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Protein

7-dehydrocholesterol reductase

Gene

Dhcr7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC).

Catalytic activityi

Cholesterol + NADP+ = cholesta-5,7-dien-3-beta-ol + NADPH.

Pathwayi

GO - Molecular functioni

  1. 7-dehydrocholesterol reductase activity Source: RGD

GO - Biological processi

  1. blood vessel development Source: Ensembl
  2. cell differentiation Source: Ensembl
  3. cholesterol biosynthetic process Source: RGD
  4. lung development Source: Ensembl
  5. multicellular organism growth Source: Ensembl
  6. post-embryonic development Source: Ensembl
  7. regulation of cell proliferation Source: Ensembl
  8. regulation of cholesterol biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.3.1.21. 5301.
ReactomeiREACT_198613. Activation of gene expression by SREBF (SREBP).
REACT_238041. Cholesterol biosynthesis.
UniPathwayiUPA00063.

Names & Taxonomyi

Protein namesi
Recommended name:
7-dehydrocholesterol reductase (EC:1.3.1.21)
Short name:
7-DHC reductase
Alternative name(s):
Sterol Delta(7)-reductase
Gene namesi
Name:Dhcr7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi621769. Dhcr7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei36 – 5621HelicalSequence AnalysisAdd
BLAST
Transmembranei95 – 11521HelicalSequence AnalysisAdd
BLAST
Transmembranei144 – 16421HelicalSequence AnalysisAdd
BLAST
Transmembranei173 – 19321HelicalSequence AnalysisAdd
BLAST
Transmembranei233 – 25321HelicalSequence AnalysisAdd
BLAST
Transmembranei262 – 28221HelicalSequence AnalysisAdd
BLAST
Transmembranei302 – 32221HelicalSequence AnalysisAdd
BLAST
Transmembranei327 – 34721HelicalSequence AnalysisAdd
BLAST
Transmembranei416 – 43621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. intracellular membrane-bounded organelle Source: RGD
  4. nuclear outer membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4714717-dehydrocholesterol reductasePRO_0000207504Add
BLAST

Proteomic databases

PaxDbiQ9Z2Z8.
PRIDEiQ9Z2Z8.

Expressioni

Gene expression databases

GenevestigatoriQ9Z2Z8.

Interactioni

Protein-protein interaction databases

MINTiMINT-4580360.
STRINGi10116.ENSRNOP00000028194.

Family & Domainsi

Sequence similaritiesi

Belongs to the ERG4/ERG24 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG72042.
GeneTreeiENSGT00390000000417.
HOGENOMiHOG000193296.
HOVERGENiHBG007825.
InParanoidiQ9Z2Z8.
KOiK00213.
OMAiALWFANA.
OrthoDBiEOG75B85C.
PhylomeDBiQ9Z2Z8.
TreeFamiTF101180.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z2Z8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKSQHNAS KAKNHNVKAE SQGQWGRAWE VDWFSLVSVI FLLLFAPFIV
60 70 80 90 100
YYFIMACDQY SCSLTAPILD VATGRASLAD IWAKTPPVTA KAAQLYALWV
110 120 130 140 150
SFQVLLYSWL PDFCHRFLPG YVGGVQEGAI TPAGIVNKYE VNGLQAWLIT
160 170 180 190 200
HFLWFVNAYL LSWFSPTIIF DNWIPLLWCA NILGYAVSTF AMIKGYLFPT
210 220 230 240 250
SAEDCKFTGN FFYNYMMGIE FNPRIGKWFD FKLFFNGRPG IVAWTLINLS
260 270 280 290 300
FAAKQQELYG HVTNSMILVN VLQAIYVLDF FWNETWYLKT IDICHDHFGW
310 320 330 340 350
YLGWGDCVWL PYLYTLQGLY LVYHPVQLST PNALGVLLLG LVGYYIFRMT
360 370 380 390 400
NHQKDLFRRT DGHCLIWGKK PKAIECSYTS ADGLKHRSKL LVSGFWGVAR
410 420 430 440 450
HFNYTGDLMG SLAYCLACGG GHLLPYFYII YMTILLTHRC LRDEHRCANK
460 470
YGRDWERYVA AVPYRLLPGI F
Length:471
Mass (Da):54,155
Last modified:May 1, 1999 - v1
Checksum:iEBF0CBC4F4222FDB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016800 mRNA. Translation: BAA34306.1.
AF071500 mRNA. Translation: AAD31383.1.
AF272393 mRNA. Translation: AAM45144.1.
AF279892 Genomic DNA. Translation: AAK69490.1.
BC081688 mRNA. Translation: AAH81688.1.
RefSeqiNP_071784.1. NM_022389.2.
XP_006230954.1. XM_006230892.2.
XP_006230955.1. XM_006230893.2.
XP_006230956.1. XM_006230894.2.
XP_008758393.1. XM_008760171.1.
XP_008758394.1. XM_008760172.1.
XP_008758395.1. XM_008760173.1.
UniGeneiRn.228.

Genome annotation databases

EnsembliENSRNOT00000028195; ENSRNOP00000028194; ENSRNOG00000020776.
GeneIDi64191.
KEGGirno:64191.
UCSCiRGD:621769. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016800 mRNA. Translation: BAA34306.1.
AF071500 mRNA. Translation: AAD31383.1.
AF272393 mRNA. Translation: AAM45144.1.
AF279892 Genomic DNA. Translation: AAK69490.1.
BC081688 mRNA. Translation: AAH81688.1.
RefSeqiNP_071784.1. NM_022389.2.
XP_006230954.1. XM_006230892.2.
XP_006230955.1. XM_006230893.2.
XP_006230956.1. XM_006230894.2.
XP_008758393.1. XM_008760171.1.
XP_008758394.1. XM_008760172.1.
XP_008758395.1. XM_008760173.1.
UniGeneiRn.228.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4580360.
STRINGi10116.ENSRNOP00000028194.

Chemistry

BindingDBiQ9Z2Z8.
ChEMBLiCHEMBL4965.

Proteomic databases

PaxDbiQ9Z2Z8.
PRIDEiQ9Z2Z8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028195; ENSRNOP00000028194; ENSRNOG00000020776.
GeneIDi64191.
KEGGirno:64191.
UCSCiRGD:621769. rat.

Organism-specific databases

CTDi1717.
RGDi621769. Dhcr7.

Phylogenomic databases

eggNOGiNOG72042.
GeneTreeiENSGT00390000000417.
HOGENOMiHOG000193296.
HOVERGENiHBG007825.
InParanoidiQ9Z2Z8.
KOiK00213.
OMAiALWFANA.
OrthoDBiEOG75B85C.
PhylomeDBiQ9Z2Z8.
TreeFamiTF101180.

Enzyme and pathway databases

UniPathwayiUPA00063.
BRENDAi1.3.1.21. 5301.
ReactomeiREACT_198613. Activation of gene expression by SREBF (SREBP).
REACT_238041. Cholesterol biosynthesis.

Miscellaneous databases

NextBioi612852.
PROiQ9Z2Z8.

Gene expression databases

GenevestigatoriQ9Z2Z8.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Transmembrane configuration of sterol delta 7-reductase as a potential sterol sensing protein."
    Nishino H., Ishibashi T.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Cholesterol biosynthesis from lanosterol. Molecular cloning, tissue distribution, expression, chromosomal localization, and regulation of rat 7-dehydrocholesterol reductase, a Smith-Lemli-Opitz syndrome-related protein."
    Bae S.-H., Lee J.N., Fitzky B.U., Seong J., Paik Y.-K.
    J. Biol. Chem. 274:14624-14631(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  3. "Structure and alternative splicing of the rat 7-dehydrocholesterol reductase gene."
    Lee J.-N., Bae S.-H., Paik Y.-K.
    Biochim. Biophys. Acta 1576:148-156(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiDHCR7_RAT
AccessioniPrimary (citable) accession number: Q9Z2Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.