| IED ID | IndEnz0002006688 |
| Enzyme Type ID | protease006688 |
| Protein Name |
Metalloendopeptidase OMA1, mitochondrial zfoma1 EC 3.4.24.- Overlapping with the m-AAA protease 1 homolog |
| Gene Name | oma1 si:ch73-215a11.1 |
| Organism | Danio rerio (Zebrafish) (Brachydanio rerio) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio) |
| Enzyme Sequence | MQQTCIRLVKLDMLSTLTRFRTHSAIRCCAQRLFHCRPSLFISARTYFIKIDSSSLPKLKGSVSFSASCVSLGSSRLGLCSSSFKTGAPAALRAPVVFQRTRGFHTSGRRRALPALPLLWMVLKPLQKIMAIILGRSIRKWWVALPANKKQLFREWSWRRRWHFLGAGTGLLFIASLFFFTHLDESPITGRTRLLVFSRKNFRELAQFNADAFMEEFKDSLIASSDPRHKVVEQVVQILAQRNQDIAEISAVPWTVHVVDSPTMNAFVLPNGEIFVFTGMLNAVTDIHQLTFILGHEMAHALIGHAAEQASLSHVVELLSLVLLTAIWAVCPRDSLAALGHWIQGKLVQFLFDRPFSRKLEAEADQVGLQMAAKACADVRAGPVFWEQMEIFDQLSGQPTMPEWLSTHPSHQNRVRQLDRLIPEALELRARCNCPELPKTDPRVVFNEAVRLVLEGKKEQMLEKEEKNGKTQTGDMFP |
| Enzyme Length | 478 |
| Uniprot Accession Number | E9QBI7 |
| Absorption | |
| Active Site | ACT_SITE 297; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Protease activity is activated upon autocatalytic cleavage in response to mitochondrial depolarization. {ECO:0000250|UniProtKB:Q9D8H7}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as opa1 and dele1. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of opa1 at S1 position, leading to opa1 inactivation and negative regulation of mitochondrial fusion (By similarity). Also acts as an activator of the integrated stress response (ISR): in response to mitochondrial stress, mediates cleavage of dele1 to generate the processed form of dele1 (S-DELE1), which translocates to the cytosol and activates eif2ak1/hri to trigger the ISR (By similarity). Required for the stability of the respiratory supercomplexes (PubMed:26365306). {ECO:0000250|UniProtKB:Q96E52, ECO:0000250|UniProtKB:Q9D8H7, ECO:0000269|PubMed:26365306}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Metal binding (3); Propeptide (2); Region (1); Topological domain (2); Transit peptide (1); Transmembrane (1) |
| Keywords | Autocatalytic cleavage;Disulfide bond;Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Protease;Reference proteome;Transit peptide;Transmembrane;Transmembrane helix;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9D8H7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D8H7}. |
| Modified Residue | |
| Post Translational Modification | PTM: Autocatalytically cleaved in response to mitochondrial depolarization both at the N-terminus and C-terminus to generate the short active form (S-OMA1). The S-OMA1 form is unstable. {ECO:0000250|UniProtKB:Q9D8H7}.; PTM: May form a redox-dependent disulfide bond (By similarity). Exists in a semi-oxidized state and is activated by prolonged hypoxia (By similarity). {ECO:0000250|UniProtKB:P36163, ECO:0000250|UniProtKB:Q96E52}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 54,050 |
| Kinetics | |
| Metal Binding | METAL 296; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 300; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 361; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |