A0A9L0RXR0 · A0A9L0RXR0_HORSE
- ProteinLon protease homolog, mitochondrial
- GeneLONP1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids942 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 523-530 | ATP (UniProtKB | ChEBI) | |||
Active site | 855 | ||||
Active site | 898 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent peptidase activity | |
Molecular Function | sequence-specific DNA binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | cellular response to oxidative stress | |
Biological Process | chaperone-mediated protein complex assembly | |
Biological Process | oxidation-dependent protein catabolic process | |
Biological Process | protein quality control for misfolded or incompletely synthesized proteins |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLon protease homolog, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Equidae > Equus
Accessions
- Primary accessionA0A9L0RXR0
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-67 | Mitochondrion | |||
Chain | PRO_5040555743 | 68-942 | Lon 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.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 74-108 | Disordered | |||
Domain | 125-370 | Lon N-terminal | |||
Compositional bias | 224-256 | Basic and acidic residues | |||
Region | 224-261 | Disordered | |||
Domain | 759-942 | Lon proteolytic | |||
Region | 903-942 | Disordered | |||
Sequence similarities
Belongs to the peptidase S16 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length942
- Mass (Da)103,916
- Last updated2023-09-13 v1
- MD5 Checksum6FB282EE3BD58AABF25C708816AB7F02
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F7CA98 | F7CA98_HORSE | LONP1 | 1052 | ||
A0A9L0SXF8 | A0A9L0SXF8_HORSE | LONP1 | 921 | ||
A0A9L0SRM0 | A0A9L0SRM0_HORSE | LONP1 | 942 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 224-256 | Basic and acidic residues | |||
Keywords
- Technical term