protein quality control for misfolded or incompletely synthesized proteins
negative regulation of mitochondrial fusion
proteolysis
lipid metabolism
glucose metabolic process
diet induced thermogenesis
regulation of apoptotic process
positive regulation of cold-induced thermogenesis
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
115209
67013
Ensembl
ENSG00000162600
ENSMUSG00000035069
UniProt
Q96E52
Q9D8H7
RefSeq (mRNA)
NM_145243
NM_025909
RefSeq (protein)
NP_660286
NP_080185
Location (UCSC)
Chr 1: 58.42 – 58.55 Mb
Chr 4: 103.17 – 103.23 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Metalloendopeptidase OMA1, mitochondrial is an enzyme that in humans is encoded by the OMA1 gene.[5][6] OMA1 is a Zn2+-dependent metalloendopeptidase in the inner membrane of mitochondria. The OMA1 acronym was derived from overlapping proteolytic activity with m-AAA protease 1.[6]
The OMA1 protease acts at the intersection of a mitochondrial quality control system and energy metabolism, whereby its activation correlates with outer membrane permeabilization and cytochrome c release in the context of apoptosis.
Mammalian OMA1 can cleave the inner-membrane shaping protein OPA1 and the signaling peptide DELE1 in a context-dependent manner.[7][8][9][10]
^ abcGRCh38: Ensembl release 89: ENSG00000162600 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000035069 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Entrez Gene: OMA1 zinc metallopeptidase".
^ abKaser M, Kambacheld M, Kisters-Woike B, Langer T (November 2003). "Oma1, a novel membrane-bound metallopeptidase in mitochondria with activities overlapping with the m-AAA protease". The Journal of Biological Chemistry. 278 (47): 46414–23. doi:10.1074/jbc.m305584200. PMID 12963738.
^Ehses S, Raschke I, Mancuso G, Bernacchia A, Geimer S, Tondera D, et al. (December 2009). "Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1". The Journal of Cell Biology. 187 (7): 1023–36. doi:10.1083/jcb.200906084. PMC 2806285. PMID 20038678.
^Head B, Griparic L, Amiri M, Gandre-Babbe S, van der Bliek AM (December 2009). "Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells". The Journal of Cell Biology. 187 (7): 959–66. doi:10.1083/jcb.200906083. PMC 2806274. PMID 20038677.
^Guo X, Aviles G, Liu Y, Tian R, Unger BA, Lin YT, et al. (March 2020). "Mitochondrial stress is relayed to the cytosol by an OMA1-DELE1-HRI pathway". Nature. 579 (7799): 427–432. Bibcode:2020Natur.579..427G. doi:10.1038/s41586-020-2078-2. PMC 7147832. PMID 32132707.
^Fessler E, Eckl EM, Schmitt S, Mancilla IA, Meyer-Bender MF, Hanf M, et al. (March 2020). "A pathway coordinated by DELE1 relays mitochondrial stress to the cytosol". Nature. 579 (7799): 433–437. Bibcode:2020Natur.579..433F. doi:10.1038/s41586-020-2076-4. PMC 7116715. PMID 32132706.
Metalloendopeptidase OMA1, mitochondrial is an enzyme that in humans is encoded by the OMA1 gene. OMA1 is a Zn2+-dependent metalloendopeptidase in the...
the dynamin-like GTPase optic atrophy 1 (OPA1) Loss of YME1L1 accelerates OMA1-dependent long-form OPA1 cleavage, resulting in short-form OPA1 accumulation...
independent of interferon production. The UQCC3 protein can be cleaved by OMA1 metalloprotease during mitochondrial depolarization, targeting the cell for...