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OMA1 information


OMA1
Identifiers
AliasesOMA1, 2010001O09Rik, DAB1, MPRP-1, YKR087C, ZMPpeptidase, OMA1 zinc metallopeptidase, MPRP1
External IDsOMIM: 617081 MGI: 1914263 HomoloGene: 12070 GeneCards: OMA1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_145243

NM_025909

RefSeq (protein)

NP_660286

NP_080185

Location (UCSC)Chr 1: 58.42 – 58.55 MbChr 4: 103.17 – 103.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000162600 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035069 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: OMA1 zinc metallopeptidase".
  6. ^ a b Kaser 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.
  7. ^ 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.
  8. ^ 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.
  9. ^ 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.
  10. ^ 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.

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OMA1

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Metalloendopeptidase OMA1, mitochondrial is an enzyme that in humans is encoded by the OMA1 gene. OMA1 is a Zn2+-dependent metalloendopeptidase in the...

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Chromosome 1

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protein 9 NRAS (1p13) NOTCH2 (1p12) OLFML3: Olfactomedin-like 3 OMA1: Metalloendopeptidase OMA1, mitochondrial OVGP1: Oviductal glycoprotein 1 PARK7 (1p36):...

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YME1L1

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the dynamin-like GTPase optic atrophy 1 (OPA1) Loss of YME1L1 accelerates OMA1-dependent long-form OPA1 cleavage, resulting in short-form OPA1 accumulation...

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independent of interferon production. The UQCC3 protein can be cleaved by OMA1 metalloprotease during mitochondrial depolarization, targeting the cell for...

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