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   24-JAN-2024, entry version 149.
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. Interacts with TMEM147. {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   PhosphoSitePlus; Q9Z2Z8; -.
DR   SwissPalm; Q9Z2Z8; -.
DR   jPOST; Q9Z2Z8; -.
DR   PaxDb; 10116-ENSRNOP00000028194; -.
DR   Ensembl; ENSRNOT00000028195.6; ENSRNOP00000028194.2; ENSRNOG00000020776.6.
DR   GeneID; 64191; -.
DR   KEGG; rno:64191; -.
DR   UCSC; RGD:621769; rat.
DR   AGR; RGD:621769; -.
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   OrthoDB; 275939at2759; -.
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 cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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: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:0006695; P:cholesterol biosynthetic process; IDA:RGD.
DR   GO; GO:0030324; P:lung development; ISO:RGD.
DR   GO; GO:0060487; P:lung epithelial cell differentiation; 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   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.
DR   Genevisible; Q9Z2Z8; RN.
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
//