Cloned (Comment) | Organism |
---|---|
gene Lon1, phylogenetic tree | Zea mays |
gene Lonp2, phylogenetic tree | Mus musculus |
gene NCU08303, phylogenetic tree | Neurospora crassa |
gene PLN, phylogenetic tree, recombinant expression of HpPln, a GFP-PLN hybrid gene under control of the PLN promoter, constructed for the subcellular localization study, coexpression of te peroxisomal marker GFP-SKL in Hansenula polymorpha | Ogataea angusta |
gene YALI0F23595g, phylogenetic tree | Yarrowia lipolytica |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of the various disruption strains of the Hansenula polymorpha PLN gene, the pln deletion cells grow normally like wild-type cells on methanol at 37°C. Growth is also unaffected at elevated growth temperatures (45°C) or upon heat shock | Ogataea angusta |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
peroxisome | - |
Mus musculus | 5777 | - |
peroxisome | - |
Zea mays | 5777 | - |
peroxisome | - |
Yarrowia lipolytica | 5777 | - |
peroxisome | - |
Neurospora crassa | 5777 | - |
peroxisome | HpPln is localized in peroxisomes in Hansenula polymorpha, subcellular localization study | Ogataea angusta | 5777 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
104900 | - |
about, sequence calculation | Ogataea angusta |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Ogataea angusta | the enzyme degrades soluble unfolded and non-assembled peroxisomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein | ? | - |
? | |
additional information | Ogataea angusta NCYC495 | the enzyme degrades soluble unfolded and non-assembled peroxisomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q9DBN5 | Lon protease homolog 2, peroxisomal | - |
Neurospora crassa | Q7SA85 | Lon protease homolog 2, peroxisomal; gene NCU08303 | - |
Ogataea angusta | Q2V573 | PLN, Lon protease homolog 2, peroxisomal; i.e. Pichia angusta | - |
Ogataea angusta NCYC495 | Q2V573 | PLN, Lon protease homolog 2, peroxisomal; i.e. Pichia angusta | - |
Yarrowia lipolytica | Q6C0L7 | Lon protease homolog 2, peroxisomal; i.e. Candida lipolytica, gene YALI0F23595g | - |
Zea mays | P93647 | Lon protease homolog 2, peroxisomal | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme degrades soluble unfolded and non-assembled peroxisomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein | Ogataea angusta | ? | - |
? | |
additional information | the enzyme degrades soluble unfolded and non-assembled peroxisomal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein | Ogataea angusta NCYC495 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789) | Ogataea angusta |
Synonyms | Comment | Organism |
---|---|---|
HpPln | - |
Ogataea angusta |
LONP2 | - |
Mus musculus |
LONP2 | - |
Zea mays |
LONP2 | - |
Yarrowia lipolytica |
LONP2 | - |
Neurospora crassa |
Mm-p | - |
Mus musculus |
Nc-p | - |
Neurospora crassa |
peroxisomal Lon protease | - |
Ogataea angusta |
peroxisomal Lon protease | - |
Mus musculus |
peroxisomal Lon protease | - |
Zea mays |
peroxisomal Lon protease | - |
Yarrowia lipolytica |
peroxisomal Lon protease | - |
Neurospora crassa |
Pln | - |
Ogataea angusta |
Yl-p | - |
Yarrowia lipolytica |
Zm-p | - |
Zea mays |
Organism | Comment | Expression |
---|---|---|
Ogataea angusta | the expression of PLN is not significantly enhanced in glucose-grown cells upon heat shock as reported for the mitochondrial Lon protease, PIM1, of Saccharomyces cerevisiae | additional information |
General Information | Comment | Organism |
---|---|---|
evolution | Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases | Mus musculus |
evolution | Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases | Zea mays |
evolution | Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases | Yarrowia lipolytica |
evolution | Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases | Neurospora crassa |
evolution | Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases. Peroxismal Lon protease from Hansenula polymorpha shows 39% sequence identity with the putative peroxisomal Lon protease of Mus musculus | Ogataea angusta |
malfunction | the absence of enzyme HpPln affects the viability of cells blocked in pexophagy, but does not affect cell growth. The number of peroxisomes is enhanced in enzyme deletion mutant cells | Ogataea angusta |
additional information | the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789). The ATPase domain in Lon proteases is required for ATP?dependent unfolding of the target protein, prior to degradation by the protease domain | Ogataea angusta |
physiological function | most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality | Mus musculus |
physiological function | most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality | Zea mays |
physiological function | most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality | Yarrowia lipolytica |
physiological function | most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality | Neurospora crassa |
physiological function | most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality, although the enzyme is not important for the viability | Ogataea angusta |