OMA1 metalloendopeptidase [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

Official Symbol: OMA1
Official Full Name: metalloendopeptidase
Primary source: SGD:S000001795
Locus tag: YKR087C
See related: AllianceGenome:SGD:S000001795; FungiDB:YKR087C; VEuPathDB:YKR087C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables metalloendopeptidase activity. Involved in TOR signaling; cellular protein catabolic process; and response to redox state. Located in mitochondrial inner membrane. Orthologous to human OMA1 (OMA1 zinc metallopeptidase). [provided by Alliance of Genome Resources, Apr 2022]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

See OMA1 in Genome Data Viewer

Location:: chromosome: XI

Exon count:: 1

Sequence:: Chromosome: XI; NC_001143.9 (603195..604232, complement)

Chromosome XI - NC_001143.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001143.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The redox status of these cysteines may act as a redox-tunable switch to optimize Oma1 proteolytic function for specific cellular conditions or homeostatic challenges.
Title: Redox Regulation of the Mitochondrial Quality Control Protease Oma1.
Study shows that in Saccharomyces cerevisiae, inactivation of the membrane-bound intramitochondrial quality control protease Oma1 interferes with oxidative-stress responses through enhanced production of reactive oxygen species during logarithmic growth and reduced stress signaling via the TORC1-Rim15-Msn2/Msn4 axis.
Title: Oma1 Links Mitochondrial Protein Quality Control and TOR Signaling To Modulate Physiological Plasticity and Cellular Stress Responses.
yeast Oma1 is an important player in IM protein homeostasis and integrity by acting in concert with other intramitochondrial quality control components.
Title: Stress-triggered activation of the metalloprotease Oma1 involves its C-terminal region and is important for mitochondrial stress protection in yeast.
Specific Cox1 proteolysis in coa2Delta cells arises from a combination of Oma1 activation and a susceptible conformation of Cox1.
Title: Selective Oma1 protease-mediated proteolysis of Cox1 subunit of cytochrome oxidase in assembly mutants.

Submit: New GeneRIF Correction

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables metalloendopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metalloendopeptidase activity	IEA Inferred from Electronic Annotation more info
enables metalloendopeptidase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables metallopeptidase activity	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in TOR signaling	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitochondrial protein catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitochondrial protein processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein quality control for misfolded or incompletely synthesized proteins	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein quality control for misfolded or incompletely synthesized proteins	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in mitochondrial inner membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrial inner membrane	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial inner membrane	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: metalloendopeptidase

NP_013013.2

Metalloendopeptidase of the mitochondrial inner membrane; important for adaptive responses to various homeostatic insults, preservation of normal mitochondrial function under damage-eliciting conditions, and stability of respiratory supercomplexes; involved in turnover of membrane-embedded proteins; mediates degradation of Cox1p in coa2 mutant cells; zebrafish ortholog has a role in organ development and mouse ortholog is also required for respiratory supercomplex stability

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001143.9 Reference assembly

Range

603195..604232 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179877.1 → NP_013013.2 TPA: metalloendopeptidase [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013013.2

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VXE7, P36163

UniProtKB/TrEMBL

A7A046, B3LRG1, B5VMM9, C7GXC3, C8ZCP8, G2WIB4, N1NZK4

Conserved Domains (1) summary

cd07331
Location:132 → 323

M48C_Oma1_like; Peptidase M48C, integral membrane endopeptidase