##gff-version 3 O15270 UniProtKB Chain 1 562 . . . ID=PRO_0000163858;Note=Serine palmitoyltransferase 2 O15270 UniProtKB Transmembrane 67 87 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O15270 UniProtKB Modified residue 379 379 . . . Note=N6-(pyridoxal phosphate)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250 O15270 UniProtKB Natural variant 182 182 . . . ID=VAR_069525;Note=In HSAN1C%3B reduced activity with L-serine as substrate%3B increased activity toward L-alanine resulting in the accumulation of 1-deoxy-sphinganine. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23658386;Dbxref=dbSNP:rs864621998,PMID:23658386 O15270 UniProtKB Natural variant 183 183 . . . ID=VAR_081286;Note=In HSAN1C%3B late onset%3B slightly increased activity with L-serine as substrate%3B highly increased activity toward L-alanine resulting in the accumulation of 1-deoxy-sphinganine. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26573920;Dbxref=dbSNP:rs775437084,PMID:26573920 O15270 UniProtKB Natural variant 359 359 . . . ID=VAR_064798;Note=In HSAN1C%3B partial loss of normal activity as measured by reduced formation of sphinganine%3B affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20920666;Dbxref=dbSNP:rs267607090,PMID:20920666 O15270 UniProtKB Natural variant 382 382 . . . ID=VAR_064799;Note=In HSAN1C%3B complete loss of normal activity as measured by lack of formation of sphinganine%3B affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20920666;Dbxref=dbSNP:rs267607089,PMID:20920666 O15270 UniProtKB Natural variant 504 504 . . . ID=VAR_064800;Note=In HSAN1C%3B partial loss of normal activity as measured by reduced formation of sphinganine%3B affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20920666;Dbxref=dbSNP:rs267607091,PMID:20920666 O15270 UniProtKB Mutagenesis 122 122 . . . Note=Decreased catalytic activity with L-serine and palmitoyl-CoA as substrates. Does not affect the negative regulation by OMRDL3 and ceramides. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:33558762,ECO:0000269|PubMed:37308477;Dbxref=PMID:33558762,PMID:37308477 O15270 UniProtKB Mutagenesis 126 126 . . . Note=Some decrease in catalytic activity with L-serine and palmitoyl-CoA as substrates. L->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558762;Dbxref=PMID:33558762 O15270 UniProtKB Mutagenesis 130 130 . . . Note=Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates. I->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558762;Dbxref=PMID:33558762 O15270 UniProtKB Mutagenesis 134 134 . . . Note=Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558762;Dbxref=PMID:33558762 O15270 UniProtKB Mutagenesis 176 176 . . . Note=Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558762;Dbxref=PMID:33558762 O15270 UniProtKB Mutagenesis 258 258 . . . Note=Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558762;Dbxref=PMID:33558762 O15270 UniProtKB Mutagenesis 302 302 . . . Note=Reduces the dimerization propensity with SPTLC1%3B reduces the dimerization propensity with SPTLC1%3B when associated with A-305. Does not impair enzymatic activity%3B when associated with A-304 and A-305. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558761;Dbxref=PMID:33558761 O15270 UniProtKB Mutagenesis 304 304 . . . Note=Reduces the dimerization propensity with SPTLC1%3B when associated with A-302 and A-304. Does not impair enzymatic activity%3B when associated with A-302 and A-304. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558761;Dbxref=PMID:33558761 O15270 UniProtKB Mutagenesis 305 305 . . . Note=Reduces the dimerization propensity with SPTLC1%3B when associated with A-302 and A-304. Does not impair enzymatic activity%3B when associated with A-302 and A-304. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558761;Dbxref=PMID:33558761 O15270 UniProtKB Mutagenesis 320 320 . . . Note=Decreased catalytic activity with L-serine and palmitoyl-CoA as substrates. M->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558762;Dbxref=PMID:33558762 O15270 UniProtKB Mutagenesis 378 378 . . . Note=Decreased catalytic activity with L-serine and palmitoyl-CoA as substrates. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558762;Dbxref=PMID:33558762 O15270 UniProtKB Mutagenesis 379 379 . . . Note=Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558762;Dbxref=PMID:33558762 O15270 UniProtKB Mutagenesis 479 479 . . . Note=Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates. I->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558762;Dbxref=PMID:33558762 O15270 UniProtKB Mutagenesis 503 503 . . . Note=Loss of negative regulation by OMRDL3 and ceramides. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37308477;Dbxref=PMID:37308477 O15270 UniProtKB Mutagenesis 509 509 . . . Note=Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558762;Dbxref=PMID:33558762 O15270 UniProtKB Sequence conflict 61 64 . . . Note=EAFE->TLAR;Ontology_term=ECO:0000305;evidence=ECO:0000305 O15270 UniProtKB Sequence conflict 436 562 . . . Note=KECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRHRLVPLLDRPFDETTYEETED->NGITIHEVVQTRNTYHRFSPLSPVFSHQCLWIMLP;Ontology_term=ECO:0000305;evidence=ECO:0000305 O15270 UniProtKB Beta strand 50 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6M4O O15270 UniProtKB Beta strand 54 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7CQI O15270 UniProtKB Helix 68 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 100 102 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7CQI O15270 UniProtKB Helix 106 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 109 111 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0J O15270 UniProtKB Helix 117 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 121 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 128 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 137 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7CQI O15270 UniProtKB Beta strand 143 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 154 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0N O15270 UniProtKB Beta strand 161 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 178 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7CQI O15270 UniProtKB Beta strand 184 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 187 199 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 204 206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0N O15270 UniProtKB Turn 207 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 214 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 229 236 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 238 249 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 255 259 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 264 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 275 280 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 285 298 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 300 303 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 310 318 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Turn 319 322 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 327 337 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 340 344 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Turn 346 351 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 352 356 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0N O15270 UniProtKB Helix 359 363 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 367 369 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 370 377 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Turn 378 381 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 386 390 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 392 401 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 403 407 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 413 426 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Turn 427 430 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 431 433 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0N O15270 UniProtKB Helix 434 456 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 462 465 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0M O15270 UniProtKB Beta strand 467 472 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Helix 476 488 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 494 496 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Turn 498 500 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Turn 503 505 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6M4O O15270 UniProtKB Beta strand 507 511 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K O15270 UniProtKB Beta strand 513 515 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7CQI O15270 UniProtKB Helix 518 535 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7K0K