ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q7SXF1

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DHCR7_DANRE
Primary accession number Q7SXF1
Secondary accession numbers None
Integrated into Swiss-Prot on September 13, 2005
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 40)
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
Danio rerio (Zebrafish) (Brachydanio rerio) [TaxID: 7955] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; Cyprinidae; Danio.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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
BC055631; AAH55631.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_958487.1; -.
UniGene Dr.83800
3D structure databases
ModBase Q7SXF1.
Organism-specific databases
ZFIN ZDB-GENE-030912-9; dhcr7.
Gene expression databases
ArrayExpress Q7SXF1; -.
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.
BLOCKS Q7SXF1.
ProtoNet Q7SXF1.
Genome annotation databases
Ensembl ENSDARG00000015564; Danio rerio. [Contig view]
GeneID 378446; -.
KEGG dre:378446; -.
Phylogenomic databases
HOGENOM Q7SXF1; -.
HOVERGEN Q7SXF1; -.
Other
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   478  478     7-dehydrocholesterol reductase. PRO_0000207505
TRANSMEM   43    63  21     Potential. 
TRANSMEM   97   117  21     Potential. 
TRANSMEM   180   200  21     Potential. 
TRANSMEM   269   289  21     Potential. 
TRANSMEM   309   329  21     Potential. 
TRANSMEM   333   353  21     Potential. 
TRANSMEM   424   444  21     Potential. 
Sequence information
Length: 478 AA [This is the length of the unprocessed precursor] Molecular weight: 55189 Da [This is the MW of the unprocessed precursor] CRC64: EFFDB76773E4ECD7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MMASDRVRKR HKGSANGAQT VEKEPSKEPA QWGRAWEVDW FSLSGVILLL CFAPFLVSFF 

        70         80         90        100        110        120 
IMACDQYQCS ISHPLLDLYN GDATLFTIWN RAPSFTWAAA KIYAIWVTFQ VVLYMCVPDF 

       130        140        150        160        170        180 
LHKILPGYVG GVQDGARTPA GLINKYEVNG LQCWLITHVL WVLNAQHFHW FSPTIIIDNW 

       190        200        210        220        230        240 
IPLLWCTNIL GYAVSTFAFI KAYLFPTNPE DCKFTGNMFY NYMMGIEFNP RIGKWFDFKL 

       250        260        270        280        290        300 
FFNGRPGIVA WTLINLSYAA KQQELYGYVT NSMILVNVLQ AVYVVDFFWN EAWYLKTIDI 

       310        320        330        340        350        360 
CHDHFGWYLG WGDCVWLPFL YTLQGLYLVY NPIQLSTPHA AGVLILGLVG YYIFRVTNHQ 

       370        380        390        400        410        420 
KDLFRRTEGN CSIWGKKPTF IECSYQSADG AIHKSKLMTS GFWGVARHMN YTGDLMGSLA 

       430        440        450        460        470 
YCLACGGNHL LPYFYIIYMT ILLVHRCIRD EHRCSNKYGK DWERYTAAVS YRLLPNIF
Q7SXF1 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!