A0A9L0RXR0 · A0A9L0RXR0_HORSE

  • Protein
    Lon protease homolog, mitochondrial
  • Gene
    LONP1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

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.

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.

1942100200300400500600700800900
Type
IDPosition(s)Description
Binding site523-530ATP (UniProtKB | ChEBI)
Active site855
Active site898

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
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

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

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Thoroughbred
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Equidae > Equus

Accessions

  • Primary accession
    A0A9L0RXR0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

Type
IDPosition(s)Description
Transit peptide1-67Mitochondrion
ChainPRO_504055574368-942Lon 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
Region74-108Disordered
Domain125-370Lon N-terminal
Compositional bias224-256Basic and acidic residues
Region224-261Disordered
Domain759-942Lon proteolytic
Region903-942Disordered

Sequence similarities

Belongs to the peptidase S16 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    942
  • Mass (Da)
    103,916
  • Last updated
    2023-09-13 v1
  • MD5 Checksum
    6FB282EE3BD58AABF25C708816AB7F02
MATCTGYVRLWGAARCWALRRPLLAAAGGRVPTAAGAWLSRGRRTCDASPPWPLWGRCPAAAGQWRGLWEANNRSGGGAFPGGEDASEGGAEDGAAGAGGSAGGGEGPVITALTPMTIPDVFPHLPLIAVTRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYAGVFLKRDDSNESDVVESLDEVYHTGTFVQIHEMQDLGDKLRMIVMGHRRIHINRPLEVEPEEAEAESKQKARRKAKRGKKEAEDEASARRQMEAGVEPAAAPGEVLMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKEDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSDENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTRTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANITETIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKARLSSAVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAEFVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPRDSDSKGDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHDPSNEYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMDRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAVSQPPTQGCPSSGRHMAAGPGPREGGGRPVTARPEPRGAGS

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F7CA98F7CA98_HORSELONP11052
A0A9L0SXF8A0A9L0SXF8_HORSELONP1921
A0A9L0SRM0A0A9L0SRM0_HORSELONP1942

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias224-256Basic and acidic residues

Keywords

Genome annotation databases

Similar Proteins

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