A0A1L8FZ98 · PEX2_XENLA
- ProteinPeroxisome biogenesis factor 2
- Genepex2.L
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids306 (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 (PubMed:35931083).
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 | 245 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 248 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 260 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 262 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 265 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 268 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 281 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 284 | 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 | 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 > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionA0A1L8FZ98
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 | 1-15 | Peroxisomal matrix | ||||
Sequence: MAASENNMEEINPVL | ||||||
Transmembrane | 16-42 | Helical; Name=TM1 | ||||
Sequence: RISQLDAIELNKALEQLIWSQFSSCFQ | ||||||
Topological domain | 43-48 | Cytoplasmic | ||||
Sequence: GFKPGL | ||||||
Transmembrane | 49-74 | Helical; Name=TM2 | ||||
Sequence: LTRFEPEIKASLCLFLWRYTIYTKNA | ||||||
Topological domain | 75-98 | Peroxisomal matrix | ||||
Sequence: TVGQTILNMQYKNDLAVTKKYRPL | ||||||
Transmembrane | 99-125 | Helical; Name=TM3 | ||||
Sequence: NKQQKVWFALFLVGGKWLEERSFDLFS | ||||||
Topological domain | 126-134 | Cytoplasmic | ||||
Sequence: NHPFGASFQ | ||||||
Transmembrane | 135-161 | Helical; Name=TM4 | ||||
Sequence: RTKYFLNAISGLLKFGALLNFLIFLQQ | ||||||
Topological domain | 162-188 | Peroxisomal matrix | ||||
Sequence: GKFATLTERLLGIRSVFSRPQDVRQVG | ||||||
Transmembrane | 189-212 | Helical; Name=TM5 | ||||
Sequence: FEYMNREILWHGFAEFLIFLLPLI | ||||||
Topological domain | 213-306 | Cytoplasmic | ||||
Sequence: NTQKLKSKLFSWCKPAKSHGVSDPSLAVICKECCLCGEWPAMPHTIGCSHVFCYYCIKSNYMSDMYFTCPKCSSQVHNLQPLEFKIEISEVHTL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000456984 | 1-306 | Peroxisome biogenesis factor 2 | |||
Sequence: MAASENNMEEINPVLRISQLDAIELNKALEQLIWSQFSSCFQGFKPGLLTRFEPEIKASLCLFLWRYTIYTKNATVGQTILNMQYKNDLAVTKKYRPLNKQQKVWFALFLVGGKWLEERSFDLFSNHPFGASFQRTKYFLNAISGLLKFGALLNFLIFLQQGKFATLTERLLGIRSVFSRPQDVRQVGFEYMNREILWHGFAEFLIFLLPLINTQKLKSKLFSWCKPAKSHGVSDPSLAVICKECCLCGEWPAMPHTIGCSHVFCYYCIKSNYMSDMYFTCPKCSSQVHNLQPLEFKIEISEVHTL |
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 | 245-285 | RING-type | ||||
Sequence: CCLCGEWPAMPHTIGCSHVFCYYCIKSNYMSDMYFTCPKCS |
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
- Length306
- Mass (Da)35,374
- Last updated2017-03-15 v1
- ChecksumE20B87750FF05CB0
Keywords
- Technical term