRP1%3B when associated with A-283%3B A-291%3B A-293%3B A-302 and A-341. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678114;Dbxref=PMID:16678114 P30533 UniProtKB Mutagenesis 341 341 . . . Note=Strongly reduced interaction with LRP1%3B when associated with A-283%3B A-291%3B A-293%3B A-302 and A-307. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16678114;Dbxref=PMID:16678114 P30533 UniProtKB Sequence conflict 100 100 . . . Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P30533 UniProtKB Sequence conflict 183 183 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P30533 UniProtKB Sequence conflict 339 339 . . . Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 P30533 UniProtKB Beta strand 53 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LRE P30533 UniProtKB Helix 57 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LRE P30533 UniProtKB Helix 73 99 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LRE P30533 UniProtKB Helix 107 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1LRE P30533 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1NRE P30533 UniProtKB Beta strand 127 130 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1OP1 P30533 UniProtKB Helix 149 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P01 P30533 UniProtKB Helix 166 195 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P01 P30533 UniProtKB Beta strand 208 210 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P01 P30533 UniProtKB Beta strand 213 216 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P01 P30533 UniProtKB Helix 217 243 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P01 P30533 UniProtKB Beta strand 246 249 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2FTU P30533 UniProtKB Helix 255 265 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2FCW P30533 UniProtKB Helix 271 311 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2FCW P30533 UniProtKB Turn 314 316 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2FCW P30533 UniProtKB Helix 317 353 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2FCW