 |
|
Annotation rule MF_03120 |
General rule information
[?]
Accession |
MF_03120 |
Dates |
18-JUN-2010 (Created) 20-NOV-2019 (Last updated, Version 12) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
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>
else case <OC:Fungi>
end case
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. |
case <FTTag:ATP>
end case
case <OC:Mammalia> or <OC:Saccharomyces>
end case
GO:0005759; Cellular component: mitochondrial matrix.
GO:0005524; Molecular function: ATP binding.
GO:0016887; Molecular function: ATPase 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.
case not <OC:Mammalia> and not <OC:Saccharomyces>
General |
TransitM; -; 0-1; trigger=yes; |
end case
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) |
NP_BIND
|
|
523
|
|
530
|
|
ATP
|
|
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 |