Q8LFT2 · DRP3B_ARATH

Function

function

Involved in the control of mitochondrial and peroxisomal division and morphology.

Features

Showing features for binding site.

1780100200300400500600700
TypeIDPosition(s)Description
Binding site50-57GTP (UniProtKB | ChEBI)
Binding site157-161GTP (UniProtKB | ChEBI)
Binding site226-229GTP (UniProtKB | ChEBI)

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 Componentcytoplasm
Cellular Componentmembrane
Cellular Componentmicrotubule
Cellular Componentmitochondrion
Cellular Componentperoxisome
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionmicrotubule binding
Biological Processcell division
Biological Processmitochondrial fission
Biological Processperoxisome fission

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Dynamin-related protein 3B
  • Alternative names
    • Dynamin-like protein 2b

Gene names

    • Name
      DRP3B
    • Synonyms
      ADL2B
    • ORF names
      T22C12.1
    • Ordered locus names
      At2g14120

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
    Q8LFT2
  • Secondary accessions
    • Q8LPH8
    • Q8S8A4
    • Q8S943
    • Q9SI47

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Reduced plant growth. Increase in the size of peroxisomes and decrease in the number of peroxisomes per cell.

Variants

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

The viewer provides 56 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00002065852-780

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with ARC5 on peroxisomes and ELM1 on mitochondria.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q8LFT2DRP3A Q8S9446EBI-2265511, EBI-2265428
BINARY Q8LFT2LSD1 P940773EBI-2265511, EBI-5849461

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain40-315Dynamin-type G
Region50-57G1 motif
Region76-78G2 motif
Region157-160G3 motif
Region226-229G4 motif
Region256-259G5 motif
Region536-558Disordered
Region573-592Disordered
Domain654-745GED
Region753-780Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8LFT2-1

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.

  • Length
    780
  • Mass (Da)
    86,644
  • Last updated
    2005-02-01 v2
  • Checksum
    CB50374F3F428714
MSVDDLPPSSASAVTPLGSSVIPIVNKLQDIFAQLGSQSTIALPQVAVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLRLQLVQTKPSSDGGSDEEWGEFLHHDPVRRIYDFSEIRREIEAETNRVSGENKGVSDIPIGLKIFSPNVLDISLVDLPGITKVPVGDQPSDIEARIRTMILTYIKEPSCLILAVSPANTDLANSDALQIAGNADPDGHRTIGVITKLDIMDRGTDARNHLLGKTIPLRLGYVGVVNRSQEDILMNRSIKDALVAEEKFFRSRPVYSGLTDRLGVPQLAKKLNQVLVQHIKALLPSLKSRINNALFATAKEYESYGDITESRGGQGALLLSFITKYCEAYSSTLEGKSKEMSTSELSGGARILYIFQSVFVKSLEEVDPCEDLTADDIRTAIQNATGPRSALFVPDVPFEVLVRRQISRLLDPSLQCARFIFDELVKISHQCMMKELQRFPVLQKRMDEVIGNFLREGLEPSQAMIRDLIEMEMDYINTSHPNFIGGTKAVEQAMQTVKSSRIPHPVARPRDTVEPERTASSGSQIKTRSFLGRQANGIITDQAVPTAADAERPAPAGSTSWSGFSSIFRGSDGQAAAKNNLLNKPFSETTQEVYQNLSTIYLKEPPTILKSSETHSEQESVEIEITKLLLKSYYDIVRKNVEDLVPKAIMHFLVNYTKRELHNVFIEKLYRENLIEELLKEPDELAIKRKRTQETLRILQQANRTLDELPLEAESVERGYKIGSEAKHEELPGTRRSRTETNGNGRLHM

Q8LFT2-2

  • Name
    2
  • Note
    May be due to an intron retention.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 343-370: GGQGALLLSFITKYCEAYSSTLEGKSKE → VCGFWPVLALYIPSILNDGIAICFFCVV
    • 371-780: Missing

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1P8AXZ9A0A1P8AXZ9_ARATHAt2g140801082
A0A1P8AX46A0A1P8AX46_ARATHDRP3B737
F4IFF6F4IFF6_ARATHAt2g140801215
F4IFG1F4IFG1_ARATHDRP3B780
F4IFG2F4IFG2_ARATHDRP3B809

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict96in Ref. 1; BAB85645
Sequence conflict204in Ref. 4; AAM20619
Alternative sequenceVSP_012757343-370in isoform 2
Sequence conflict369In isoform Q8LFT2-2; in Ref. 5; AAM61220
Alternative sequenceVSP_012758371-780in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB072375
EMBL· GenBank· DDBJ
BAB85645.1
EMBL· GenBank· DDBJ
mRNA
AC007197
EMBL· GenBank· DDBJ
AAM15450.1
EMBL· GenBank· DDBJ
Genomic DNA
AC007197
EMBL· GenBank· DDBJ
AAD25856.2
EMBL· GenBank· DDBJ
Genomic DNA
CP002685
EMBL· GenBank· DDBJ
AEC06282.1
EMBL· GenBank· DDBJ
Genomic DNA
AY099768
EMBL· GenBank· DDBJ
AAM20619.1
EMBL· GenBank· DDBJ
mRNA
AY084657
EMBL· GenBank· DDBJ
AAM61220.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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