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Protein

7-dehydrocholesterol reductase

Gene

DWF5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC). Lesions in the gene coding for the enzyme cause dwarfism.

Catalytic activityi

Cholesterol + NADP+ = cholesta-5,7-dien-3-beta-ol + NADPH.

Pathway: steroid biosynthesis

This protein is involved in the pathway steroid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway steroid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

  • 7-dehydrocholesterol reductase activity Source: UniProtKB-EC
  • sterol delta7 reductase activity Source: TAIR

GO - Biological processi

  • brassinosteroid biosynthetic process Source: TAIR
  • cholesterol biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciARA:AT1G50430-MONOMER.
ARA:GQT-228-MONOMER.
MetaCyc:AT1G50430-MONOMER.
BRENDAi1.3.1.21. 399.
UniPathwayiUPA00062.

Names & Taxonomyi

Protein namesi
Recommended name:
7-dehydrocholesterol reductase (EC:1.3.1.21)
Short name:
7-DHC reductase
Alternative name(s):
Protein DWARF 5
Sterol Delta(7)-reductase
Gene namesi
Name:DWF5
Synonyms:ST7R
Ordered Locus Names:At1g50430
ORF Names:F11F12.21
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G50430.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3423HelicalSequence AnalysisAdd
BLAST
Transmembranei64 – 8623HelicalSequence AnalysisAdd
BLAST
Transmembranei107 – 12620HelicalSequence AnalysisAdd
BLAST
Transmembranei136 – 15520HelicalSequence AnalysisAdd
BLAST
Transmembranei195 – 21218HelicalSequence AnalysisAdd
BLAST
Transmembranei227 – 24923HelicalSequence AnalysisAdd
BLAST
Transmembranei261 – 28323HelicalSequence AnalysisAdd
BLAST
Transmembranei287 – 30923HelicalSequence AnalysisAdd
BLAST
Transmembranei371 – 39323HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: TAIR
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi257 – 2571D → N in DWF5-4; dwarf plant. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4324327-dehydrocholesterol reductasePRO_0000207509Add
BLAST

Proteomic databases

PaxDbiQ9LDU6.
PRIDEiQ9LDU6.

Expressioni

Gene expression databases

ExpressionAtlasiQ9LDU6. baseline and differential.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NIP1-1Q8VZW12EBI-4439540,EBI-4424378

Protein-protein interaction databases

BioGridi26690. 5 interactions.
IntActiQ9LDU6. 5 interactions.
STRINGi3702.AT1G50430.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LDU6.
SMRiQ9LDU6. Positions 14-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ERG4/ERG24 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG72042.
HOGENOMiHOG000193296.
InParanoidiQ9LDU6.
KOiK00213.
OMAiALWFANA.
PhylomeDBiQ9LDU6.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9LDU6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAETVHSPIV TYASMLSLLA FCPPFVILLW YTMVHQDGSV TQTFGFFWEN
60 70 80 90 100
GVQGLINIWP RPTLIAWKII FCYGAFEAIL QLLLPGKRVE GPISPAGNRP
110 120 130 140 150
VYKANGLAAY FVTLATYLGL WWFGIFNPAI VYDHLGEIFS ALIFGSFIFC
160 170 180 190 200
VLLYIKGHVA PSSSDSGSCG NLIIDFYWGM ELYPRIGKSF DIKVFTNCRF
210 220 230 240 250
GMMSWAVLAV TYCIKQYEIN GKVSDSMLVN TILMLVYVTK FFWWEAGYWN
260 270 280 290 300
TMDIAHDRAG FYICWGCLVW VPSVYTSPGM YLVNHPVELG TQLAIYILVA
310 320 330 340 350
GILCIYINYD CDRQRQEFRR TNGKCLVWGR APSKIVASYT TTSGETKTSL
360 370 380 390 400
LLTSGWWGLA RHFHYVPEIL SAFFWTVPAL FDNFLAYFYV IFLTLLLFDR
410 420 430
AKRDDDRCRS KYGKYWKLYC EKVKYRIIPG IY
Length:432
Mass (Da):49,591
Last modified:October 1, 2000 - v1
Checksum:i5458E495BE1EF4B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171Y → H in AAC49278 (PubMed:8631902).Curated
Sequence conflicti308 – 3081N → K in AAC49278 (PubMed:8631902).Curated
Sequence conflicti391 – 3922Missing in AAC49278 (PubMed:8631902).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49398 mRNA. Translation: AAC49278.1.
AF239701 Genomic DNA. Translation: AAF63498.1.
AC012561 Genomic DNA. Translation: AAF87888.1.
CP002684 Genomic DNA. Translation: AEE32547.1.
AY099589 mRNA. Translation: AAM20440.1.
BT000245 mRNA. Translation: AAN15564.1.
PIRiF96540.
RefSeqiNP_175460.1. NM_103926.5. [Q9LDU6-1]
UniGeneiAt.25165.

Genome annotation databases

EnsemblPlantsiAT1G50430.1; AT1G50430.1; AT1G50430. [Q9LDU6-1]
GeneIDi841465.
KEGGiath:AT1G50430.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49398 mRNA. Translation: AAC49278.1.
AF239701 Genomic DNA. Translation: AAF63498.1.
AC012561 Genomic DNA. Translation: AAF87888.1.
CP002684 Genomic DNA. Translation: AEE32547.1.
AY099589 mRNA. Translation: AAM20440.1.
BT000245 mRNA. Translation: AAN15564.1.
PIRiF96540.
RefSeqiNP_175460.1. NM_103926.5. [Q9LDU6-1]
UniGeneiAt.25165.

3D structure databases

ProteinModelPortaliQ9LDU6.
SMRiQ9LDU6. Positions 14-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi26690. 5 interactions.
IntActiQ9LDU6. 5 interactions.
STRINGi3702.AT1G50430.1.

Proteomic databases

PaxDbiQ9LDU6.
PRIDEiQ9LDU6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G50430.1; AT1G50430.1; AT1G50430. [Q9LDU6-1]
GeneIDi841465.
KEGGiath:AT1G50430.

Organism-specific databases

TAIRiAT1G50430.

Phylogenomic databases

eggNOGiNOG72042.
HOGENOMiHOG000193296.
InParanoidiQ9LDU6.
KOiK00213.
OMAiALWFANA.
PhylomeDBiQ9LDU6.

Enzyme and pathway databases

UniPathwayiUPA00062.
BioCyciARA:AT1G50430-MONOMER.
ARA:GQT-228-MONOMER.
MetaCyc:AT1G50430-MONOMER.
BRENDAi1.3.1.21. 399.

Miscellaneous databases

PROiQ9LDU6.

Gene expression databases

ExpressionAtlasiQ9LDU6. baseline and differential.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning by metabolic interference in yeast and enzymatic characterization of Arabidopsis thaliana sterol delta 7-reductase."
    Lecain E., Chenivesse X., Spagnoli R., Pompon D.
    J. Biol. Chem. 271:10866-10873(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Seedling.
  2. "Lesions in the sterol delta reductase gene of Arabidopsis cause dwarfism due to a block in brassinosteroid biosynthesis."
    Choe S., Tanaka A., Noguchi T., Fujioka S., Takatsuto S., Ross A.S., Tax F.E., Yoshida S., Feldmann K.A.
    Plant J. 21:431-443(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, MUTAGENESIS OF ASP-257.
    Strain: cv. Wassilewskija-2.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    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.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiST7R_ARATH
AccessioniPrimary (citable) accession number: Q9LDU6
Secondary accession number(s): Q38930
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.