##gff-version 3 Q9BTZ2 UniProtKB Chain 1 278 . . . ID=PRO_0000054647;Note=Dehydrogenase/reductase SDR family member 4 Q9BTZ2 UniProtKB Motif 276 278 . . . Note=Peroxisomal targeting signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WNV7 Q9BTZ2 UniProtKB Active site 182 182 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10001 Q9BTZ2 UniProtKB Binding site 36 60 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WNV7 Q9BTZ2 UniProtKB Binding site 169 169 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99714 Q9BTZ2 UniProtKB Binding site 186 186 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8WNV7 Q9BTZ2 UniProtKB Site 176 176 . . . Note=Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19056333;Dbxref=PMID:19056333 Q9BTZ2 UniProtKB Site 179 179 . . . Note=Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19056333;Dbxref=PMID:19056333 Q9BTZ2 UniProtKB Modified residue 92 92 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LB2 Q9BTZ2 UniProtKB Modified residue 92 92 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LB2 Q9BTZ2 UniProtKB Modified residue 105 105 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LB2 Q9BTZ2 UniProtKB Modified residue 216 216 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LB2 Q9BTZ2 UniProtKB Modified residue 216 216 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LB2 Q9BTZ2 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LB2 Q9BTZ2 UniProtKB Modified residue 227 227 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LB2 Q9BTZ2 UniProtKB Modified residue 234 234 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99LB2 Q9BTZ2 UniProtKB Alternative sequence 1 18 . . . ID=VSP_044947;Note=In isoform 8. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9BTZ2 UniProtKB Alternative sequence 19 221 . . . ID=VSP_031435;Note=In isoform 6. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17230527;Dbxref=PMID:17230527 Q9BTZ2 UniProtKB Alternative sequence 103 222 . . . ID=VSP_008585;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:10333503;Dbxref=PMID:10333503 Q9BTZ2 UniProtKB Alternative sequence 103 136 . . . ID=VSP_031436;Note=In isoform 4%2C isoform 5 and isoform 8. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17230527;Dbxref=PMID:17230527 Q9BTZ2 UniProtKB Alternative sequence 137 222 . . . ID=VSP_008586;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10333503,ECO:0000303|PubMed:15473316;Dbxref=PMID:10333503,PMID:15473316 Q9BTZ2 UniProtKB Alternative sequence 137 188 . . . ID=VSP_031437;Note=In isoform 7. TLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTA->RRLSGDRVFHSSLQSISSLDGQGKRGKHERNPADKKVRRARGLCWHRVFPVL;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.5 Q9BTZ2 UniProtKB Alternative sequence 178 222 . . . ID=VSP_031438;Note=In isoform 5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17230527;Dbxref=PMID:17230527 Q9BTZ2 UniProtKB Alternative sequence 189 278 . . . ID=VSP_031439;Note=In isoform 7. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.5 Q9BTZ2 UniProtKB Natural variant 31 31 . . . ID=VAR_057272;Note=A->T;Dbxref=dbSNP:rs1043442 Q9BTZ2 UniProtKB Natural variant 202 202 . . . ID=VAR_061846;Note=P->S;Dbxref=dbSNP:rs1043650 Q9BTZ2 UniProtKB Mutagenesis 176 176 . . . Note=Decreased reduction activity for benzil%2C isatin and retinal and increased activity for 5beta-Pregnane-3%2C20-dione and 5beta-Dihydrotestosterone. No change of stereoselectivity in 3-ketosteroids reduction and no change in 3beta-hydroxysteroid oxidation. Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3%2C20-dione%2C 5beta-Dihydrotestosterone%2C benzil and retinal%3B when associated with L-179. Change in stereoselective activity by the reduction of 5beta-Pregnane-3%2C20-dione predominantly to the 3alpha-hydroxysteroid%3B when associated with L-179. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation%3B when associated with L-179. Loss of cold catalytic inactivation%3B when associated with L-179 and N-195. Increased reduction activity for renital and oxidation activity for retinol%3B when associated with L-179 and N-195. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19056333;Dbxref=PMID:19056333 Q9BTZ2 UniProtKB Mutagenesis 179 179 . . . Note=Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3%2C20-dione%2C 5beta-Dihydrotestosterone%2C benzil and retinal%3B when associated with F-176. Change in stereoselective activity by the reduction of 5beta-Pregnane-3%2C20-dione predominantly to the 3alpha-hydroxysteroid%3B when associated with F-176. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation%3B when associated with F-176. Loss of cold catalytic inactivation%3B when associated with F-176 and N-195. Increased reduction activity for renital and oxidation activity for retinol%3B when associated with F-176 and N-195. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19056333;Dbxref=PMID:19056333 Q9BTZ2 UniProtKB Mutagenesis 195 195 . . . Note=Loss of cold catalytic inactivation. Loss of cold catalytic inactivation%3B when associated with F-176 and L-179. Switch in stereoselective activity from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation%3B when associated with F-176 and L-179. Increased reduction activity for renital and oxidation activity for retinol%3B when associated with F-176 and L-179. T->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18571493,ECO:0000269|PubMed:19056333;Dbxref=PMID:18571493,PMID:19056333 Q9BTZ2 UniProtKB Sequence conflict 37 37 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9BTZ2 UniProtKB Sequence conflict 50 50 . . . Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9BTZ2 UniProtKB Sequence conflict 89 89 . . . Note=H->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9BTZ2 UniProtKB Sequence conflict 102 102 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9BTZ2 UniProtKB Sequence conflict 126 126 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9BTZ2 UniProtKB Turn 29 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Beta strand 34 39 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 43 54 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Beta strand 58 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 66 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Beta strand 83 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 93 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Beta strand 112 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Turn 126 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 131 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 143 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Beta strand 162 167 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 170 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 180 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 201 203 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Beta strand 205 212 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 221 223 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 227 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 245 248 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 249 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Helix 258 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Beta strand 267 271 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3O4R Q9BTZ2 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648