OMA1
| OMA1 | ||||||
|---|---|---|---|---|---|---|
| Identifiers | ||||||
| Aliases | OMA1, 2010001O09Rik, DAB1, MPRP-1, YKR087C, ZMPpeptidase, OMA1 zinc metallopeptidase | |||||
| External IDs | MGI: 1914263 HomoloGene: 12070 GeneCards: OMA1 | |||||
| Orthologs | ||||||
| Species | Human | Mouse | ||||
| Entrez | ||||||
| Ensembl | ||||||
| UniProt | ||||||
| RefSeq (mRNA) | ||||||
| RefSeq (protein) | ||||||
| Location (UCSC) | Chr 1: 58.42 – 58.55 Mb | Chr 4: 103.31 – 103.37 Mb | ||||
| PubMed search | [1] | [2] | ||||
| Wikidata | ||||||
| View/Edit Human | View/Edit Mouse |
Metalloendopeptidase OMA1, mitochondrial is an enzyme that in humans is encoded by the OMA1 gene.[3][4] As a Metalloprotease, this protein is a substantial component of the quality control system in the inner membrane of mitochondria. Being activated by enzyme Bax and Bak, mitochondrial protease OMA1 promotes cytochrome c release which subsequently induces apoptosis.[5]
Structure
Gene
The gene OMA1 encodes a metalloprotease, a founding member of a conserved family of membrane-embedded metallopeptidases in mitochondria. The human gene has 9 exons and locates at chromosome band 1p32.2-p32.1
Protein
The human protein Metalloendopetidase OMA1, mitochondrial is 60 kDa in size and composed of 524 amino acids. The peptide fragment 1-13 is mitochondrial transition peptide, the mature protein has a theoretical PI of 9.35.[6]
Function
The inner membrane of mitochondrial houses two AAA proteases and these membrane-embedded peptidases were termed m- and i-AAA proteases to indicate their different topology in the inner membrane. The m-AAA protease is facing the matrix and the i-AAA protease is facing the intermembrane space. OMA1 was shown to share an overlapping proteolytic activity with m-AAA protease. However, OMA1 doesn't completely regulate the turnover of a model substrate, Oxa1, as what the m-AAA protease does. On the contrary, Oma1 only generates N- and C-terminal proteolytic fragments.[4] Recent study showed that the mammalian mitochondrial inner membrane fusion protein OPA1 can be degraded by OMA1 when mitochondria lose membrane potential or adenosine triphosphate. Such inducible proteolysis acts as a regulatory mechanism to proteolytically inactivate of OPA1, thus preventing the fusion of the mitochondrial network.[7][8][9]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ "Entrez Gene: OMA1 zinc metallopeptidase".
- 1 2 Kaser, M; Kambacheld, M; Kisters-Woike, B; Langer, T (21 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.
- ↑ Jiang, X; Jiang, H; Shen, Z; Wang, X (14 October 2014). "Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis.". Proceedings of the National Academy of Sciences of the United States of America. 111 (41): 14782–7. doi:10.1073/pnas.1417253111. PMID 25275009.
- ↑ "Uniprot: Q96E52 - OMA1_HUMAN".
- ↑ Head, B; Griparic, L; Amiri, M; Gandre-Babbe, S; van der Bliek, AM (28 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. PMID 20038677.
- ↑ Ehses, S; Raschke, I; Mancuso, G; Bernacchia, A; Geimer, S; Tondera, D; Martinou, JC; Westermann, B; Rugarli, EI; Langer, T (28 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. PMID 20038678.
- ↑ McBride, H; Soubannier, V (23 March 2010). "Mitochondrial function: OMA1 and OPA1, the grandmasters of mitochondrial health.". Current Biology. 20 (6): R274–6. doi:10.1016/j.cub.2010.02.011. PMID 20334834.