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A0A7J8BTB3 · A0A7J8BTB3_ROUAE

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 promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site527-534ATP (UniProtKB | ChEBI)

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lon protease homolog, mitochondrial
  • EC number
  • Alternative names
    • Lon protease-like protein
      (LONP
      )
    • Mitochondrial ATP-dependent protease Lon
    • Serine protease 15

Gene names

    • Name
      LONP1
    • ORF names
      HJG63_012612

Organism names

Accessions

  • Primary accession
    A0A7J8BTB3

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

Type
IDPosition(s)Description
Transit peptide1-67Mitochondrion
ChainPRO_502999070968-974Lon protease homolog, mitochondrial

Interaction

Subunit

Homohexamer. Organized in a ring with a central cavity. The ATP-binding and proteolytic domains (AP-domain) form a hexameric chamber, while the N-terminal domain is arranged as a trimer of dimers. DNA and RNA binding is stimulated by substrate and inhibited by ATP binding. Interacts with TWNK and mitochondrial DNA polymerase subunit POLG.

Family & Domains

Features

Showing features for region, domain, compositional bias.

Type
IDPosition(s)Description
Region76-106Disordered
Domain128-374Lon N-terminal
Compositional bias226-259Basic and acidic residues
Region226-262Disordered
Region786-805Disordered
Compositional bias788-802Basic and acidic residues
Region880-940Disordered
Compositional bias911-940Basic and acidic residues

Sequence similarities

Belongs to the peptidase S16 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    974
  • Mass (Da)
    108,063
  • Last updated
    2021-04-07 v1
  • MD5 Checksum
    1588A8B15E8A5E6F0D21F9C377178BFD
MAAGTGYVRLWGAARCWALRRPVLAVAGGRVPTAAGAWLPRGRRTCDACSPWALWGRGPAAAGQWRGFWEANSRGGGAGGGSFSGGEDASEGGAEDGAAGAGGNAGGGESPVITALTPMTIPDVFPHLPLIAVTRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYAGVFLKRDDTNESDVVESLDEVYHTGTFVQIHEMQDLGDKLRMIVMGHRRIHISRQLEVEPEEAEAENKQKARRKPKRSRKEAEEEPGARRQMEMVAEPNSGAPGEVLMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETSIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKEDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLSLLDNHSSEFNVTRNYLDWLTSIPWGKYSDENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMADVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTETIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKARLSSDVLTVLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTALGGSTLFVETSPRRPQEKDSHGDKDGSLEVTGQLGDVMKESARIAYTFARAFLMQHDPSNQYLVASHLHLHVPEVRPAWALAAPGPPTSLVCLPPTCPFLPGRHPQGRPERRLHHRHSPALAGHGPACAAQPGHDRRGLPHRQDPASGRHQGEDHRGQACRSDVHHPACREQKGLLRPGCLHYRGPGGPLRGALPRDL

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A7J8BSB2A0A7J8BSB2_ROUAELONP1829
A0A7J8BSB3A0A7J8BSB3_ROUAELONP1973
A0A7J8BS03A0A7J8BS03_ROUAELONP1937
A0A7J8BS26A0A7J8BS26_ROUAELONP1895
A0A7J8BT50A0A7J8BT50_ROUAELONP1963

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias226-259Basic and acidic residues
Compositional bias788-802Basic and acidic residues
Compositional bias911-940Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACASE010000016
EMBL· GenBank· DDBJ
KAF6401635.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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