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UniProtKB/Swiss-Prot entry Q9LDU6


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

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Entry information
Entry name ST7R_ARATH
Primary accession number Q9LDU6
Secondary accession number Q38930
Integrated into Swiss-Prot on January 31, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 55)
Name and origin of the protein
Protein name 7-dehydrocholesterol reductase
Synonyms 7-DHC reductase
EC 1.3.1.21
Sterol Delta(7)-reductase
Protein DWARF 5
Gene name
Name: DWF5
Synonyms: ST7R
OrderedLocusNames: At1g50430
ORFNames: F11F12.21
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Seedling;
DOI=10.1074/jbc.271.18.10866; PubMed=8631902 [NCBI, ExPASy, EBI, Israel, Japan]
Lecain E., Chenivesse X., Spagnoli R., Pompon D.;
"Cloning by metabolic interference in yeast and enzymatic characterization of Arabidopsis thaliana sterol delta 7-reductase.";
J. Biol. Chem. 271:10866-10873(1996).
[2]
NUCLEOTIDE SEQUENCE, AND MUTAGENESIS OF ASP-257.
STRAIN=cv. Wassilewskija-2;
PubMed=10758495 [NCBI, ExPASy, EBI, Israel, Japan]
Choe S., Tanaka A., Noguchi T., Fujioka S., Takatsuto S., Ross A.S., Tax F.E., Yoshida S., Feldmann K.A.;
"Lesions in the sterol delta reductase gene of Arabidopsis cause dwarfism due to a block in brassinosteroid biosynthesis.";
Plant J. 21:431-443(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
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
U49398; AAC49278.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF239701; AAF63498.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC012561; AAF87888.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY099589; AAM20440.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000245; AAN15564.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F96540; F96540.
RefSeq NP_175460.1; -.
UniGene At.25165
3D structure databases
ModBase Q9LDU6.
Enzyme and pathway databases
BioCyc MetaCyc:MON-7241; -.
Organism-specific databases
TAIR At1g50430; -.
Gene expression databases
ArrayExpress Q9LDU6; -.
GermOnline AT1G50430; Arabidopsis thaliana.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0047598; Molecular function: 7-dehydrocholesterol reductase activity (inferred from electronic annotation from EC).
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 Q9LDU6.
Genome annotation databases
GeneID 841465; -.
GenomeReviews CT485782_GR; AT1G50430.
NMPDR fig|3702.1.peg.4516; -.
Other
ProtoNet Q9LDU6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cholesterol biosynthesis; Complete proteome; 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   432  432     7-dehydrocholesterol reductase. PRO_0000207509
TRANSMEM   12    34  23     Potential. 
TRANSMEM   64    86  23     Potential. 
TRANSMEM   107   126  20     Potential. 
TRANSMEM   136   155  20     Potential. 
TRANSMEM   195   212  18     Potential. 
TRANSMEM   227   249  23     Potential. 
TRANSMEM   261   283  23     Potential. 
TRANSMEM   287   309  23     Potential. 
TRANSMEM   371   393  23     Potential. 
MUTAGEN   257   257        D->N: In DWF5-4; dwarf plant. 
CONFLICT   117   117        Y -> H (in Ref. 1; AAC49278). 
CONFLICT   308   308        N -> K (in Ref. 1; AAC49278). 
CONFLICT   391   392        Missing (in Ref. 1; AAC49278). 
Sequence information
Length: 432 AA [This is the length of the unprocessed precursor] Molecular weight: 49591 Da [This is the MW of the unprocessed precursor] CRC64: 5458E495BE1EF4B0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAETVHSPIV TYASMLSLLA FCPPFVILLW YTMVHQDGSV TQTFGFFWEN GVQGLINIWP 

        70         80         90        100        110        120 
RPTLIAWKII FCYGAFEAIL QLLLPGKRVE GPISPAGNRP VYKANGLAAY FVTLATYLGL 

       130        140        150        160        170        180 
WWFGIFNPAI VYDHLGEIFS ALIFGSFIFC VLLYIKGHVA PSSSDSGSCG NLIIDFYWGM 

       190        200        210        220        230        240 
ELYPRIGKSF DIKVFTNCRF GMMSWAVLAV TYCIKQYEIN GKVSDSMLVN TILMLVYVTK 

       250        260        270        280        290        300 
FFWWEAGYWN TMDIAHDRAG FYICWGCLVW VPSVYTSPGM YLVNHPVELG TQLAIYILVA 

       310        320        330        340        350        360 
GILCIYINYD CDRQRQEFRR TNGKCLVWGR APSKIVASYT TTSGETKTSL LLTSGWWGLA 

       370        380        390        400        410        420 
RHFHYVPEIL SAFFWTVPAL FDNFLAYFYV IFLTLLLFDR AKRDDDRCRS KYGKYWKLYC 

       430 
EKVKYRIIPG IY 

Q9LDU6 in FASTA format

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