E9QBI7 · OMA1_DANRE
- ProteinMetalloendopeptidase OMA1, mitochondrial
- Geneoma1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids478 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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 (By similarity).
Involved in the fusion of the mitochondrial inner membranes by mediating cleavage of opa1 at S1 position, generating the soluble opa1 (S-opa1), which cooperates with the membrane form (L-opa1) to coordinate the fusion of mitochondrial inner membranes (By similarity).
Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of opa1, leading to excess production of soluble opa1 (S-opa1) 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).
Involved in the fusion of the mitochondrial inner membranes by mediating cleavage of opa1 at S1 position, generating the soluble opa1 (S-opa1), which cooperates with the membrane form (L-opa1) to coordinate the fusion of mitochondrial inner membranes (By similarity).
Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of opa1, leading to excess production of soluble opa1 (S-opa1) 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).
Cofactor
Note: Binds 1 zinc ion per subunit.
Activity regulation
Protease activity is activated upon autocatalytic cleavage in response to mitochondrial depolarization.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial membrane | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | diet induced thermogenesis | |
Biological Process | energy homeostasis | |
Biological Process | glucose metabolic process | |
Biological Process | HRI-mediated signaling | |
Biological Process | integrated stress response signaling | |
Biological Process | lipid metabolic process | |
Biological Process | mitochondrial protein processing | |
Biological Process | mitochondrial respiratory chain complex assembly | |
Biological Process | negative regulation of mitochondrial fusion | |
Biological Process | positive regulation of apoptotic process | |
Biological Process | protein autoprocessing | |
Biological Process | protein quality control for misfolded or incompletely synthesized proteins | |
Biological Process | regulation of cristae formation | |
Biological Process | zymogen activation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMetalloendopeptidase OMA1, mitochondrial
- EC number
- Short nameszfoma1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionE9QBI7
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | ?-162 | Mitochondrial matrix | ||||
Sequence: MQQTCIRLVKLDMLSTLTRFRTHSAIRCCAQRLFHCRPSLFISARTYFIKIDSSSLPKLKGSVSFSASCVSLGSSRLGLCSSSFKTGAPAALRAPVVFQRTRGFHTSGRRRALPALPLLWMVLKPLQKIMAIILGRSIRKWWVALPANKKQLFREWSWRRRW | ||||||
Transmembrane | 163-183 | Helical | ||||
Sequence: HFLGAGTGLLFIASLFFFTHL | ||||||
Topological domain | 184-? | Mitochondrial intermembrane | ||||
Sequence: MQQTCIRLVKLDMLSTLTRFRTHSAIRCCAQRLFHCRPSLFISARTYFIKIDSSSLPKLKGSVSFSASCVSLGSSRLGLCSSSFKTGAPAALRAPVVFQRTRGFHTSGRRRALPALPLLWMVLKPLQKIMAIILGRSIRKWWVALPANKKQLFREWSWRRRWHFLGAGTGLLFIASLFFFTHL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for propeptide, transit peptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000450319 | ?-111 | ||||
Sequence: MQQTCIRLVKLDMLSTLTRFRTHSAIRCCAQRLFHCRPSLFISARTYFIKIDSSSLPKLKGSVSFSASCVSLGSSRLGLCSSSFKTGAPAALRAPVVFQRTRGFHTSGRRR | ||||||
Propeptide | PRO_0000450320 | ?-478 | ||||
Sequence: MQQTCIRLVKLDMLSTLTRFRTHSAIRCCAQRLFHCRPSLFISARTYFIKIDSSSLPKLKGSVSFSASCVSLGSSRLGLCSSSFKTGAPAALRAPVVFQRTRGFHTSGRRRALPALPLLWMVLKPLQKIMAIILGRSIRKWWVALPANKKQLFREWSWRRRWHFLGAGTGLLFIASLFFFTHLDESPITGRTRLLVFSRKNFRELAQFNADAFMEEFKDSLIASSDPRHKVVEQVVQILAQRNQDIAEISAVPWTVHVVDSPTMNAFVLPNGEIFVFTGMLNAVTDIHQLTFILGHEMAHALIGHAAEQASLSHVVELLSLVLLTAIWAVCPRDSLAALGHWIQGKLVQFLFDRPFSRKLEAEADQVGLQMAAKACADVRAGPVFWEQMEIFDQLSGQPTMPEWLSTHPSHQNRVRQLDRLIPEALELRARCNCPELPKTDPRVVFNEAVRLVLEGKKEQMLEKEEKNGKTQTGDMFP | ||||||
Transit peptide | 1-? | Mitochondrion | ||||
Chain | PRO_0000417520 | 112-? | Metalloendopeptidase OMA1, mitochondrial | |||
Sequence: MQQTCIRLVKLDMLSTLTRFRTHSAIRCCAQRLFHCRPSLFISARTYFIKIDSSSLPKLKGSVSFSASCVSLGSSRLGLCSSSFKTGAPAALRAPVVFQRTRGFHTSGRRR | ||||||
Disulfide bond | 376↔434 | |||||
Sequence: CADVRAGPVFWEQMEIFDQLSGQPTMPEWLSTHPSHQNRVRQLDRLIPEALELRARCNC |
Post-translational modification
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.
May form a redox-dependent disulfide bond (By similarity).
Exists in a semi-oxidized state and is activated by prolonged hypoxia (By similarity).
Exists in a semi-oxidized state and is activated by prolonged hypoxia (By similarity).
Keywords
- PTM
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 134-164 | Stress-sensor region | ||||
Sequence: LGRSIRKWWVALPANKKQLFREWSWRRRWHF |
Domain
The stress-sensor region regulates proteolysis and activation.
Sequence similarities
Belongs to the peptidase M48 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length478
- Mass (Da)54,050
- Last updated2011-04-05 v1
- Checksum7FE406BD2CBFB963
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8M9P2W7 | A0A8M9P2W7_DANRE | oma1 | 510 |
Keywords
- Technical term