##gff-version 3 Q15125 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25944712;Dbxref=PMID:25944712 Q15125 UniProtKB Chain 2 230 . . . ID=PRO_0000174342;Note=3-beta-hydroxysteroid-Delta(8)%2CDelta(7)-isomerase Q15125 UniProtKB Transmembrane 29 49 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q15125 UniProtKB Transmembrane 66 86 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q15125 UniProtKB Transmembrane 121 141 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q15125 UniProtKB Transmembrane 185 205 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q15125 UniProtKB Domain 61 204 . . . Note=EXPERA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01087 Q15125 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25944712;Dbxref=PMID:25944712 Q15125 UniProtKB Natural variant 18 18 . . . ID=VAR_074633;Note=In MEND%3B patients have mildly increased concentrations of plasma 8(9)-cholestenol and 8-dehydrocholesterol%3B probable hypomorphic mutation. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12503101;Dbxref=dbSNP:rs104894795,PMID:12503101 Q15125 UniProtKB Natural variant 47 47 . . . ID=VAR_074634;Note=In MEND%3B patients have increased concentrations of plasma 8(9)-cholestenol%2C 8-dehydrocholesterol and 7-dehydrocholesterol%3B probable hypomorphic mutation. W->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20949533;Dbxref=dbSNP:rs587783599,PMID:20949533 Q15125 UniProtKB Natural variant 47 47 . . . ID=VAR_074635;Note=In MEND%3B patients have increased concentrations of plasma 8-dehydrocholesterol and 8(9)-cholestenol%3B probable hypomorphic mutation. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24459067;Dbxref=dbSNP:rs878854359,PMID:24459067 Q15125 UniProtKB Natural variant 75 75 . . . ID=VAR_074636;Note=In MEND%3B patients have increased plasma levels of 8(9)-cholestenol%3B probable hypomorphic mutation. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24700572;Dbxref=dbSNP:rs797045153,PMID:24700572 Q15125 UniProtKB Natural variant 80 80 . . . ID=VAR_012105;Note=In CDPX2. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10391219;Dbxref=dbSNP:rs104894800,PMID:10391219 Q15125 UniProtKB Natural variant 103 103 . . . ID=VAR_074637;Note=In CDPX2. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18176751;Dbxref=PMID:18176751 Q15125 UniProtKB Natural variant 110 110 . . . ID=VAR_012106;Note=In CDPX2. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10391218;Dbxref=dbSNP:rs1602090481,PMID:10391218 Q15125 UniProtKB Natural variant 147 147 . . . ID=VAR_012107;Note=In CDPX2. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11493318;Dbxref=PMID:11493318 Q15125 UniProtKB Natural variant 147 147 . . . ID=VAR_012108;Note=In CDPX2. R->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10391219,ECO:0000269|PubMed:10942423,ECO:0000269|PubMed:25814754;Dbxref=dbSNP:rs28935174,PMID:10391219,PMID:10942423,PMID:25814754 Q15125 UniProtKB Mutagenesis 68 68 . . . Note=Reduces catalytic activity to less than 35%25 of wild-type. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9894009;Dbxref=PMID:9894009 Q15125 UniProtKB Mutagenesis 75 75 . . . Note=Reduces catalytic activity to less than 35%25 of wild-type. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9894009;Dbxref=PMID:9894009 Q15125 UniProtKB Mutagenesis 76 76 . . . Note=Reduces catalytic activity to less than 10%25 of wild-type. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9894009;Dbxref=PMID:9894009 Q15125 UniProtKB Mutagenesis 80 80 . . . Note=Reduces catalytic activity to less than 10%25 of wild-type. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9894009;Dbxref=PMID:9894009 Q15125 UniProtKB Mutagenesis 111 111 . . . Note=Reduces catalytic activity to less than 2%25 of wild-type. Y->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12760743;Dbxref=PMID:12760743 Q15125 UniProtKB Mutagenesis 121 121 . . . Note=Reduces catalytic activity to less than 35%25 of wild-type. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12760743;Dbxref=PMID:12760743 Q15125 UniProtKB Mutagenesis 121 121 . . . Note=No effect on catalytic activity. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12760743;Dbxref=PMID:12760743 Q15125 UniProtKB Mutagenesis 122 122 . . . Note=Reduces catalytic activity to less than 10%25 of wild-type. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9894009;Dbxref=PMID:9894009 Q15125 UniProtKB Mutagenesis 125 125 . . . Note=Reduces catalytic activity to less than 10%25 of wild-type. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9894009;Dbxref=PMID:9894009 Q15125 UniProtKB Mutagenesis 188 188 . . . Note=Reduces catalytic activity to less than 35%25 of wild-type. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9894009;Dbxref=PMID:9894009 Q15125 UniProtKB Mutagenesis 189 189 . . . Note=Reduces catalytic activity to less than 35%25 of wild-type. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12760743;Dbxref=PMID:12760743 Q15125 UniProtKB Mutagenesis 189 189 . . . Note=No effect on catalytic activity. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12760743;Dbxref=PMID:12760743 Q15125 UniProtKB Mutagenesis 193 193 . . . Note=Reduces catalytic activity to less than 10%25 of wild-type. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9894009;Dbxref=PMID:9894009 Q15125 UniProtKB Mutagenesis 196 196 . . . Note=Reduces catalytic activity to less than 10%25 of wild-type. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9894009;Dbxref=PMID:9894009 Q15125 UniProtKB Sequence conflict 187 188 . . . Note=FY->IF;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q15125 UniProtKB Helix 28 51 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Helix 61 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Helix 96 106 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Turn 111 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Helix 116 127 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Helix 129 139 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Turn 140 143 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Helix 146 171 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Turn 172 174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Helix 182 189 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT Q15125 UniProtKB Helix 190 215 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OHT