Q9M9L8 · LONM3_ARATH

Function

function

ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.

Catalytic activity

  • Hydrolysis of proteins in presence of ATP.
    EC:3.4.21.53 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, active site.

1924100200300400500600700800900
TypeIDPosition(s)Description
Binding site447-454ATP (UniProtKB | ChEBI)
Active site828
Active site871

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 Componentmitochondrial matrix
Cellular Componentmitochondrion
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionsequence-specific DNA binding
Molecular Functionserine-type endopeptidase activity
Biological Processcellular response to oxidative stress
Biological Processchaperone-mediated protein complex assembly
Biological Processoxidation-dependent protein catabolic process
Biological Processprotein quality control for misfolded or incompletely synthesized proteins

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Lon protease homolog 3, mitochondrial
  • EC number

Gene names

    • Name
      LON3
    • ORF names
      F10A16.7
    • Ordered locus names
      At3g05780

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
    Q9M9L8

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-63Mitochondrion
ChainPRO_000004542464-924Lon protease homolog 3, mitochondrial

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homohexamer or homoheptamer. Organized in a ring with a central cavity.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain112-325Lon N-terminal
Domain738-922Lon proteolytic

Sequence similarities

Belongs to the peptidase S16 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    924
  • Mass (Da)
    103,476
  • Last updated
    2000-10-01 v1
  • Checksum
    DF6BCA96ECF99C65
MMPKRFNTSGFDTTLRLPSYYGFLHLTQSLTLNSRVFYGARHVTPPAIRIGSNPVQSLLLFRAPTQLTGWNRSSRDLLGRRVSFSDRSDGVDLLSSSPILSTNPNLDDSLTVIALPLPHKPLIPGFYMPIHVKDPKVLAALQESTRQQSPYVGAFLLKDCASTDSSSRSETEDNVVEKFKVKGKPKKKRRKELLNRIHQVGTLAQISSIQGEQVILVGRRRLIIEEMVSEDPLTVRVDHLKDKPYDKDNAVIKASYVEVISTLREVLKTNSLWRDQDIGDFSYQHLADFGAGISGANKHKNQGVLTELDVHKRLELTLELVKKQVEINKIKETDDGSSLSAKIRVRIDTKRDKIPKHVIKVMEEEFTKLEMLEENYSDFDLTYNYLHWLTVLPWGNFSYENFDVLRAKKILDEDHYGLSDVKERILEFIAVGRLRGTSQGKIICLSGPPGVGKTSIGRSIARALDRKFFRFSVGGLSDVAEIKGHCQTYVGAMPGKMVQCLKSVGTANPLILFDEIDKLGRCHTGDPASALLEVMDPEQNAKFLDHFLNVTIDLSKVLFVCTANVIEMIPGPLLDRMEVIDLSGYVTDEKMHIARDYLVKKTCRDCGIKPEHVDLSDAALLSLIENYCREAGVRNLQKQIEKIYRKVALELVRQGAVSFDVTDTKDTKSLAKTDSEVKRMKVADIMKILESATGDSTESKTKQSGLVAKTFEKVMIDESNLADYVGKPVFQEEKIYEQTPVGVVMGLAWTSMGGSTLYIETTFVEEGLGKGGLHITGQLGDVMKESAQIAHTVARRIMFEKEPENLFFANSKLHLHVPEGATPKDGPSAGCTMITSFLSLAMKKLVRKDLAMTGEVTLTGRILPIGGVKEKTIAARRSQIKTIIFPEANRRDFEELAENMKEGLDVHFVDEYEKIFDLAFNYDH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC012393
EMBL· GenBank· DDBJ
AAF26080.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE74296.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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