Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9LDU6

- ST7R_ARATH

UniProt

Q9LDU6 - ST7R_ARATH

Protein

7-dehydrocholesterol reductase

Gene

DWF5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    Pathwayi

    GO - Molecular functioni

    1. 7-dehydrocholesterol reductase activity Source: UniProtKB-EC
    2. protein binding Source: IntAct
    3. sterol delta7 reductase activity Source: TAIR

    GO - Biological processi

    1. brassinosteroid biosynthetic process Source: TAIR
    2. cholesterol biosynthetic process Source: UniProtKB-KW

    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.
    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: Chromosome 1

    Organism-specific databases

    TAIRiAT1G50430.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. Golgi apparatus Source: TAIR
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: TAIR

    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

    GenevestigatoriQ9LDU6.

    Interactioni

    Binary interactionsi

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

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LDU6.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    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

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ERG4/ERG24 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG72042.
    HOGENOMiHOG000193296.
    InParanoidiQ9LDU6.
    KOiK00213.
    OMAiFYIIYMT.
    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. Align

    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

    MAETVHSPIV TYASMLSLLA FCPPFVILLW YTMVHQDGSV TQTFGFFWEN    50
    GVQGLINIWP RPTLIAWKII FCYGAFEAIL QLLLPGKRVE GPISPAGNRP 100
    VYKANGLAAY FVTLATYLGL WWFGIFNPAI VYDHLGEIFS ALIFGSFIFC 150
    VLLYIKGHVA PSSSDSGSCG NLIIDFYWGM ELYPRIGKSF DIKVFTNCRF 200
    GMMSWAVLAV TYCIKQYEIN GKVSDSMLVN TILMLVYVTK FFWWEAGYWN 250
    TMDIAHDRAG FYICWGCLVW VPSVYTSPGM YLVNHPVELG TQLAIYILVA 300
    GILCIYINYD CDRQRQEFRR TNGKCLVWGR APSKIVASYT TTSGETKTSL 350
    LLTSGWWGLA RHFHYVPEIL SAFFWTVPAL FDNFLAYFYV IFLTLLLFDR 400
    AKRDDDRCRS KYGKYWKLYC EKVKYRIIPG IY 432
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi F96540.
    RefSeqi NP_175460.1. NM_103926.5. [Q9LDU6-1 ]
    UniGenei At.25165.

    3D structure databases

    ProteinModelPortali Q9LDU6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 26690. 5 interactions.
    IntActi Q9LDU6. 5 interactions.
    STRINGi 3702.AT1G50430.1-P.

    Proteomic databases

    PaxDbi Q9LDU6.
    PRIDEi Q9LDU6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G50430.1 ; AT1G50430.1 ; AT1G50430 . [Q9LDU6-1 ]
    GeneIDi 841465.
    KEGGi ath:AT1G50430.

    Organism-specific databases

    TAIRi AT1G50430.

    Phylogenomic databases

    eggNOGi NOG72042.
    HOGENOMi HOG000193296.
    InParanoidi Q9LDU6.
    KOi K00213.
    OMAi FYIIYMT.
    PhylomeDBi Q9LDU6.

    Enzyme and pathway databases

    UniPathwayi UPA00062 .
    BioCyci ARA:AT1G50430-MONOMER.
    ARA:GQT-228-MONOMER.
    MetaCyc:AT1G50430-MONOMER.

    Miscellaneous databases

    PROi Q9LDU6.

    Gene expression databases

    Genevestigatori Q9LDU6.

    Family and domain databases

    InterProi IPR001171. Ergosterol_biosynth_ERG4_ERG24.
    IPR018083. Sterol_reductase_CS.
    [Graphical view ]
    Pfami PF01222. ERG4_ERG24. 1 hit.
    [Graphical view ]
    PROSITEi PS01017. STEROL_REDUCT_1. 1 hit.
    PS01018. STEROL_REDUCT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 108 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