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UniProtKB/Swiss-Prot entry Q9Z2Z8


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHCR7_RAT
Primary accession number Q9Z2Z8
Secondary accession numbers None
Integrated into Swiss-Prot on September 13, 2005
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 52)
Name and origin of the protein
Protein name 7-dehydrocholesterol reductase
Synonyms 7-DHC reductase
EC 1.3.1.21
Sterol Delta(7)-reductase
Gene name
Name: Dhcr7
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Liver;
Nishino H., Ishibashi T.;
"Transmembrane configuration of sterol delta 7-reductase as a potential sterol sensing protein.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
DOI=10.1074/jbc.274.21.14624; PubMed=10329655 [NCBI, ExPASy, EBI, Israel, Japan]
Bae S.-H., Lee J.N., Fitzky B.U., Seong J., Paik Y.-K.;
"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.";
J. Biol. Chem. 274:14624-14631(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1016/S0167-4781(02)00285-3; PubMed=12031495 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J.-N., Bae S.-H., Paik Y.-K.;
"Structure and alternative splicing of the rat 7-dehydrocholesterol reductase gene.";
Biochim. Biophys. Acta 1576:148-156(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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
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
AB016800; BAA34306.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF071500; AAD31383.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF272393; AAM45144.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF279892; AAK69490.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC081688; AAH81688.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_071784.1; -.
UniGene Rn.228
3D structure databases
ModBase Q9Z2Z8.
Organism-specific databases
RGD 621769; Dhcr7.
Gene expression databases
ArrayExpress Q9Z2Z8; -.
GermOnline ENSRNOG00000020776; Rattus norvegicus.
Ontologies
GO
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 electronic annotation from EC).
GO:0006695; Biological process: cholesterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
ProtoNet Q9Z2Z8.
Genome annotation databases
Ensembl ENSRNOG00000020776; Rattus norvegicus. [Contig view]
GeneID 64191; -.
KEGG rno:64191; -.
Phylogenomic databases
HOVERGEN Q9Z2Z8; -.
Other
NextBio 612852; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cholesterol biosynthesis; Endoplasmic reticulum; Lipid synthesis; Membrane; NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   471  471     7-dehydrocholesterol reductase. PRO_0000207504
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. 
Sequence information
Length: 471 AA [This is the length of the unprocessed precursor] Molecular weight: 54155 Da [This is the MW of the unprocessed precursor] CRC64: EBF0CBC4F4222FDB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASKSQHNAS KAKNHNVKAE SQGQWGRAWE VDWFSLVSVI FLLLFAPFIV YYFIMACDQY 

        70         80         90        100        110        120 
SCSLTAPILD VATGRASLAD IWAKTPPVTA KAAQLYALWV SFQVLLYSWL PDFCHRFLPG 

       130        140        150        160        170        180 
YVGGVQEGAI TPAGIVNKYE VNGLQAWLIT HFLWFVNAYL 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 PNALGVLLLG LVGYYIFRMT NHQKDLFRRT 

       370        380        390        400        410        420 
DGHCLIWGKK PKAIECSYTS ADGLKHRSKL LVSGFWGVAR HFNYTGDLMG SLAYCLACGG 

       430        440        450        460        470 
GHLLPYFYII YMTILLTHRC LRDEHRCANK YGRDWERYVA AVPYRLLPGI F 

Q9Z2Z8 in FASTA format

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