Oma1
entrez
298282
canonical
uniprot
D3ZS74
canonical
ensembl
ENSRNOG00000007214
resolver
ensp
ENSRNOP00000009515
resolver
ensp
ENSRNOP00000100728
resolver
enst
ENSRNOT00000009516
resolver
enst
ENSRNOT00000128078
resolver
genesymbol
Oma1
resolver
uniprot
A0ABK0L791
resolver
uniprot_entry
A0ABK0L791_RAT
resolver
uniprot_entry
OMA1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Protease activity is activated upon autocatalytic cleavage in response to mitochondrial depolarization. {ECO:0000250|UniProtKB:Q9D8H7}.
uniprot
proteins
amino_acid_sequence
MNFLYGLQSATRNQFLSGVNTLARRRTWTPPAGCPLASRLPAVNANWGLSTVSHCYSVILLPRNLHFCRTLKNKRSRCLSSAQSKEMGVLTYNWTVWGDASCSPNYAAIREVRSFHTSAPRQAAPVPLLMLILKPVQKLLAIIVGRGIRKWWQALPPDKKALFKDSVKRNKWRLLLGLSAFGLLFVVFYFTHLEVSPVTGRSKLLLVGKEHFRLLSDLEYEVWMEEFKNDLLPEEDPRYLTVKKVVYHLTQCNQDVPGVSEINWVVHVVHSPKVNAFVLPNGQVFVFTGLLNSVTDMHQLSFLLGHEIAHAVLGHAAEKASLVHLLDFLGMIFLTMIWAICPRDSLAVLGQWIQSKLQEYMFDRPYSRTLEAEADKIGLQLAAKACVDVRASSVFWQQMEFSESLHGYPKLPEWLSTHPSHGNRAEYLDRLIPQALKLREVCNCPPLSGPDPRLLFRLTVKHLLEDSEKEDLNITVKKQKPDALPIQKQEQIPLTYALGKRTAG
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Metalloprotease that is part of the quality control system in the inner membrane of mitochondria (PubMed:30926535). Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1 (PubMed:30926535). 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). Involved in mitochondrial safeguard in response to transient mitochondrial membrane depolarization (flickering) by catalyzing cleavage of OPA1, leading to excess production of S-OPA1, preventing mitochondrial hyperfusion (By similarity). Also acts as a regulator of apoptosis: upon BAK and BAX aggregation, mediates cleavage of OPA1, leading to the remodeling of mitochondrial cristae and allowing the release of cytochrome c from mitochondrial cristae (By similarity). In depolarized mitochondria, may also act as a backup protease for PINK1 by mediating PINK1 cleavage and promoting its subsequent degradation by the proteasome (By similarity). May also cleave UQCC3 in response to mitochondrial depolarization (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). Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions (By similarity). Binds cardiolipin, possibly regulating its protein turnover (By similarity). Required for the stability of the respiratory supercomplexes (By similarity). {ECO:0000250|UniProtKB:Q96E52, ECO:0000250|UniProtKB:Q9D8H7, ECO:0000269|PubMed:30926535}.
uniprot
proteins
mass_dalton
57145
uniprot
proteins
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). Autocatalytic processing at the C-terminus takes place at residues 426-435. The S-OMA1 form is unstable (By similarity). OMA1 pre-processing by AFG3L2 may participate in maturation before OMA1 autocatalytic cleavage (By similarity). Degraded by YMEL1 in response to membrane depolarization (By similarity). Protein turnover is regulated by prohibitin (PHB and PHB2), which promotes degradation of OMA1 in a cardiolipin-binding manner (By similarity). {ECO:0000250|UniProtKB:Q96E52, 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}.
uniprot
proteins
protein_family
Peptidase M48 family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
30926535
uniprot
proteins
sequence_length
504
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9D8H7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D8H7}.
uniprot
proteins
transmembrane_region
TRANSMEM 175..195; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins