[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C57BL/6J; DOI=10.1073/pnas.95.14.8181; PubMed=9653161 [NCBI, ExPASy, EBI, Israel, Japan] Fitzky B.U., Witsch-Baumgartner M., Erdel M., Lee J.N., Paik Y.-K., Glossmann H., Utermann G., Moebius F.F.; "Mutations in the delta7-sterol reductase gene in patients with the Smith-Lemli-Opitz syndrome."; Proc. Natl. Acad. Sci. U.S.A. 95:8181-8186(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC).
CATALYTIC ACTIVITY: Cholesterol + NADP⁺ = cholesta-5,7-dien-3-beta-ol + NADPH.
PATHWAY: Steroid biosynthesis; cholesterol biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.
SIMILARITY: Belongs to the ERG4/ERG24 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF057368; AAC40164.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006854; AAH06854.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_031882.1; -.

UniGene

Mm.249342

3D structure databases

ModBase

O88455.

PTM databases

PhosphoSite

O88455; -.

Organism-specific databases

MGI

MGI:1298378; Dhcr7.

Gene expression databases

ArrayExpress

O88455; -.

CleanEx

MM_DHCR7; -.

GermOnline

ENSMUSG00000058454; Mus musculus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0047598;	Molecular function: 7-dehydrocholesterol reductase activity (inferred from direct assay from MGI).
GO:0001568;	Biological process: blood vessel development (inferred from mutant phenotype from MGI).
GO:0030154;	Biological process: cell differentiation (inferred from mutant phenotype from MGI).
GO:0006695;	Biological process: cholesterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0030324;	Biological process: lung development (inferred from mutant phenotype from MGI).
GO:0035264;	Biological process: multicellular organism growth (inferred from mutant phenotype from MGI).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009791;	Biological process: post-embryonic development (inferred from mutant phenotype from MGI).
GO:0042127;	Biological process: regulation of cell proliferation (inferred from mutant phenotype from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001171; ERG4_ERG24.
Graphical view of domain structure.

Pfam

PF01222; ERG4_ERG24; 1.
Pfam graphical view of domain structure.

PROSITE

PS01017; STEROL_REDUCT_1; 1.
PS01018; STEROL_REDUCT_2; 1.

Proteomics databases

PRIDE

O88455; -.

Genome annotation databases

Ensembl

ENSMUSG00000058454; Mus musculus. [Contig view]

GeneID

13360; -.

KEGG

mmu:13360; -.

Phylogenomic databases

HOGENOM

O88455; -.

HOVERGEN

O88455; -.

Other

283692; -.

Dhcr7; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cholesterol biosynthesis; Endoplasmic reticulum; Lipid synthesis; Membrane; NADP; Oxidoreductase; Phosphoprotein; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 471`	`471`	`7-dehydrocholesterol reductase.`	`PRO_0000207503`
`TRANSMEM`	`36 56`	`21`	`Potential.`
`TRANSMEM`	`95 115`	`21`	`Potential.`
`TRANSMEM`	`144 164`	`21`	`Potential.`
`TRANSMEM`	`173 193`	`21`	`Potential.`
`TRANSMEM`	`233 253`	`21`	`Potential.`
`TRANSMEM`	`262 282`	`21`	`Potential.`
`TRANSMEM`	`302 322`	`21`	`Potential.`
`TRANSMEM`	`327 347`	`21`	`Potential.`
`TRANSMEM`	`416 436`	`21`	`Potential.`
`MOD_RES`	`14 14`		`Phosphoserine (By similarity).`

Sequence information

Length: 471 AA [This is the length of the unprocessed precursor]

Molecular weight: 53919 Da [This is the MW of the unprocessed precursor]

CRC64: 6B1BC356CC539290 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASKSQHNAP KVKSPNGKAG SQGQWGRAWE VDWFSLASII FLLLFAPFIV YYFIMACDQY 

        70         80         90        100        110        120 
SCSLTAPALD IATGHASLAD IWAKTPPVTA KAAQLYALWV SFQVLLYSWL PDFCHRFLPG 

       130        140        150        160        170        180 
YVGGVQEGAI TPAGVVNKYE VNGLQAWLIT HILWFVNAYL LSWFSPTIIF DNWIPLLWCA 

       190        200        210        220        230        240 
NILGYAVSTF AMIKGYLFPT SAEDCKFTGN FFYNYMMGIE FNPRIGKWFD FKLFFNGRPG 

       250        260        270        280        290        300 
IVAWTLINLS FAAKQQELYG HVTNSMILVN VLQAIYVLDF FWNETWYLKT IDICHDHFGW 

       310        320        330        340        350        360 
YLGWGDCVWL PYLYTLQGLY LVYHPVQLST PNALGILLLG LVGYYIFRMT NHQKDLFRRT 

       370        380        390        400        410        420 
DGRCLIWGKK PKAIECSYTS ADGLKHHSKL LVSGFWGVAR HFNYTGDLMG SLAYCLACGG 

       430        440        450        460        470 
GHLLPYFYII YMTILLTHRC LRDEHRCANK YGRDWERYTA AVPYRLLPGI F

O88455 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools