##gff-version 3 P49769 UniProtKB Chain 1 298 . . . ID=PRO_0000025597;Note=Presenilin-1 NTF subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250 P49769 UniProtKB Chain 299 467 . . . ID=PRO_0000025598;Note=Presenilin-1 CTF subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250 P49769 UniProtKB Chain 346 467 . . . ID=PRO_0000236058;Note=Presenilin-1 CTF12;Ontology_term=ECO:0000250;evidence=ECO:0000250 P49769 UniProtKB Topological domain 1 82 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Transmembrane 83 103 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Topological domain 104 132 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Transmembrane 133 153 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Topological domain 154 166 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Transmembrane 167 189 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Topological domain 190 194 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Transmembrane 195 216 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Topological domain 217 220 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Transmembrane 221 241 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Topological domain 242 248 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Transmembrane 249 272 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Topological domain 273 380 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Transmembrane 381 401 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Topological domain 402 407 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Transmembrane 408 428 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Topological domain 429 432 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Transmembrane 433 453 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Topological domain 454 467 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Region 1 68 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P49769 UniProtKB Region 288 290 . . . Note=Important for cleavage of target proteins;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Region 304 357 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P49769 UniProtKB Region 322 450 . . . Note=Required for interaction with CTNNB1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Region 372 399 . . . Note=Required for interaction with CTNND2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Region 377 381 . . . Note=Important for cleavage of target proteins;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Region 432 434 . . . Note=Important for cleavage of target proteins;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Region 464 467 . . . Note=Interaction with MTCH1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Motif 433 435 . . . Note=PAL P49769 UniProtKB Compositional bias 1 32 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P49769 UniProtKB Compositional bias 33 47 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P49769 UniProtKB Compositional bias 304 328 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P49769 UniProtKB Compositional bias 337 352 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P49769 UniProtKB Active site 257 257 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Active site 385 385 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Site 291 292 . . . Note=Cleavage%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Site 292 293 . . . Note=Cleavage%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Site 298 299 . . . Note=Cleavage;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Site 345 346 . . . Note=Cleavage%3B by caspase;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Modified residue 51 51 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P97887 P49769 UniProtKB Modified residue 329 329 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19144319,ECO:0007744|PubMed:21183079;Dbxref=PMID:19144319,PMID:21183079 P49769 UniProtKB Modified residue 346 346 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49768 P49769 UniProtKB Modified residue 367 367 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:21183079;Dbxref=PMID:17242355,PMID:21183079 P49769 UniProtKB Modified residue 370 370 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:21183079;Dbxref=PMID:17242355,PMID:21183079 P49769 UniProtKB Modified residue 371 371 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:21183079;Dbxref=PMID:17242355,PMID:21183079 P49769 UniProtKB Alternative sequence 257 261 . . . ID=VSP_008381;Note=In isoform 2. DLVAV->GKAQD;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P49769 UniProtKB Alternative sequence 262 467 . . . ID=VSP_008382;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P49769 UniProtKB Natural variant 9 9 . . . Note=In strain: SAMP8. S->T P49769 UniProtKB Natural variant 40 40 . . . Note=In strain: SAMP8. D->E P49769 UniProtKB Natural variant 67 67 . . . Note=In strain: SAMP8. E->CM P49769 UniProtKB Natural variant 196 196 . . . Note=In strain: SAMP8. V->L P49769 UniProtKB Natural variant 321 322 . . . Note=In strain: SAMP8. ER->RRD