DHCR7_RAT
ID DHCR7_RAT Reviewed; 471 AA.
AC Q9Z2Z8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=7-dehydrocholesterol reductase {ECO:0000303|PubMed:10329655};
DE Short=7-DHC reductase;
DE EC=1.3.1.21 {ECO:0000269|PubMed:10329655};
DE AltName: Full=Sterol Delta(7)-reductase {ECO:0000303|Ref.1};
GN Name=Dhcr7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Nishino H., Ishibashi T.;
RT "Transmembrane configuration of sterol delta 7-reductase as a potential
RT sterol sensing protein.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=10329655; DOI=10.1074/jbc.274.21.14624;
RA Bae S.-H., Lee J.N., Fitzky B.U., Seong J., Paik Y.-K.;
RT "Cholesterol biosynthesis from lanosterol. Molecular cloning, tissue
RT distribution, expression, chromosomal localization, and regulation of rat
RT 7-dehydrocholesterol reductase, a Smith-Lemli-Opitz syndrome-related
RT protein.";
RL J. Biol. Chem. 274:14624-14631(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=12031495; DOI=10.1016/s0167-4781(02)00285-3;
RA Lee J.-N., Bae S.-H., Paik Y.-K.;
RT "Structure and alternative splicing of the rat 7-dehydrocholesterol
RT reductase gene.";
RL Biochim. Biophys. Acta 1576:148-156(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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:0000269|PubMed:10329655}.
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:0000269|PubMed:10329655};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23986;
CC Evidence={ECO:0000305|PubMed:10329655};
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:0000269|PubMed:10329655}.
CC -!- SUBUNIT: Interacts with DHCR24; this interaction regulates DHCR7
CC activity. {ECO:0000250|UniProtKB:Q9UBM7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UBM7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highest expression is detected in liver, followed
CC by kidney and brain. {ECO:0000269|PubMed:10329655}.
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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DR EMBL; AB016800; BAA34306.1; -; mRNA.
DR EMBL; AF071500; AAD31383.1; -; mRNA.
DR EMBL; AF272393; AAM45144.1; -; mRNA.
DR EMBL; AF279892; AAK69490.1; -; Genomic_DNA.
DR EMBL; BC081688; AAH81688.1; -; mRNA.
DR RefSeq; NP_071784.1; NM_022389.2.
DR RefSeq; XP_006230954.1; XM_006230892.3.
DR RefSeq; XP_006230955.1; XM_006230893.3.
DR RefSeq; XP_006230956.1; XM_006230894.3.
DR RefSeq; XP_008758394.1; XM_008760172.2.
DR RefSeq; XP_008758395.1; XM_008760173.2.
DR AlphaFoldDB; Q9Z2Z8; -.
DR SMR; Q9Z2Z8; -.
DR STRING; 10116.ENSRNOP00000028194; -.
DR BindingDB; Q9Z2Z8; -.
DR ChEMBL; CHEMBL4965; -.
DR SwissPalm; Q9Z2Z8; -.
DR jPOST; Q9Z2Z8; -.
DR PaxDb; Q9Z2Z8; -.
DR PRIDE; Q9Z2Z8; -.
DR Ensembl; ENSRNOT00000028195; ENSRNOP00000028194; ENSRNOG00000020776.
DR GeneID; 64191; -.
DR KEGG; rno:64191; -.
DR UCSC; RGD:621769; rat.
DR CTD; 1717; -.
DR RGD; 621769; Dhcr7.
DR eggNOG; KOG1435; Eukaryota.
DR GeneTree; ENSGT00390000000417; -.
DR HOGENOM; CLU_015631_0_0_1; -.
DR InParanoid; Q9Z2Z8; -.
DR OMA; TSGFWGW; -.
DR OrthoDB; 532774at2759; -.
DR PhylomeDB; Q9Z2Z8; -.
DR TreeFam; TF101180; -.
DR BRENDA; 1.3.1.21; 5301.
DR Reactome; R-RNO-6807047; Cholesterol biosynthesis via desmosterol.
DR Reactome; R-RNO-6807062; Cholesterol biosynthesis via lathosterol.
DR UniPathway; UPA00063; -.
DR PRO; PR:Q9Z2Z8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020776; Expressed in ovary and 20 other tissues.
DR Genevisible; Q9Z2Z8; RN.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005640; C:nuclear outer membrane; ISO:RGD.
DR GO; GO:0047598; F:7-dehydrocholesterol reductase activity; IMP:RGD.
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:0009918; F:sterol delta7 reductase activity; IBA:GO_Central.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IDA:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IDA:RGD.
DR GO; GO:0016126; P:sterol biosynthetic process; ISO:RGD.
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 1: Evidence at protein 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..471
FT /note="7-dehydrocholesterol reductase"
FT /id="PRO_0000207504"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 354
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 358
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 391
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 396
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 403..404
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 443
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 447..451
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 458
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ SEQUENCE 471 AA; 54155 MW; EBF0CBC4F4222FDB CRC64;
MASKSQHNAS KAKNHNVKAE SQGQWGRAWE VDWFSLVSVI FLLLFAPFIV YYFIMACDQY
SCSLTAPILD VATGRASLAD IWAKTPPVTA KAAQLYALWV SFQVLLYSWL PDFCHRFLPG
YVGGVQEGAI TPAGIVNKYE VNGLQAWLIT HFLWFVNAYL LSWFSPTIIF DNWIPLLWCA
NILGYAVSTF AMIKGYLFPT SAEDCKFTGN FFYNYMMGIE FNPRIGKWFD FKLFFNGRPG
IVAWTLINLS FAAKQQELYG HVTNSMILVN VLQAIYVLDF FWNETWYLKT IDICHDHFGW
YLGWGDCVWL PYLYTLQGLY LVYHPVQLST PNALGVLLLG LVGYYIFRMT NHQKDLFRRT
DGHCLIWGKK PKAIECSYTS ADGLKHRSKL LVSGFWGVAR HFNYTGDLMG SLAYCLACGG
GHLLPYFYII YMTILLTHRC LRDEHRCANK YGRDWERYVA AVPYRLLPGI F
