G2Q5N0 · PEX12_THET4

Function

function

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 (By similarity).
PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (By similarity).
When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation (By similarity).

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for binding site.

143950100150200250300350400
TypeIDPosition(s)Description
Binding site367Zn2+ (UniProtKB | ChEBI)
Binding site370Zn2+ (UniProtKB | ChEBI)
Binding site387Zn2+ (UniProtKB | ChEBI)
Binding site390Zn2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentperoxisomal membrane
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 assembly protein 12
  • Alternative names
    • Peroxin-12

Gene names

    • Name
      PEX12
    • ORF names
      MYCTH_2053677

Organism names

Accessions

  • Primary accession
    G2Q5N0

Proteomes

Organism-specific databases

Subcellular Location

Peroxisome membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-17Peroxisomal matrix
Transmembrane18-45Helical; Name=TM1
Topological domain46-49Cytoplasmic
Transmembrane50-74Helical; Name=TM2
Topological domain75-115Peroxisomal matrix
Transmembrane116-149Helical; Name=TM3
Topological domain150-162Cytoplasmic
Transmembrane163-199Helical; Name=TM4
Topological domain200-253Peroxisomal matrix
Transmembrane254-281Helical; Name=TM5
Topological domain282-439Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004569911-439Peroxisome assembly protein 12

Interaction

Subunit

Component of the PEX2-PEX10-PEX12 retrotranslocation channel, composed of PEX2, PEX10 and PEX12.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, zinc finger.

TypeIDPosition(s)Description
Region292-343Disordered
Zinc finger366-439RING-type; degenerate

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 (PubMed:35768507).
The RING-type zinc-fingers that catalyze PEX5 receptor ubiquitination are positioned above the pore on the cytosolic side of the complex (PubMed:35768507).
The RING-type zinc-finger is degenerated and only coordinates one zinc ions, preventing E3 ubiquitin-protein ligase activity.

Sequence similarities

Belongs to the pex2/pex10/pex12 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    439
  • Mass (Da)
    49,301
  • Last updated
    2011-11-16 v1
  • Checksum
    406DA4CAF6278E4C
MEFIPALQARIDEHKPSLFELLSEQQLAALLPPTVRYLLTVLTQRYPRYLLRVLNSFDELYALAALVVERHYLRTRGGSFTEHFYGLKRERALAAEIPRASAAAPGAVRDALRLRPADVWRNLLVIVGVPYLKRKLDEAHEADAPRAMMGAAYNRPPLPGAPWRERVAFWWRCFLRRVYPAVNAAYYLSILAFNLAYLFDNSKYHSPFLCLIGTRVRRMSAADYRAIEALEERAAKRRGGRSVAARMLGGLSLVLPTSIFALKFLEWWYASDFAKQLSRKAAESLDLPPPVVAGLPTGAGGGGGSEKAQQPRREKELGKEKDEEVEEEEEEVSEEEKERRAIERAPVSASSLLPIYTVPPPENSDQCPICEGEITTAAACQTGIVYCYPCIHKWLTGTHPRQEKFMAERAGKWESGEGRCAVTGRRVLGGTEGLRRIMV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP003002
EMBL· GenBank· DDBJ
AEO55466.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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