| IED ID | IndEnz0002000046 |
| Enzyme Type ID | protease000046 |
| Protein Name |
Lon protease homolog, mitochondrial EC 3.4.21.53 Lon protease-like protein LONP Mitochondrial ATP-dependent protease Lon Serine protease 15 |
| Gene Name | Lonp1 Lon Prss15 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MAASTGYVRLWAAARCWVLRRPLLAVTGGRVPSASGSWLRRGCRVCDTSTPWGGRVPMGGGQWRGLWDAGSRGGSDETSEGGVEDGATASSGEGPVVTALAPMTVPDVFPHLPLIAISRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVTGHRRIHISRQLEVEPEGLEPEAENKQKSRRKLKRGKKEVGDELGAKPQLEMVTEATSDTSKEVLMVEVENVAHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQSVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARTLCGLDESKAQLSATVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVSGEAQTVHVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQPSGSKEDKDGSLEVTGQLGDVMKESARIAYTFARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDFSDLAPFITEGLEVHFVEHYRDIFRIAFPLREHQEALAVER |
| Enzyme Length | 950 |
| Uniprot Accession Number | Q924S5 |
| Absorption | |
| Active Site | ACT_SITE 845; /evidence=ECO:0000255|HAMAP-Rule:MF_03120; ACT_SITE 888; /evidence=ECO:0000255|HAMAP-Rule:MF_03120 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|HAMAP-Rule:MF_03120}; |
| DNA Binding | |
| EC Number | 3.4.21.53 |
| Enzyme 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. {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12752449, ECO:0000269|PubMed:15560797}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 513..520; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_03120 |
| Features | Active site (2); Chain (1); Domain (2); Nucleotide binding (1); Region (2); Transit peptide (1) |
| Keywords | ATP-binding;DNA-binding;Hydrolase;Mitochondrion;Nucleotide-binding;Protease;Reference proteome;Serine protease;Transit peptide |
| Interact With | |
| Induction | INDUCTION: By hypoxia or ER stress. {ECO:0000269|PubMed:12082077}. |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12752449, ECO:0000269|PubMed:15560797, ECO:0000269|PubMed:7961901}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10050756; 16396496; 19010380; |
| Motif | |
| Gene Encoded By | |
| Mass | 105,793 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |