DHCR7_DANRE
ID DHCR7_DANRE Reviewed; 478 AA.
AC Q7SXF1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-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}.
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DR EMBL; BC055631; AAH55631.1; -; mRNA.
DR RefSeq; NP_958487.1; NM_201330.1.
DR AlphaFoldDB; Q7SXF1; -.
DR SMR; Q7SXF1; -.
DR STRING; 7955.ENSDARP00000101967; -.
DR PaxDb; Q7SXF1; -.
DR GeneID; 378446; -.
DR KEGG; dre:378446; -.
DR CTD; 1717; -.
DR ZFIN; ZDB-GENE-030912-9; dhcr7.
DR eggNOG; KOG1435; Eukaryota.
DR InParanoid; Q7SXF1; -.
DR OrthoDB; 532774at2759; -.
DR PhylomeDB; Q7SXF1; -.
DR Reactome; R-DRE-6807047; Cholesterol biosynthesis via desmosterol.
DR Reactome; R-DRE-6807062; Cholesterol biosynthesis via lathosterol.
DR UniPathway; UPA00063; -.
DR PRO; PR:Q7SXF1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IDA:ZFIN.
DR GO; GO:0009918; F:sterol delta7 reductase activity; IBA:GO_Central.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001171; ERG24_DHCR-like.
DR InterPro; IPR018083; Sterol_reductase_CS.
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..478
FT /note="7-dehydrocholesterol reductase"
FT /id="PRO_0000207505"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 361
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 365
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 403
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 410..411
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 450
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 454..458
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 465
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ SEQUENCE 478 AA; 55189 MW; EFFDB76773E4ECD7 CRC64;
MMASDRVRKR HKGSANGAQT VEKEPSKEPA QWGRAWEVDW FSLSGVILLL CFAPFLVSFF
IMACDQYQCS ISHPLLDLYN GDATLFTIWN RAPSFTWAAA KIYAIWVTFQ VVLYMCVPDF
LHKILPGYVG GVQDGARTPA GLINKYEVNG LQCWLITHVL WVLNAQHFHW FSPTIIIDNW
IPLLWCTNIL GYAVSTFAFI KAYLFPTNPE DCKFTGNMFY NYMMGIEFNP RIGKWFDFKL
FFNGRPGIVA WTLINLSYAA KQQELYGYVT NSMILVNVLQ AVYVVDFFWN EAWYLKTIDI
CHDHFGWYLG WGDCVWLPFL YTLQGLYLVY NPIQLSTPHA AGVLILGLVG YYIFRVTNHQ
KDLFRRTEGN CSIWGKKPTF IECSYQSADG AIHKSKLMTS GFWGVARHMN YTGDLMGSLA
YCLACGGNHL LPYFYIIYMT ILLVHRCIRD EHRCSNKYGK DWERYTAAVS YRLLPNIF
