Q39085 · DIM_ARATH

Function

function

Plays a critical role in the general process of plant cell elongation. Involved in the synthesis of campesterol, an early precursor of brassinolide. Required for the conversion of 24-methylenecholesterol to campesterol and for the conversion of isofucosterol to sitosterol. Necessary for both the isomerization and reduction of 24-methylenecholesterol. Regulates indirectly phytochrome-mediated light responses through the modulation of brassinosteroid biosynthesis.

Catalytic activity

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum
Cellular Componentmembrane
Cellular Componentplant-type vacuole
Cellular Componentvacuole
Molecular Functioncalmodulin binding
Molecular Functiondelta24-sterol reductase activity
Molecular FunctionFAD binding
Biological Processbrassinosteroid biosynthetic process
Biological Processlignin metabolic process
Biological Processplant-type secondary cell wall biogenesis
Biological Processunidimensional cell growth

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Delta(24)-sterol reductase
  • EC number
  • Alternative names
    • Cell elongation protein DIMINUTO
    • Cell elongation protein Dwarf1
    • Protein CABBAGE1
    • Protein ENHANCED VERY-LOW-FLUENCE RESPONSE 1

Gene names

    • Name
      DIM
    • Synonyms
      CBB1, DWF1, EVE1
    • ORF names
      MPN9.6
    • Ordered locus names
      At3g19820

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q39085
  • Secondary accessions
    • Q0WWL4
    • Q38808
    • Q8RXF4

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain1-25Lumenal
Transmembrane26-46Helical; Signal-anchor
Topological domain47-561Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

Dwarf and reduced fertility.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis131In dwf1-9; dwarf phenotype.
Mutagenesis163In dwf1-3; dwarf phenotype.
Mutagenesis172In dwf1-10; dwarf phenotype.
Mutagenesis220In dwf1-11; dwarf phenotype.
Mutagenesis282In dwf1-7; dwarf phenotype.
Mutagenesis521-523Loss of calmodulin binding and loss of function.
Mutagenesis531Decreased calmodulin binding and partial loss of function.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00002194951-561Delta24-sterol reductase
Modified residue2Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with calmodulin.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q39085At3g54130 Q9M3913EBI-16906963, EBI-25520805

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain49-232FAD-binding PCMH-type
Region518-539Interaction with calmodulin

Sequence similarities

Belongs to the DIMINUTO family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    561
  • Mass (Da)
    65,394
  • Last updated
    2001-11-02 v2
  • Checksum
    CD25EF655AD44200
MSDLQTPLVRPKRKKTWVDYFVKFRWIIVIFIVLPFSATFYFLIYLGDMWSESKSFEKRQKEHDENVKKVIKRLKGRDASKDGLVCTARKPWIAVGMRNVDYKRARHFEVDLGEFRNILEINKEKMTARVEPLVNMGQISRATVPMNLSLAVVAELDDLTVGGLINGYGIEGSSHIYGLFADTVEAYEIVLAGGELVRATRDNEYSDLYYAIPWSQGTLGLLVAAEIRLIKVKEYMRLTYIPVKGDLQALAQGYIDSFAPKDGDKSKIPDFVEGMVYNPTEGVMMVGTYASKEEAKKKGNKINNVGWWFKPWFYQHAQTALKKGQFVEYIPTREYYHRHTRCLYWEGKLILPFGDQFWFRYLLGWLMPPKVSLLKATQGEAIRNYYHDMHVIQDMLVPLYKVGDALEWVHREMEVYPIWLCPHKLFKQPIKGQIYPEPGFEYENRQGDTEDAQMYTDVGVYYAPGCVLRGEEFDGSEAVRRMEKWLIENHGFQPQYAVSELDEKSFWRMFNGELYEECRKKYRAIGTFMSVYYKSKKGRKTEKEVREAEQAHLETAYAEAD

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict399in Ref. 5; AAL91175/AAN15686
Sequence conflict450in Ref. 1; AAA67055
Sequence conflict476in Ref. 1; AAA67055
Sequence conflict506in Ref. 1; AAA67055
Sequence conflict527in Ref. 5; AAL91175/AAN15686
Sequence conflict556-558in Ref. 1; AAA67055

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L38520
EMBL· GenBank· DDBJ
AAA67055.1
EMBL· GenBank· DDBJ
mRNA
U12400
EMBL· GenBank· DDBJ
AAA20244.1
EMBL· GenBank· DDBJ
mRNA
AB025631
EMBL· GenBank· DDBJ
BAB01296.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE76293.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE76294.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE76295.1
EMBL· GenBank· DDBJ
Genomic DNA
AY072216
EMBL· GenBank· DDBJ
AAL60037.1
EMBL· GenBank· DDBJ
mRNA
AY081286
EMBL· GenBank· DDBJ
AAL91175.1
EMBL· GenBank· DDBJ
mRNA
AY096472
EMBL· GenBank· DDBJ
AAM20112.1
EMBL· GenBank· DDBJ
mRNA
BT000367
EMBL· GenBank· DDBJ
AAN15686.1
EMBL· GenBank· DDBJ
mRNA
AK226335
EMBL· GenBank· DDBJ
BAE98484.1
EMBL· GenBank· DDBJ
mRNA
AB493623
EMBL· GenBank· DDBJ
BAH30461.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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