A0A6G0T2N0 · A0A6G0T2N0_APHGL
- ProteinLon protease homolog, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids927 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 DNA in a site-specific manner.
Catalytic activity
Features
Showing features for binding site, active site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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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 | |
Molecular Function | single-stranded DNA binding | |
Biological Process | cellular response to oxidative stress | |
Biological Process | chaperone-mediated protein complex assembly | |
Biological Process | mitochondrion organization | |
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
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Sternorrhyncha > Aphidomorpha > Aphidoidea > Aphididae > Aphidini > Aphis > Aphis
Accessions
- Primary accessionA0A6G0T2N0
Proteomes
Subcellular Location
Interaction
Subunit
Homohexamer or homoheptamer. Organized in a ring with a central cavity.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 102-346 | Lon N-terminal | ||||
Sequence: LPFLPLVTIAKPPLYPRLFRIVEISDPRLIALIKRKKALNQPFIGLFMRKNIDTVPDNIVTNIDEVYSVGSLGRINEMRDFGNKLHMLIQCFRRIKLTKPLFEDQDIDKITNDLTKRNKKQSRNKGSSSSTEIEPIPVTEKTQNQVLMVEVENLKDEPYDKTMEIKALSQEIIKTIQSVISINPIYKEILHPMLQHGNVSDDPSYLSDIAAAIADCETHEYQEILEEINVPKRLLLALGCVKKLL | ||||||
Region | 216-238 | Disordered | ||||
Sequence: TKRNKKQSRNKGSSSSTEIEPIP | ||||||
Domain | 735-926 | Lon proteolytic | ||||
Sequence: DPIPGVVMGLAWTAMGGALMYIETEWTKDPATIIDKDKAVGNIILTGRLGETMQESAKIAYTVAKQFLSDLDPKNQTLLTGNIHLHVPEGATPKDGPSAGCTIVTALLSLALNIPIRNNVAMTGEISLKGKVMPVGGIKEKTIAAKRENVNCLILPDENKKDFNELPKFITDGIEVHFVSYYKDIFKIVFEN |
Sequence similarities
Belongs to the peptidase S16 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length927
- Mass (Da)104,970
- Last updated2020-08-12 v1
- Checksum37F95E72599A1A3F
Keywords
- Technical term