Oma1
entrez
67013
canonical
uniprot
Q9D8H7
canonical
ensembl
ENSMUSG00000035069
resolver
ensp
ENSMUSP00000045269
resolver
ensp
ENSMUSP00000242564
resolver
ensp
ENSMUSP00000242567
resolver
ensp
ENSMUSP00000242568
resolver
ensp
ENSMUSP00000242569
resolver
ensp
ENSMUSP00000242571
resolver
ensp
ENSMUSP00000242574
resolver
ensp
ENSMUSP00000242575
resolver
ensp
ENSMUSP00000242583
resolver
ensp
ENSMUSP00000242590
resolver
ensp
ENSMUSP00000242592
resolver
ensp
ENSMUSP00000242593
resolver
ensp
ENSMUSP00000340925
resolver
ensp
ENSMUSP00000360048
resolver
genesymbol
Oma1
resolver
uniprot
Q3UWN9
resolver
uniprot_entry
OMA1_MOUSE
resolver
uniprot_sec
Q3UWN9
resolver
activity_regulation
ACTIVITY REGULATION: Protease activity is activated upon autocatalytic cleavage in response to mitochondrial depolarization. {ECO:0000269|PubMed:24550258, ECO:0000269|PubMed:24719224}.
uniprot
proteins
amino_acid_sequence
MSLLYGLQSTRINRFLSGVNNLANRRQWTPPASCPLAPKLRAVNAYWGLNTVSHCHSVTLLPRNFLFCRTLNHKKSRCLSSAQSKELGVLTYRCTVRGDSVLRQGARKVAGVPALAASCSPSCPAVIEARSFRTSARVQAAPVPLLLLILKPVQKLLAIIVGRGIRKWWQALPPNKKELFKDSVRKNKWRLLLGLSAFGLLFVVFYFTHLEVSPVTGRSKLLLVGKEHFRLLSDLEYEVWMEEFKNDLLPERDPRYLTVKEMVYHLTQCNRDVPGISETNWVVHVVDSPAVNAFVLPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEKASLVHLLDFLGMIFLTMIWAICPRDSLAVLGQWIQSKLQEYMFDRPYSRTLEAEADKVGLQLAAKACADVRASSVFWQQMEFSESLHGYPKLPEWLSTHPSHGNRAEYLDRLIPQALKLREVCNCPPLSGPDPRLLFRLTVKRFLEDSEKEDLNITVKKQKTDALPMQKQEQIPLTYVLEKRTAG
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:20038678, PubMed:22433842, PubMed:24550258, PubMed:24616225, PubMed:24719224, PubMed:26785494). Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1 (PubMed:20038678, PubMed:22433842, PubMed:24550258, PubMed:24616225, PubMed:26785494). 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 (PubMed:20038678, PubMed:24616225). 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 (PubMed:22433842, PubMed:24550258, PubMed:26783299, PubMed:26785494). 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 (PubMed:33200421). 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 (PubMed:22433842). Binds cardiolipin, possibly regulating its protein turnover (PubMed:31819158). Required for the stability of the respiratory supercomplexes (PubMed:26365306). {ECO:0000250|UniProtKB:Q96E52, ECO:0000269|PubMed:20038678, ECO:0000269|PubMed:22433842, ECO:0000269|PubMed:24550258, ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:24719224, ECO:0000269|PubMed:26365306, ECO:0000269|PubMed:26783299, ECO:0000269|PubMed:26785494, ECO:0000269|PubMed:31819158, ECO:0000269|PubMed:33200421}.
uniprot
proteins
mass_dalton
58878
uniprot
proteins
mutagenesis
MUTAGEN 324; /note="E->Q: Abolished protease activity and ability to cleave OPA1. Abolished autocatalytic processing."; /evidence="ECO:0000269|PubMed:24550258, ECO:0000269|PubMed:24719224
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) (PubMed:24550258, PubMed:24719224). Autocatalytic processing at the C-terminus takes place at residues 443-452 (PubMed:24719224). The S-OMA1 form is unstable (PubMed:24719224). 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 (PubMed:31819158). {ECO:0000250|UniProtKB:Q96E52, ECO:0000269|PubMed:24550258, ECO:0000269|PubMed:24719224, ECO:0000269|PubMed:31819158}.; 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
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20038678
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22433842
uniprot
proteins
pubmed
24550258
uniprot
proteins
pubmed
24616225
uniprot
proteins
pubmed
24719224
uniprot
proteins
pubmed
26365306
uniprot
proteins
pubmed
26783299
uniprot
proteins
pubmed
26785494
uniprot
proteins
pubmed
29593106
uniprot
proteins
pubmed
31819158
uniprot
proteins
pubmed
33200421
uniprot
proteins
sequence_length
521
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:24550258, ECO:0000305|PubMed:20038678}; Single-pass membrane protein {ECO:0000305|PubMed:24550258}.
uniprot
proteins
transmembrane_region
TRANSMEM 192..212; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins