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HAMAP rule MF_03120

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General rule information [?]

Accession MF_03120
Dates 18-JUN-2010 (Created)
1-JUN-2023 (Last updated, Version 17)
Name lonm_euk
Scope(s) Eukaryota
Template(s) P36776 (LONM_HUMAN); Q59HJ6 (LONM_BOVIN); P36775 (LONM_YEAST); [ Recover all ]
Triggered by HAMAP; MF_03120 (Get profile general information and statistics)

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 Name=LONP1;
else case <OC:Fungi>
Gene name Name=PIM1;
end case

Comments [?]

case <OC:Mammalia>
FUNCTIONATP-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
FUNCTIONATP-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>
SUBUNITHomohexamer. 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>
SUBUNITHomoheptamer. Organized in a ring with a central cavity. Oligomerization is independent of its proteolytic activity and the autocatalytic maturation of its subunits.
else
SUBUNITHomohexamer or homoheptamer. Organized in a ring with a central cavity.
end case
SUBCELLULAR LOCATIONMitochondrion matrix.
case not <OC:Mammalia> and not <OC:Saccharomyces> and not <AnyFeature:TransitM>
MISCELLANEOUSThis protein may be expected to contain an N-terminal transit peptide but none has been predicted.
end case
SIMILARITYBelongs to the peptidase S16 family.

Keywords [?]

case <FTTag:ATP>
ATP-binding
Nucleotide-binding
end case
DNA-binding
Hydrolase
Mitochondrion
Protease
Serine protease
case <OC:Mammalia> or <OC:Saccharomyces>
Transit peptide
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;
PROSITE PS51786; LON_PROTEOLYTIC; 1;
PROSITE PS01046; LON_SER; 1;
Pfam PF00004; AAA; 1;
Pfam PF02190; LON; 1;
Pfam PF03357; Snf7; 1;
PRINTS PR00830; ENDOLAPTASE; 1;
NCBIfam TIGR00763; lon; 1;
General TransitM; -; 0-1;

Features [?]

From: LONM_BOVIN (Q59HJ6)
Key From To Description Tag Condition FTGroup
case <OC:Mammalia>
TRANSIT Nter 67 /note="Mitochondrion"
CHAIN 68 Cter /note="Lon protease homolog, mitochondrial"
end case
From: LONM_YEAST (P36775)
Key From To Description Tag Condition FTGroup
case <OC:Saccharomyces>
TRANSIT Nter 37 /note="Mitochondrion"
PROPEP 38 98 /note="Removed in mature form; by autocatalysis"
CHAIN 99 Cter /note="Lon protease homolog, mitochondrial"
end case
From: LONM_HUMAN (P36776)
Key From To Description Tag Condition FTGroup
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
MF_01973
Fusion Nter: None Cter: None



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