[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SLOS LEU-119; ARG-244 AND CYS-248. DOI=10.1086/301982; PubMed=9683613 [NCBI, ExPASy, EBI, Israel, Japan] Waterham H.R., Wijburg F.A., Hennekam R.C.M., Vreken P., Poll-The B.T., Dorland L., Duran M., Jira P.E., Smeitink J.A.M., Wevers R.A., Wanders R.J.A.; "Smith-Lemli-Opitz syndrome is caused by mutations in the 7-dehydrocholesterol reductase gene."; Am. J. Hum. Genet. 63:329-338(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. TISSUE=Liver; DOI=10.1073/pnas.95.4.1899; PubMed=9465114 [NCBI, ExPASy, EBI, Israel, Japan] Moebius F.F., Fitzky B.U., Lee J.N., Paik Y.K., Glossmann H.; "Molecular cloning and expression of the human delta7-sterol reductase."; Proc. Natl. Acad. Sci. U.S.A. 95:1899-1902(1998).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1006/geno.1998.5615; PubMed=9878250 [NCBI, ExPASy, EBI, Israel, Japan] Holmer L., Pezhman A., Worman H.J.; "The human lamin B receptor/sterol reductase multigene family."; Genomics 54:469-476(1998).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; 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).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 14-475. TISSUE=Liver; DOI=10.1086/301936; PubMed=9634533 [NCBI, ExPASy, EBI, Israel, Japan] Wassif C.A., Maslen C., Kachilele-Linjewile S., Lin D., Linck L.M., Conner W.E., Steiner R.D., Porter F.D.; "Mutations in the human sterol delta 7-reductase gene at 11q12-13 cause Smith-Lemli-Opitz syndrome."; Am. J. Hum. Genet. 63:55-62(1998).
[6]	VARIANTS SLOS SER-51; MET-93; PRO-99; PRO-157; VAL-247; LEU-326; TRP-352; SER-380; CYS-404 AND SER-410. 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).
[7]	VARIANTS SLOS SER-51; MET-93; PRO-99; HIS-107; PRO-109; ASP-147; MET-154; PRO-157; LEU-169; CYS-182; CYS-242; VAL-247; MET-281; ILE-289; GLY-311; TYR-311; HIS-324; LEU-326; GLN-352; TRP-352; ALA-353; CYS-362; TYR-380; ARG-380; SER-380; LEU-397; CYS-404; SER-404; HIS-408; SER-410; ARG-410; CYS-443; GLN-446; GLN-448; LYS-448 AND LEU-450. DOI=10.1086/302760; PubMed=10677299 [NCBI, ExPASy, EBI, Israel, Japan] Witsch-Baumgartner M., Fitzky B.U., Ogorelkova M., Kraft H.G., Moebius F.F., Glossmann H., Seedorf U., Gillessen-Kaesbach G., Hoffmann G.F., Clayton P., Kelley R.I., Utermann G.; "Mutational spectrum in the Delta7-sterol reductase gene and genotype-phenotype correlation in 84 patients with Smith-Lemli-Opitz syndrome."; Am. J. Hum. Genet. 66:402-412(2000).
[8]	VARIANT SLOS ILE-289. DOI=10.1002/1096-8628(20000918)94:3<214::AID-AJMG7>3.3.CO;2-I; PubMed=10995508 [NCBI, ExPASy, EBI, Israel, Japan] Krakowiak P.A., Nwokoro N.A., Wassif C.A., Battaile K.P., Nowaczyk M.J.M., Connor W.E., Maslen C., Steiner R.D., Porter F.D.; "Mutation analysis and description of sixteen RSH/Smith-Lemli-Opitz syndrome patients: polymerase chain reaction-based assays to simplify genotyping."; Am. J. Med. Genet. 94:214-227(2000).
[9]	VARIANTS SLOS MET-93; PRO-109; LEU-119; MET-154; LEU-182; TYR-183; GLU-198; HIS-242; ARG-244; CYS-248 AND LEU-255. DOI=10.1017/S0003480001008600; PubMed=11427181 [NCBI, ExPASy, EBI, Israel, Japan] Jira P.E., Wanders R.J.A., Smeitink J.A.M., De Jong J., Wevers R.A., Oostheim W., Tuerlings J.H.A.M., Hennekam R.C.M., Sengers R.C.A., Waterham H.R.; "Novel mutations in the 7-dehydrocholesterol reductase gene of 13 patients with Smith-Lemli-Opitz syndrome."; Ann. Hum. Genet. 65:229-236(2001).
[10]	VARIANTS SLOS MET-93; LEU-326; TRP-352 AND CYS-404. DOI=10.1038/sj.ejhg.5200579; PubMed=11175299 [NCBI, ExPASy, EBI, Israel, Japan] Witsch-Baumgartner M., Ciara E., Loffler J., Menzel H.J., Seedorf U., Burn J., Gillessen-Kaesbach G., Hoffmann G.F., Fitzky B.U., Mundy H., Clayton P., Kelley R.I., Krajewska-Walasek M., Utermann G.; "Frequency gradients of DHCR7 mutations in patients with Smith-Lemli-Opitz syndrome in Europe: evidence for different origins of common mutations."; Eur. J. Hum. Genet. 9:45-50(2001).
[11]	VARIANT SLOS LYS-448. DOI=10.1002/ajmg.a.20207; PubMed=12949967 [NCBI, ExPASy, EBI, Israel, Japan] Langius F.A., Waterham H.R., Romeijn G.J., Oostheim W., de Barse M.M., Dorland L., Duran M., Beemer F.A., Wanders R.J., Poll-The B.T.; "Identification of three patients with a very mild form of Smith-Lemli-Opitz syndrome."; Am. J. Med. Genet. A 122:24-29(2003).
[12]	VARIANTS SLOS PRO-68; CYS-113; VAL-138; LEU-145; SER-235; CYS-242; THR-297; ARG-344; CYS-404; TYR-405; HIS-408 AND PRO-426. DOI=10.1002/humu.9346; PubMed=15954111 [NCBI, ExPASy, EBI, Israel, Japan] Waye J.S., Krakowiak P.A., Wassif C.A., Sterner A.L., Eng B., Nakamura L.M., Nowaczyk M.J.M., Porter F.D.; "Identification of nine novel DHCR7 missense mutations in patients with Smith-Lemli-Opitz syndrome (SLOS)."; Hum. Mutat. 26:59-59(2005).

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 metabolism; cholesterol biosynthesis .
INTERACTION:
O60427:DKFZp762M2311; NbExp=1; IntAct=EBI-1054468, EBI-1055473;
Q99608:NDN; NbExp=1; IntAct=EBI-1054468, EBI-718177;
O14656:TOR1A; NbExp=1; IntAct=EBI-1054468, EBI-524257;
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.
TISSUE SPECIFICITY: Most abundant in adrenal gland, liver, testis, and brain.
DISEASE: Defects in DHCR7 are the cause of Smith-Lemli-Opitz syndrome (SLOS) [MIM:270400]; also known as SLO syndrome or RSH syndrome. SLOS is an autosomal recessive frequent inborn disorder of sterol metabolism with characteristic congenital malformations and dysmorphias. All patients suffer from mental retardation. Children with SLOS have elevated serum 7-dehydrocholesterol (7-DHC) levels and low serum cholesterol levels. SLOS occurs in relatively high frequency: approximately 1 in 20,000 to 30,000 births in populations of northern and central European background. Historically, a clinical distinction often was made between classic ("type I") SLOS and the more severely affected ("type II") patients. There is, in reality, a clinical and biochemical continuum from mild to severe SLOS.
SIMILARITY: Belongs to the ERG4/ERG24 family.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=DHCR7";.

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

AF096305; AAD09766.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF034544; AAC05086.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF110060; AAD24762.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF067127; AAD02816.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000054; AAH00054.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF062481; AAC18345.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001351.2; -.

UniGene

Hs.503134

3D structure databases

ModBase

Q9UBM7.

Protein-protein interaction databases

IntAct

Q9UBM7; -.

PTM databases

PhosphoSite

Q9UBM7; -.

Enzyme and pathway databases

Reactome

REACT_602; Lipid and lipoprotein metabolism.

Organism-specific databases

HGNC:2860; DHCR7.

270400; phenotype. [NCBI / EBI]
602858; gene. [NCBI / EBI]

Orphanet

818; Smith-Lemli-Opitz syndrome.

PharmGKB

PA27321; -.

GeneCards

Q9UBM7.

Gene expression databases

ArrayExpress

Q9UBM7; -.

CleanEx

HS_DHCR7; -.

GermOnline

ENSG00000172893; Homo sapiens.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from experiment from Reactome).
GO:0005640;	Cellular component: nuclear outer membrane (inferred from direct assay from UniProtKB).
GO:0047598;	Molecular function: 7-dehydrocholesterol reductase activity (inferred from direct assay from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006695;	Biological process: cholesterol biosynthetic process (inferred from mutant phenotype from UniProtKB).
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.

BLOCKS

Q9UBM7.

Proteomic databases

PeptideAtlas

Q9UBM7; -.

Genome annotation databases

Ensembl

ENSG00000172893; Homo sapiens. [Contig view]

GeneID

1717; -.

KEGG

hsa:1717; -.

Phylogenomic databases

HOGENOM

Q9UBM7; -.

HOVERGEN

Q9UBM7; -.

Other

DB00157; NADH.

DHCR7; Homo sapiens.

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 475`	`475`	`7-dehydrocholesterol reductase.`	`PRO_0000207502`
`TRANSMEM`	`40 60`	`21`	`Potential.`
`TRANSMEM`	`154 174`	`21`	`Potential.`
`TRANSMEM`	`177 197`	`21`	`Potential.`
`TRANSMEM`	`266 286`	`21`	`Potential.`
`TRANSMEM`	`306 326`	`21`	`Potential.`
`TRANSMEM`	`331 351`	`21`	`Potential.`
`TRANSMEM`	`420 440`	`21`	`Potential.`
`VARIANT`	`51 51`	`1`	`P -> S (in SLOS).`	`VAR_012717`
`VARIANT`	`68 68`	`1`	`L -> P (in SLOS).`	`VAR_023148`
`VARIANT`	`93 93`	`1`	`T -> M (in SLOS).`	`VAR_012718`
`VARIANT`	`99 99`	`1`	`L -> P (in SLOS).`	`VAR_012719`
`VARIANT`	`107 107`	`1`	`Q -> H (in SLOS).`	`VAR_023149`
`VARIANT`	`109 109`	`1`	`L -> P (in SLOS).`	`VAR_023150`
`VARIANT`	`113 113`	`1`	`S -> C (in SLOS).`	`VAR_023151`
`VARIANT`	`119 119`	`1`	`H -> L (in SLOS).`	`VAR_012720`
`VARIANT`	`138 138`	`1`	`G -> V (in SLOS).`	`VAR_023152`
`VARIANT`	`145 145`	`1`	`I -> L (in SLOS).`	`VAR_023153`
`VARIANT`	`147 147`	`1`	`G -> D (in SLOS).`	`VAR_023154`
`VARIANT`	`154 154`	`1`	`T -> M (in SLOS).`	`VAR_023155`
`VARIANT`	`157 157`	`1`	`L -> P (in SLOS).`	`VAR_012721`
`VARIANT`	`169 169`	`1`	`S -> L (in SLOS).`	`VAR_023156`
`VARIANT`	`182 182`	`1`	`W -> C (in SLOS).`	`VAR_023157`
`VARIANT`	`182 182`	`1`	`W -> L (in SLOS).`	`VAR_023158`
`VARIANT`	`183 183`	`1`	`C -> Y (in SLOS).`	`VAR_023159`
`VARIANT`	`198 198`	`1`	`K -> E (in SLOS).`	`VAR_023160`
`VARIANT`	`235 235`	`1`	`F -> S (in SLOS).`	`VAR_023161`
`VARIANT`	`242 242`	`1`	`R -> C (in SLOS).`	`VAR_023162`
`VARIANT`	`242 242`	`1`	`R -> H (in SLOS).`	`VAR_023163`
`VARIANT`	`244 244`	`1`	`G -> R (in SLOS).`	`VAR_012722`
`VARIANT`	`247 247`	`1`	`A -> V (in SLOS).`	`VAR_012723`
`VARIANT`	`248 248`	`1`	`W -> C (in SLOS).`	`VAR_012724`
`VARIANT`	`255 255`	`1`	`F -> L (in SLOS).`	`VAR_023164`
`VARIANT`	`281 281`	`1`	`V -> M (in SLOS).`	`VAR_023165`
`VARIANT`	`289 289`	`1`	`T -> I (in SLOS).`	`VAR_012725`
`VARIANT`	`297 297`	`1`	`I -> T (in SLOS).`	`VAR_023166`
`VARIANT`	`311 311`	`1`	`C -> G (in SLOS).`	`VAR_023167`
`VARIANT`	`311 311`	`1`	`C -> Y (in SLOS).`	`VAR_023168`
`VARIANT`	`324 324`	`1`	`Y -> H (in SLOS).`	`VAR_023169`
`VARIANT`	`326 326`	`1`	`V -> L (in SLOS).`	`VAR_012726`
`VARIANT`	`344 344`	`1`	`G -> R (in SLOS).`	`VAR_023170`
`VARIANT`	`352 352`	`1`	`R -> Q (in SLOS).`	`VAR_023171`
`VARIANT`	`352 352`	`1`	`R -> W (in SLOS).`	`VAR_012727`
`VARIANT`	`353 353`	`1`	`V -> A (in SLOS).`	`VAR_023172`
`VARIANT`	`362 362`	`1`	`R -> C (in SLOS).`	`VAR_023173`
`VARIANT`	`380 380`	`1`	`C -> R (in SLOS).`	`VAR_023174`
`VARIANT`	`380 380`	`1`	`C -> S (in SLOS).`	`VAR_012728`
`VARIANT`	`380 380`	`1`	`C -> Y (in SLOS).`	`VAR_023175`
`VARIANT`	`397 397`	`1`	`S -> L (in SLOS).`	`VAR_023176`
`VARIANT`	`404 404`	`1`	`R -> C (in SLOS).`	`VAR_012729`
`VARIANT`	`404 404`	`1`	`R -> S (in SLOS).`	`VAR_023177`
`VARIANT`	`405 405`	`1`	`H -> Y (in SLOS).`	`VAR_023178`
`VARIANT`	`408 408`	`1`	`Y -> H (in SLOS).`	`VAR_023179`
`VARIANT`	`410 410`	`1`	`G -> R (in SLOS).`	`VAR_023180`
`VARIANT`	`410 410`	`1`	`G -> S (in SLOS).`	`VAR_012730`
`VARIANT`	`426 426`	`1`	`H -> P (in SLOS).`	`VAR_023181`
`VARIANT`	`443 443`	`1`	`R -> C (in SLOS).`	`VAR_023182`
`VARIANT`	`446 446`	`1`	`R -> Q (in SLOS).`	`VAR_023183`
`VARIANT`	`448 448`	`1`	`E -> K (in SLOS; mild).`	`VAR_016975`
`VARIANT`	`448 448`	`1`	`E -> Q (in SLOS).`	`VAR_023184`
`VARIANT`	`450 450`	`1`	`R -> L (in SLOS).`	`VAR_023185`
`CONFLICT`	`5 5`		`S -> L (in Ref. 2; AAC05086).`
`CONFLICT`	`14 14`		`S -> A (in Ref. 5; AAC18345).`

Sequence information

Length: 475 AA [This is the length of the unprocessed precursor]

Molecular weight: 54489 Da [This is the MW of the unprocessed precursor]

CRC64: 7D726443834C4EEB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAKSQPNIP KAKSLDGVTN DRTASQGQWG RAWEVDWFSL ASVIFLLLFA PFIVYYFIMA 

        70         80         90        100        110        120 
CDQYSCALTG PVVDIVTGHA RLSDIWAKTP PITRKAAQLY TLWVTFQVLL YTSLPDFCHK 

       130        140        150        160        170        180 
FLPGYVGGIQ EGAVTPAGVV NKYQINGLQA WLLTHLLWFA NAHLLSWFSP TIIFDNWIPL 

       190        200        210        220        230        240 
LWCANILGYA VSTFAMVKGY FFPTSARDCK FTGNFFYNYM MGIEFNPRIG KWFDFKLFFN 

       250        260        270        280        290        300 
GRPGIVAWTL INLSFAAKQR ELHSHVTNAM VLVNVLQAIY VIDFFWNETW YLKTIDICHD 

       310        320        330        340        350        360 
HFGWYLGWGD CVWLPYLYTL QGLYLVYHPV QLSTPHAVGV LLLGLVGYYI FRVANHQKDL 

       370        380        390        400        410        420 
FRRTDGRCLI WGRKPKVIEC SYTSADGQRH HSKLLVSGFW GVARHFNYVG DLMGSLAYCL 

       430        440        450        460        470 
ACGGGHLLPY FYIIYMAILL THRCLRDEHR CASKYGRDWE RYTAAVPYRL LPGIF

Q9UBM7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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