Q92265 · PEX10_PICPA
- ProteinPeroxisome biogenesis factor 10
- GenePEX10
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids419 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase component of the peroxisomal translocation complex (PubMed:12121419, PubMed:23344950, PubMed:7565793).
The two types of peroxisomal matrix targeting signals, PTS1 and PTS2, are first recognized in the cytosol by their receptors PEX5 and PEX7, respectively, which then carry the cargo to the peroxisomal membrane. The peroxisomal targeting signal (PTS) receptor-cargo complexes interact with peroxisomal membrane protein (PMP) components of the docking complex. They have then additional downstream interactions with the translocation complex, leading to the transport of fully folded and oligomerized cargo into the peroxisome matrix (PubMed:12121419).
The peroxisomal translocation complex forms the retrotranslocation channel with each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 and PEX20 through the peroxisomal membrane (By similarity).
Specifically catalyzes monoubiquitination of PEX5 and/or PEX20 at 'Cys-6' and 'Cys-8', respectively, a modification that acts as a signal for PEX5 or PEX20 export from peroxisomes to the cytosol, thereby promoting PEX5 and PEX20 recycling (PubMed:12121419, PubMed:23344950).
The two types of peroxisomal matrix targeting signals, PTS1 and PTS2, are first recognized in the cytosol by their receptors PEX5 and PEX7, respectively, which then carry the cargo to the peroxisomal membrane. The peroxisomal targeting signal (PTS) receptor-cargo complexes interact with peroxisomal membrane protein (PMP) components of the docking complex. They have then additional downstream interactions with the translocation complex, leading to the transport of fully folded and oligomerized cargo into the peroxisome matrix (PubMed:12121419).
The peroxisomal translocation complex forms the retrotranslocation channel with each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 and PEX20 through the peroxisomal membrane (By similarity).
Specifically catalyzes monoubiquitination of PEX5 and/or PEX20 at 'Cys-6' and 'Cys-8', respectively, a modification that acts as a signal for PEX5 or PEX20 export from peroxisomes to the cytosol, thereby promoting PEX5 and PEX20 recycling (PubMed:12121419, PubMed:23344950).
Catalytic activity
Activity regulation
The E3 ubiquitin-protein ligase activity is stimulated by PEX12.
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 298 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 301 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 313 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 315 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 318 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 321 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 334 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 347 | Zn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisomal membrane | |
Molecular Function | transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | protein import into peroxisome matrix, receptor recycling | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxisome biogenesis factor 10
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Pichiaceae > Komagataella
Accessions
- Primary accessionQ92265
Subcellular Location
UniProt Annotation
GO Annotation
Peroxisome membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Topological domain | 1-27 | Peroxisomal matrix | |||
Transmembrane | 28-57 | Helical; Name=TM1 | |||
Topological domain | 58 | Cytoplasmic | |||
Transmembrane | 59-80 | Helical; Name=TM2 | |||
Topological domain | 81-108 | Peroxisomal matrix | |||
Transmembrane | 109-141 | Helical; Name=TM3 | |||
Topological domain | 142-158 | Cytoplasmic | |||
Transmembrane | 159-185 | Helical; Name=TM4 | |||
Topological domain | 186-215 | Peroxisomal matrix | |||
Transmembrane | 216-235 | Helical; Name=TM5 | |||
Topological domain | 236-419 | Cytoplasmic | |||
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Leads to a peroxisomal-deficient phenotype with the absence of peroxisomes and the accumulation of aberrant peroxisomal structures resembling 'membranous ghosts'.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 313 | Loss of activity. | |||
Mutagenesis | 313-316 | Impaired recycling of PEX20. | |||
Mutagenesis | 315 | Loss of activity. | |||
Mutagenesis | 316 | No loss of activity. | |||
Mutagenesis | 318 | Loss of activity. | |||
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000056379 | 1-419 | Peroxisome biogenesis factor 10 | ||
Structure
Family & Domains
Features
Showing features for zinc finger.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Zinc finger | 298-360 | RING-type | |||
Domain
The three subunits of the retrotranslocation channel (PEX2, PEX10 and PEX12) coassemble in the membrane into a channel with an open 10 Angstrom pore. The RING-type zinc-fingers that catalyze PEX5 or PEX20 receptor ubiquitination are positioned above the pore on the cytosolic side of the complex.
Sequence similarities
Belongs to the pex2/pex10/pex12 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length419
- Mass (Da)47,948
- Last updated1997-02-01 v1
- Checksum8D073E48A956AB85
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U70066 EMBL· GenBank· DDBJ | AAB09086.1 EMBL· GenBank· DDBJ | Genomic DNA |