ID DHCR7_XENLA Reviewed; 473 AA. AC Q7ZXH1; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=7-dehydrocholesterol reductase; DE Short=7-DHC reductase; DE EC=1.3.1.21 {ECO:0000250|UniProtKB:O88455}; DE AltName: Full=Sterol Delta(7)-reductase; GN Name=dhcr7; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: 7-dehydrocholesterol reductase of the cholesterol CC biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7- CC dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien- CC 3beta-ol, two intermediates in that pathway. CC {ECO:0000250|UniProtKB:Q9UBM7}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH; CC Xref=Rhea:RHEA:23984, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, CC ChEBI:CHEBI:17759, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.21; CC Evidence={ECO:0000250|UniProtKB:Q9UBM7}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23986; CC Evidence={ECO:0000250|UniProtKB:Q9UBM7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=7-dehydrodesmosterol + H(+) + NADPH = desmosterol + NADP(+); CC Xref=Rhea:RHEA:46740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17737, CC ChEBI:CHEBI:27910, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC Evidence={ECO:0000250|UniProtKB:O88455}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46741; CC Evidence={ECO:0000250|UniProtKB:O88455}; CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. CC {ECO:0000250|UniProtKB:O88455}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9UBM7}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC044995; AAH44995.1; -; mRNA. DR RefSeq; NP_001079586.1; NM_001086117.1. DR RefSeq; XP_018114839.1; XM_018259350.1. DR AlphaFoldDB; Q7ZXH1; -. DR SMR; Q7ZXH1; -. DR DNASU; 379273; -. DR GeneID; 379273; -. DR KEGG; xla:379273; -. DR AGR; Xenbase:XB-GENE-17334842; -. DR CTD; 379273; -. DR Xenbase; XB-GENE-17334842; dhcr7.S. DR OMA; CWGIVRH; -. DR OrthoDB; 275939at2759; -. DR UniPathway; UPA00063; -. DR Proteomes; UP000186698; Chromosome 4S. DR Bgee; 379273; Expressed in neurula embryo and 19 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.120.1630; -; 1. DR InterPro; IPR001171; ERG24_DHCR-like. DR InterPro; IPR018083; Sterol_reductase_CS. DR PANTHER; PTHR21257:SF38; 7-DEHYDROCHOLESTEROL REDUCTASE; 1. DR PANTHER; PTHR21257; DELTA(14)-STEROL REDUCTASE; 1. DR Pfam; PF01222; ERG4_ERG24; 1. DR PROSITE; PS01017; STEROL_REDUCT_1; 1. DR PROSITE; PS01018; STEROL_REDUCT_2; 1. PE 2: Evidence at transcript level; KW Cholesterol biosynthesis; Cholesterol metabolism; Endoplasmic reticulum; KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase; KW Reference proteome; Steroid biosynthesis; Steroid metabolism; KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix. FT CHAIN 1..473 FT /note="7-dehydrocholesterol reductase" FT /id="PRO_0000207506" FT TRANSMEM 36..56 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 97..117 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 175..195 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 264..284 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 304..324 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 329..349 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 419..439 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 356 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 360 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 393 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 398 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 405..406 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 445 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 449..453 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:G4SW86" FT BINDING 460 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:G4SW86" SQ SEQUENCE 473 AA; 54823 MW; 8EB14E8186BDC463 CRC64; MGERRRANAS RGDKKVANGE KQHVGQWGRA WEVDYFSLAS VIFLLAFAPL IVYYFVMSCD QYQCALTAPV LDLYSGKARL SDIWDKTPAL TWTAVKIYLA WVSFQVFLYM FLPDILHKFV PGYEGGVQEG ARTPAGLINK YQVNGLQAWT ITHLLWFANA YHFHWFSPTI VIDNWIPLLW CANLLGYSVA TFALVKANFF PTNANDCKFT GNFFYDYMMG IEFNPRIGKW FDFKLFFNGR PGIVAWTLIN LSYAAKQQEL YGQVTNSMIL VNVLQAIYVV DFFWNESWYL KTIDICHDHF GWYLGWGDCV WLPYLYTLQG LYLVYNPVEL STTAAVAVLL LGLIGYYIFR MTNHQKDLFR RTNGNCKIWG KKPKSIECFY VSADGKRHYS KLMISGFWGV ARHLNYTGDL MGSLAYCLAC GFDHLLPYFY FIYMTILLVH RCIRDEHRCS SKYGKDWKLY TSAVPYRLLP GLF //