| IED ID | IndEnz0002010648 |
| Enzyme Type ID | protease010648 |
| Protein Name |
Lon protease homolog, mitochondrial EC 3.4.21.53 LONHs Lon protease-like protein LONP Mitochondrial ATP-dependent protease Lon Serine protease 15 |
| Gene Name | LONP1 PRSS15 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAASTGYVRLWGAARCWVLRRPMLAAAGGRVPTAAGAWLLRGQRTCDASPPWALWGRGPAIGGQWRGFWEASSRGGGAFSGGEDASEGGAEEGAGGAGGSAGAGEGPVITALTPMTIPDVFPHLPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVMGHRRVHISRQLEVEPEEPEAENKHKPRRKSKRGKKEAEDELSARHPAELAMEPTPELPAEVLMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQDKDAKGDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDEQAEALAVER |
| Enzyme Length | 959 |
| Uniprot Accession Number | P36776 |
| Absorption | |
| Active Site | ACT_SITE 855; /evidence=ECO:0000255|HAMAP-Rule:MF_03120; ACT_SITE 898; /evidence=ECO:0000255|HAMAP-Rule:MF_03120 |
| Activity Regulation | ACTIVITY REGULATION: Peptidase activity is subject to substrate inhibition by ATP. {ECO:0000269|PubMed:24520911}. |
| 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 (PubMed:12198491, PubMed:15870080, PubMed:17420247, PubMed:8248235). Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein, helicase Twinkle (TWNK) and the large ribosomal subunit protein bL32m. bL32m is protected from degradation by LONP1 when it is bound to a nucleic acid (RNA), but TWNK is not (PubMed:17579211, PubMed:28377575). {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12198491, ECO:0000269|PubMed:15870080, ECO:0000269|PubMed:17420247, ECO:0000269|PubMed:17579211, ECO:0000269|PubMed:28377575, ECO:0000269|PubMed:8248235}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 523..530; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_03120 |
| Features | Active site (2); Alternative sequence (2); Beta strand (7); Chain (1); Compositional bias (2); Domain (2); Erroneous initiation (1); Helix (9); Mutagenesis (9); Natural variant (15); Nucleotide binding (1); Region (2); Sequence conflict (9); Transit peptide (1); Turn (1) |
| Keywords | 3D-structure;ATP-binding;Alternative splicing;Cataract;DNA-binding;Deafness;Disease variant;Dwarfism;Hydrolase;Mitochondrion;Nucleotide-binding;Protease;Reference proteome;Serine protease;Transit peptide |
| Interact With | P02666; Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:7961901}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (14); X-ray crystallography (5) |
| Cross Reference PDB | 2X36; 6WYS; 6WZV; 6X1M; 6X27; 7KRZ; 7KSL; 7KSM; 7NFY; 7NG4; 7NG5; 7NGC; 7NGF; 7NGL; 7NGP; 7NGQ; 7P09; 7P0B; 7P0M; |
| Mapped Pubmed ID | 14743216; 15683722; 17314511; 17342744; 17353931; 17584658; 18021745; 18174225; 18378094; 19615732; 20186120; 20562859; 20711500; 20877624; 20933102; 21163940; 21182203; 21347624; 21659532; 22623428; 22904065; 23201127; 23455922; 23788038; 23902751; 24255178; 24260536; 24344204; 24355201; 24414418; 24422629; 24565693; 25128872; 25525879; 25609649; 25675302; 25922169; 26314956; 26363553; 26496610; 26627475; 26638075; 27033304; 27108387; 27387767; 27764809; 28148925; 28160744; 28442264; 29178076; 29408517; 29518248; 29899330; 30061372; 30120231; 30304514; 31091208; 31100073; 31406245; 31756517; 31923470; 31987921; 32342250; 32475470; 33431889; 33547867; 33795807; 33821636; 34050165; 34190100; 34228963; 34400774; 34461102; 34547244; |
| Motif | |
| Gene Encoded By | |
| Mass | 106,489 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.53; |