Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9LDU6 (ST7R_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
7-dehydrocholesterol reductase

Short name=7-DHC reductase
EC=1.3.1.21
Alternative name(s):
Protein DWARF 5
Sterol Delta(7)-reductase
Gene names
Name:DWF5
Synonyms:ST7R
Ordered Locus Names:At1g50430
ORF Names:F11F12.21
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Pathway

Lipid metabolism; steroid biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the ERG4/ERG24 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NIP1-1Q8VZW12EBI-4439540,EBI-4424378

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9LDU6-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4324327-dehydrocholesterol reductase
PRO_0000207509

Regions

Transmembrane12 – 3423Helical; Potential
Transmembrane64 – 8623Helical; Potential
Transmembrane107 – 12620Helical; Potential
Transmembrane136 – 15520Helical; Potential
Transmembrane195 – 21218Helical; Potential
Transmembrane227 – 24923Helical; Potential
Transmembrane261 – 28323Helical; Potential
Transmembrane287 – 30923Helical; Potential
Transmembrane371 – 39323Helical; Potential

Experimental info

Mutagenesis2571D → N in DWF5-4; dwarf plant. Ref.2
Sequence conflict1171Y → H in AAC49278. Ref.1
Sequence conflict3081N → K in AAC49278. Ref.1
Sequence conflict391 – 3922Missing in AAC49278. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 5458E495BE1EF4B0

FASTA43249,591
        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 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRF96540.
RefSeqNP_175460.1. NM_103926.5.
UniGeneAt.25165.

3D structure databases

ProteinModelPortalQ9LDU6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid26690. 5 interactions.
IntActQ9LDU6. 5 interactions.
STRING3702.AT1G50430.1-P.

Proteomic databases

PaxDbQ9LDU6.
PRIDEQ9LDU6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G50430.1; AT1G50430.1; AT1G50430. [Q9LDU6-1]
GeneID841465.
KEGGath:AT1G50430.

Organism-specific databases

TAIRAT1G50430.

Phylogenomic databases

eggNOGNOG72042.
HOGENOMHOG000193296.
InParanoidQ9LDU6.
KOK00213.
OMATFAMIKG.
PhylomeDBQ9LDU6.
ProtClustDBCLSN2682729.

Enzyme and pathway databases

BioCycARA:AT1G50430-MONOMER.
ARA:GQT-228-MONOMER.
MetaCyc:AT1G50430-MONOMER.
UniPathwayUPA00062.

Gene expression databases

GenevestigatorQ9LDU6.

Family and domain databases

InterProIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9LDU6.

Entry information

Entry nameST7R_ARATH
AccessionPrimary (citable) accession number: Q9LDU6
Secondary accession number(s): Q38930
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names