Q92265 · PEX10_PICPA

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).

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Activity regulation

The E3 ubiquitin-protein ligase activity is stimulated by PEX12.

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site298Zn2+ 1 (UniProtKB | ChEBI)
Binding site301Zn2+ 1 (UniProtKB | ChEBI)
Binding site313Zn2+ 2 (UniProtKB | ChEBI)
Binding site315Zn2+ 2 (UniProtKB | ChEBI)
Binding site318Zn2+ 1 (UniProtKB | ChEBI)
Binding site321Zn2+ 1 (UniProtKB | ChEBI)
Binding site334Zn2+ 2 (UniProtKB | ChEBI)
Binding site347Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentperoxisomal membrane
Molecular Functiontransferase activity
Molecular Functionzinc ion binding
Biological Processprotein import into peroxisome matrix, receptor recycling
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peroxisome biogenesis factor 10
  • EC number
  • Alternative names
    • E3 ubiquitin-protein ligase PEX10
    • Peroxin-10
    • Peroxisomal biogenesis factor 10
    • Peroxisome assembly protein 10
    • Peroxisome assembly protein PAS7

Gene names

    • Name
      PEX10
    • Synonyms
      PAS7

Organism names

Accessions

  • Primary accession
    Q92265

Subcellular Location

Peroxisome membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain1-27Peroxisomal matrix
Transmembrane28-57Helical; Name=TM1
Topological domain58Cytoplasmic
Transmembrane59-80Helical; Name=TM2
Topological domain81-108Peroxisomal matrix
Transmembrane109-141Helical; Name=TM3
Topological domain142-158Cytoplasmic
Transmembrane159-185Helical; Name=TM4
Topological domain186-215Peroxisomal matrix
Transmembrane216-235Helical; Name=TM5
Topological domain236-419Cytoplasmic

Keywords

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.

TypeIDPosition(s)Description
Mutagenesis313Loss of activity.
Mutagenesis313-316Impaired recycling of PEX20.
Mutagenesis315Loss of activity.
Mutagenesis316No loss of activity.
Mutagenesis318Loss of activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000563791-419Peroxisome biogenesis factor 10

Interaction

Subunit

Component of the peroxisomal translocation complex, composed of at least PEX3, PEX2, PEX10 and PEX12 (PubMed:12121419).
Interacts with PEX19 (PubMed:10359594, PubMed:28526747).

Structure

Family & Domains

Features

Showing features for zinc finger.

TypeIDPosition(s)Description
Zinc finger298-360RING-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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    419
  • Mass (Da)
    47,948
  • Last updated
    1997-02-01 v1
  • Checksum
    8D073E48A956AB85
MPPSEEIKLRAVSPRPDFKANYLEFANAPAIVRANQKDSYFETVLRDKLQNVIQIFKGQRFTHTHPEEIGVAAKALYLSLTTLLGTKTLGEEYVDLIYVSRDGKRIPRYLARAGFIFAYAILPYFLTRLFRRLKSSSTPKDEVTEEKINKELPISLRIEKYLSNMSYSKVLDTIMNLHIAVFYFSGQFYNISKRFFSMRYAFGHKINKERTPNGNYELLGGLIVLQLVMKSLGGFKGLIGSFTGNDEHDESNLRANNKDIMYGIPSEEEQEEAKQQLGIIDLSDPGQLPYIPESSRQCMLCLSYMTNPTAANCGHCFCWSCIIDWCKERQTVLCVGKKCWNSNCYHCIRLFYIPTLNKICFFFLLSFLSVRAASKEFKSTKEEFAELFNEELADIAGEDPHCPGPFPTGRTLGYFLVVF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U70066
EMBL· GenBank· DDBJ
AAB09086.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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