LONP1 — Lon peptidase 1, mitochondrial
LONP1 belongs to a gene co-expression module in 1 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
LONP1's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Macrophages | Phagocytic Endolysosomal Lysosomal & pahgocytosis | ABHD2, ACTN4, AP3S1, ARF6, ATP6V1B2, CD151, CERS2, CNIH1 +27 more | View in SCUBA |
About the gene
| Synonyms | hLON, LonHS, PIM1, PRSS15 |
|---|---|
| Chromosome | 19: 5691834-5720572 |
| Predicted location | Intracellular |
| Essential gene | Yes |
| Protein class | Disease related genes, Enzymes, Essential proteins, Human disease related genes, Potential drug targets, Predicted intracellular proteins |
| Molecular function | DNA-binding, Hydrolase, Protease, Serine protease |
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. Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein, DELE1, helicase Twinkle (TWNK) and the large ribosomal subunit protein MRPL32/bL32m. MRPL32/bL32m is protected from degradation by LONP1 when it is bound to a nucleic acid (RNA), but TWNK is not. May also have a chaperone function in the assembly of inner membrane protein complexes (By similarity). 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.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.