HAMAP logo

HAMAP rule MF_03120

Send feedback

General rule information [?]

Accession MF_03120
Dates 18-JUN-2010 (Created)
19-NOV-2022 (Last updated, Version 16)
Name lonm_euk
Scope
Eukaryota
Templates P36776 (LONM_HUMAN); Q59HJ6 (LONM_BOVIN); P36775 (LONM_YEAST): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
LONM
case <OC:Mammalia>
Protein name
RecName: Full=Lon protease homolog, mitochondrial;
EC 3.4.21.53;
AltName: Full=Lon protease-like protein;
Short=LONP;
AltName: Full=Mitochondrial ATP-dependent protease Lon;
AltName: Full=Serine protease 15;
Flags: Precursor;
else case <OC:Saccharomyces>
Protein name
RecName: Full=Lon protease homolog, mitochondrial;
EC 3.4.21.53;
Flags: Precursor;
else
Protein name
RecName: Full=Lon protease homolog, mitochondrial;
EC 3.4.21.53;
end case
case <OC:Vertebrata>
Gene name
LONP1
else case <OC:Fungi>
Gene name
PIM1
end case

Comments [?]

case <OC:Mammalia>
Function ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters.
else
Function ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
end case
Catalytic activity Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
case <OC:Mammalia>
Subunit Homohexamer. Organized in a ring with a central cavity. The ATP-binding and proteolytic domains (AP-domain) form a hexameric chamber, while the N-terminal domain is arranged as a trimer of dimers. DNA and RNA binding is stimulated by substrate and inhibited by ATP binding. Interacts with @gn(TWNK) and mitochondrial DNA polymerase subunit @gn(POLG).
else case <OC:Saccharomyces>
Subunit Homoheptamer. Organized in a ring with a central cavity. Oligomerization is independent of its proteolytic activity and the autocatalytic maturation of its subunits.
else
Subunit Homohexamer or homoheptamer. Organized in a ring with a central cavity.
end case
Subcellular location Mitochondrion matrix.
case not <OC:Mammalia> and not <OC:Saccharomyces> and not <AnyFeature:TransitM>
Miscellaneous This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
end case
Similarity Belongs to the peptidase S16 family.

Keywords [?]

case <FTTag:ATP>
end case
case <OC:Mammalia> or <OC:Saccharomyces>
end case

Gene Ontology [?]

GO:0005759; Cellular component: mitochondrial matrix.
GO:0005524; Molecular function: ATP binding.
GO:0016887; Molecular function: ATP hydrolysis activity.
GO:0004176; Molecular function: ATP-dependent peptidase activity.
GO:0004252; Molecular function: serine-type endopeptidase activity.
GO:0043565; Molecular function: sequence-specific DNA binding.
GO:0034599; Biological process: cellular response to oxidative stress.
GO:0070407; Biological process: oxidation-dependent protein catabolic process.
GO:0006515; Biological process: protein quality control for misfolded or incompletely synthesized proteins.
GO:0051131; Biological process: chaperone-mediated protein complex assembly.

Cross-references [?]

PROSITE PS51787; LON_N; 1; trigger=PRU01123;
PS51786; LON_PROTEOLYTIC; 1; trigger=PRU01122;
PS01046; LON_SER; 1;
Pfam PF00004; AAA; 1;
PF02190; LON; 1;
PF03357; Snf7; 1;
PRINTS PR00830; ENDOLAPTASE; 1;
TIGRFAMs TIGR00763; lon; 1;

Computed features [?]

case not <OC:Mammalia> and not <OC:Saccharomyces>
General TransitM; -; 0-1; trigger=yes;
end case

Features [?]

case <OC:Mammalia>
From: LONM_BOVIN (Q59HJ6)
Key     From     To       Description   Tag   Condition   FTGroup
TRANSIT     Nter     67       Mitochondrion        
CHAIN     68     Cter       Lon protease homolog, mitochondrial        
end case
case <OC:Saccharomyces>
From: LONM_YEAST (P36775)
TRANSIT     Nter     37       Mitochondrion        
PROPEP     38     98       Removed in mature form; by autocatalysis        
CHAIN     99     Cter       Lon protease homolog, mitochondrial        
end case
From: LONM_HUMAN (P36776)
BINDING     523     530       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616   ATP   G-P-[PT]-G-[TV]-G-K-T  
ACT_SITE     855     855             S  
ACT_SITE     898     898             K  

Additional information [?]

Size range 836-1177 amino acids
Related rules MF_03121 (LONP2); MF_01973 (LON)
Fusion None