Search by BoMiProt ID - Bomi7034

Primary Information

BoMiProt ID Bomi7034
Protein Name Metalloendopeptidase OMA1, mitochondrial/Overlapping with the m-AAA protease 1 homolog
Organism Bos taurus
Uniprot IDQ3SZN3
Milk FractionWhey
Ref Sequence ID NP_001030205.1
Aminoacid Length 523
Molecular Weight 59896
FASTA Sequence Download
Gene Name OMA1
Gene ID 506223
Protein Existence Status reviewed

Secondary Information

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.
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.
PTMs Autocatalytic cleavage, Disulfide bond and Zymogen formation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction 1TMH; (195-213)
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.
Additional Comments OMA1 was found to be activated in a number of disease conditions, including cancer and neurodegeneration.
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.