PIM1 ATP-dependent Lon protease PIM1 [Saccharomyces cerevisiae S288C] - Gene

Summary

Official Symbol: PIM1
Official Full Name: ATP-dependent Lon protease PIM1
Primary source: SGD:S000000118
Locus tag: YBL022C
See related: AllianceGenome:SGD:S000000118; FungiDB:YBL022C; VEuPathDB:YBL022C
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 ATP-dependent peptidase activity. Involved in chaperone-mediated protein complex assembly; protein quality control for misfolded or incompletely synthesized proteins; and regulation of mitochondrial DNA metabolic process. Located in mitochondrial matrix. Human ortholog(s) of this gene implicated in CODAS syndrome. Orthologous to human LONP1 (lon peptidase 1, mitochondrial). [provided by Alliance of Genome Resources, Dec 2024]
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Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Go to nucleotide: Graphics FASTA GenBank

Differential sensitivity of the yeast Lon protease Pim1p to impaired mitochondrial respiration.
Title: Differential sensitivity of the yeast Lon protease Pim1p to impaired mitochondrial respiration.
analysis of the nature of oxidized protein substrates and physiological partners of Pim1 protease under non-repressing growth conditions
Title: Identification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1.
The Pim1-specific ATP-dependent proteolysis of the newly identified substrate proteins was confirmed.
Title: Proteomic analysis of mitochondrial protein turnover: identification of novel substrate proteins of the matrix protease pim1.

Submit: New GeneRIF Correction

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent peptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP-dependent peptidase activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent peptidase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables sequence-specific DNA binding	IEA Inferred from Electronic Annotation more info
enables serine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info
enables serine-type peptidase activity	IEA Inferred from Electronic Annotation more info
enables single-stranded DNA binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in cellular response to oxidative stress	IEA Inferred from Electronic Annotation more info
involved_in chaperone-mediated protein complex assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in chaperone-mediated protein complex assembly	IEA Inferred from Electronic Annotation more info
involved_in chaperone-mediated protein complex assembly	IGI Inferred from Genetic Interaction more info	PubMed
involved_in mitochondrion organization	IBA Inferred from Biological aspect of Ancestor more info
involved_in oxidation-dependent protein catabolic process	IEA Inferred from Electronic Annotation more info
involved_in protein catabolic process	IEA Inferred from Electronic Annotation 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	IEA Inferred from Electronic Annotation more info
involved_in protein quality control for misfolded or incompletely synthesized proteins	IGI Inferred from Genetic Interaction more info	PubMed
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
involved_in regulation of mitochondrial DNA metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in mitochondrial matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
located_in mitochondrial matrix	IMP Inferred from Mutant Phenotype more info	PubMed
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

NP_009531.1

ATP-dependent Lon protease; involved in degradation of misfolded mitochondrial proteins; required for mitochondrial maintenance and biogenesis; regulates mitochondrial DNA copy number with Mrx6p; subunit of a complex containing Mrx6p, Pet20p, and Mam33p that may regulate mtDNA replication; protease-independent, chaperone-like function in mitochondrial membrane complex assembly; localizes to the mitochondrial matrix