Primary Information |
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| BoMiProt ID | Bomi7034 |
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| Protein Name | Metalloendopeptidase OMA1, mitochondrial/Overlapping with the m-AAA protease 1 homolog |
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| Organism | Bos taurus |
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| Uniprot ID | Q3SZN3 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001030205.1 |
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| Aminoacid Length | 523 |
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| Molecular Weight | 59896 |
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| FASTA Sequence |
Download |
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| Gene Name | OMA1 |
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| Gene ID | 506223 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | OMA1 is a mitochondrial protease. Among its substrates are DELE1, a signaling peptide, which can elicit the integrated stress response, as well as the membrane-shaping dynamin-related GTPase OPA1, which can drive mitochondrial outer membrane permeabilization. |
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| Biochemical Properties | OMA1 cleaves OPA1 at the S1 cleavage site after arginine 194. The i-AAA protease cleaves at the S2 cleavage site anywhere between 14 and 53 amino acids further downstream of S1. |
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| PTMs | Autocatalytic cleavage, Disulfide bond and Zymogen formation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH; (195-213) |
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| Significance of PTMs | 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 447-456. The S-OMA1 form is unstable. Degradaded by YMEL1 in response to membrane depolarization. Protein turnover is regulated by prohibitin (PHB and PHB2), which promotes degradation of OMA1 in a cardiolipin-binding manner. |
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| Additional Comments | OMA1 was found to be activated in a number of disease conditions, including cancer and neurodegeneration. |
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| Bibliography | Alavi MV. OMA1-An integral membrane protease? Biochim Biophys Acta Proteins Proteom. 2021 Feb;1869(2):140558. doi: 10.1016/j.bbapap.2020.140558. Epub 2020 Oct 29. PMID: 33130089; PMCID: PMC7770061. 2.N. Ishihara, Y. Fujita, T. Oka, K. Mihara, Regulation of mitochondrial morphology through
proteolytic cleavage of OPA1, EMBO J 25 (2006) 2966-2977. 3.Z. Song, H. Chen, M. Fiket, C. Alexander, D.C. Chan, OPA1 processing controls
mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and
Yme1L, J Cell Biol 178 (2007) 749-755. |
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