E7F4V8 · PEX2_DANRE
- ProteinPeroxisome biogenesis factor 2
- Genepex2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids312 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity).
The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase (By similarity).
The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase (By similarity).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 252 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 255 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 267 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 269 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 272 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 275 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 288 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 291 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisomal membrane | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | peroxisome organization | |
Biological Process | pexophagy | |
Biological Process | protein import into peroxisome matrix, receptor recycling | |
Biological Process | protein ubiquitination | |
Biological Process | response to amino acid starvation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxisome biogenesis factor 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionE7F4V8
- Secondary accessions
Proteomes
Organism-specific databases
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 | 1-22 | Peroxisomal matrix | ||||
Sequence: MAGAGGDKPFAKAGPSPLSRVL | ||||||
Transmembrane | 23-49 | Helical; Name=TM1 | ||||
Sequence: RISQLDAFELDGALEQLVWSQFTQCFQ | ||||||
Topological domain | 50-55 | Cytoplasmic | ||||
Sequence: HFKPGI | ||||||
Transmembrane | 56-81 | Helical; Name=TM2 | ||||
Sequence: LTPVEPELKALLQLLLWRFTIYSNSA | ||||||
Topological domain | 82-105 | Peroxisomal matrix | ||||
Sequence: TVGQSLLNIRYKNALIPGQKYRPM | ||||||
Transmembrane | 106-132 | Helical; Name=TM3 | ||||
Sequence: SRPQKFWFALLTVGEKWFRERSHSLFL | ||||||
Topological domain | 133-141 | Cytoplasmic | ||||
Sequence: NHPAESNAR | ||||||
Transmembrane | 142-168 | Helical; Name=TM4 | ||||
Sequence: KARKVLSILLGLTKAASLVNFLLFLQR | ||||||
Topological domain | 169-195 | Peroxisomal matrix | ||||
Sequence: GTFPTLTERLLGVQPVFSRPQGPRDIN | ||||||
Transmembrane | 196-219 | Helical; Name=TM5 | ||||
Sequence: FQYLNRELLWHGFAEFLIFLLPLI | ||||||
Topological domain | 220-312 | Cytoplasmic | ||||
Sequence: NVWKLKAGVSALFSPLSDLTGTQSSEETHLTECAICGEWPTMPHSIGCKHVFCYYCVKSNVIADIYFTCPKCGAETGQIEPVRLQVGTELLQS |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mutant fishes show a loss of peroxisomal structure, associated with high-mortality (PubMed:34016526).
Defects are similar to human Zellweger syndrome (ZS), characterized by developmental abnormalities in many organs, organ-specific accumulation and reduction of distinct fatty acid species, such as an accumulation of ultra-very-long-chain polyunsaturated fatty acids (ultra-VLC-PUFAs) (PubMed:34016526).
Defects are similar to human Zellweger syndrome (ZS), characterized by developmental abnormalities in many organs, organ-specific accumulation and reduction of distinct fatty acid species, such as an accumulation of ultra-very-long-chain polyunsaturated fatty acids (ultra-VLC-PUFAs) (PubMed:34016526).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000456983 | 1-312 | Peroxisome biogenesis factor 2 | |||
Sequence: MAGAGGDKPFAKAGPSPLSRVLRISQLDAFELDGALEQLVWSQFTQCFQHFKPGILTPVEPELKALLQLLLWRFTIYSNSATVGQSLLNIRYKNALIPGQKYRPMSRPQKFWFALLTVGEKWFRERSHSLFLNHPAESNARKARKVLSILLGLTKAASLVNFLLFLQRGTFPTLTERLLGVQPVFSRPQGPRDINFQYLNRELLWHGFAEFLIFLLPLINVWKLKAGVSALFSPLSDLTGTQSSEETHLTECAICGEWPTMPHSIGCKHVFCYYCVKSNVIADIYFTCPKCGAETGQIEPVRLQVGTELLQS |
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Component of the PEX2-PEX10-PEX12 retrotranslocation channel.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 252-292 | RING-type | ||||
Sequence: CAICGEWPTMPHSIGCKHVFCYYCVKSNVIADIYFTCPKCG |
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 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
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length312
- Mass (Da)35,131
- Last updated2011-03-08 v1
- Checksum8F905A55DE887D17
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A9B7QDH4 | A0A9B7QDH4_DANRE | pex2 | 312 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR361560 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |