Oma1 OMA1 zinc metallopeptidase [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Oma1provided by RGD
Official Full Name: OMA1 zinc metallopeptidaseprovided by RGD
Primary source: RGD:1304821
See related: EnsemblRapid:ENSRNOG00000007214 AllianceGenome:RGD:1304821
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: RGD1304821
Summary: Enables metalloendopeptidase activity. Predicted to be involved in several processes, including HRI-mediated signaling; protein processing; and regulation of mitochondrion organization. Predicted to act upstream of or within cristae formation. Predicted to be located in mitochondrial membrane. Predicted to be active in mitochondrial inner membrane and mitochondrial intermembrane space. Orthologous to human OMA1 (OMA1 zinc metallopeptidase). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Biased expression in Kidney (RPKM 88.4), Muscle (RPKM 86.3) and 9 other tissues See more
Orthologs: human mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 5q33

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	5	NC_086023.1 (123312038..123455540)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	5	NC_051340.1 (118083728..118136980)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	5	NC_005104.4 (122847624..122900475)

Chromosome 5 - NC_086023.1 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:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Mitochondrial OPA1 cleavage is reversibly activated by differentiation of H9c2 cardiomyoblasts.
Title: Mitochondrial OPA1 cleavage is reversibly activated by differentiation of H9c2 cardiomyoblasts.

Submit: New GeneRIF Correction

General gene information

Go to the top of the page Help

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables lipid binding	IEA Inferred from Electronic Annotation more info
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	IDA Inferred from Direct Assay more info	PubMed
enables metalloendopeptidase activity	IEA Inferred from Electronic Annotation more info
enables metalloendopeptidase activity	ISO Inferred from Sequence Orthology more info
enables metalloendopeptidase activity	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in HRI-mediated signaling	ISO Inferred from Sequence Orthology more info
involved_in HRI-mediated signaling	ISS Inferred from Sequence or Structural Similarity more info
involved_in cellular response to stress	ISO Inferred from Sequence Orthology more info
involved_in cristae formation	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within cristae formation	ISO Inferred from Sequence Orthology more info
involved_in diet induced thermogenesis	IEA Inferred from Electronic Annotation more info
involved_in diet induced thermogenesis	ISO Inferred from Sequence Orthology more info
involved_in diet induced thermogenesis	ISS Inferred from Sequence or Structural Similarity more info
involved_in energy homeostasis	ISO Inferred from Sequence Orthology more info
involved_in energy homeostasis	ISS Inferred from Sequence or Structural Similarity more info
involved_in glucose metabolic process	IEA Inferred from Electronic Annotation more info
involved_in glucose metabolic process	ISO Inferred from Sequence Orthology more info
involved_in glucose metabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in integrated stress response signaling	ISO Inferred from Sequence Orthology more info
involved_in integrated stress response signaling	ISS Inferred from Sequence or Structural Similarity more info
involved_in lipid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in lipid metabolic process	ISO Inferred from Sequence Orthology more info
involved_in lipid metabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in mitochondrial protein processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in mitochondrial protein processing	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within mitochondrial protein processing	ISO Inferred from Sequence Orthology more info
involved_in mitochondrial protein processing	ISO Inferred from Sequence Orthology more info
involved_in mitochondrial protein processing	ISS Inferred from Sequence or Structural Similarity more info
involved_in mitochondrial respiratory chain complex assembly	IEA Inferred from Electronic Annotation more info
involved_in mitochondrial respiratory chain complex assembly	ISO Inferred from Sequence Orthology more info
involved_in mitochondrial respiratory chain complex assembly	ISS Inferred from Sequence or Structural Similarity more info
acts_upstream_of_or_within mitochondrion organization	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of mitochondrial fusion	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of mitochondrial fusion	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of mitochondrial fusion	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of apoptotic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of cold-induced thermogenesis	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of cold-induced thermogenesis	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of cold-induced thermogenesis	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in protein autoprocessing	IEA Inferred from Electronic Annotation more info
involved_in protein autoprocessing	ISO Inferred from Sequence Orthology more info
involved_in protein autoprocessing	ISS Inferred from Sequence or Structural Similarity 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	ISO Inferred from Sequence Orthology more info
involved_in protein quality control for misfolded or incompletely synthesized proteins	ISS Inferred from Sequence or Structural Similarity more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in regulation of cristae formation	ISO Inferred from Sequence Orthology more info
involved_in regulation of cristae formation	ISS Inferred from Sequence or Structural Similarity more info
involved_in zymogen activation	IEA Inferred from Electronic Annotation more info
involved_in zymogen activation	ISO Inferred from Sequence Orthology more info
involved_in zymogen activation	ISS Inferred from Sequence or Structural Similarity 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	IEA Inferred from Electronic Annotation more info
located_in mitochondrial inner membrane	ISO Inferred from Sequence Orthology more info
located_in mitochondrial inner membrane	ISS Inferred from Sequence or Structural Similarity more info
is_active_in mitochondrial intermembrane space	ISO Inferred from Sequence Orthology more info
located_in mitochondrial membrane	ISO Inferred from Sequence Orthology more info
located_in mitochondrial membrane	ISS Inferred from Sequence or Structural Similarity more info
located_in mitochondrion	ISO Inferred from Sequence Orthology more info

General protein information

Go to the top of the page Help

Preferred Names: metalloendopeptidase OMA1, mitochondrial

Names: OMA1 homolog, zinc metallopeptidase; overlapping with the m-AAA protease 1 homolog; zinc metallopeptidase homolog

NP_001100139.1

EC 3.4.24.-

XP_063143450.1

EC 3.4.24.-

XP_063143451.1

EC 3.4.24.-

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001106669.1 → NP_001100139.1 metalloendopeptidase OMA1, mitochondrial

See identical proteins and their annotated locations for NP_001100139.1

Status: PROVISIONAL

Source sequence(s)

CH473998

UniProtKB/Swiss-Prot

D3ZS74

UniProtKB/TrEMBL

A0A8L2Q3X0

Conserved Domains (2) summary

COG0501
Location:264 → 434

HtpX; Zn-dependent protease with chaperone function [Posttranslational modification, protein turnover, chaperones]

pfam01435
Location:258 → 432

Peptidase_M48; Peptidase family M48