A0A3F3RV15 · A0A3F3RV15_ASPNG

  • Protein
    Autophagy-related protein 9
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking.
Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

GO annotations

AspectTerm
Cellular Componentcytoplasmic vesicle membrane
Cellular Componentmitochondrion
Cellular Componentphagophore
Cellular Componentphagophore assembly site membrane
Molecular Functionphospholipid scramblase activity
Molecular Functiontransaminase activity
Biological Processmitophagy
Biological Processpiecemeal microautophagy of the nucleus
Biological Processprotein localization to phagophore assembly site
Biological Processreticulophagy

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Autophagy-related protein 9

Gene names

    • ORF names
      CAN33_0045060

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • FDAARGOS_311
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati

Accessions

  • Primary accession
    A0A3F3RV15

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Multi-pass membrane protein
Preautophagosomal structure membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane236-256Helical
Transmembrane289-307Helical
Transmembrane456-480Helical
Transmembrane539-559Helical
Transmembrane579-597Helical
Transmembrane645-666Helical

Keywords

  • Cellular component

Interaction

Subunit

Homotrimer; forms a homotrimer with a central pore that forms a path between the two membrane leaflets.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-164Disordered
Compositional bias24-64Basic and acidic residues
Compositional bias143-157Pro residues
Region795-889Disordered
Compositional bias869-889Polar residues

Sequence similarities

Belongs to the ATG9 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    941
  • Mass (Da)
    106,681
  • Last updated
    2019-01-16 v1
  • Checksum
    B3B11FD93BEAA795
MMTSNILSRFLPPNGSPSVYETIRQHDNHSDASDVEERAGMAFEDEHGDRFSDRELEDALADAGRDDSPGPSEPFLPRSPPTKRDEGGFLKAGSRRRKFSRSGRIHAASPRHKFDDSDDDVPPSLLVEGDQDDDDVLRSKLPPPPRSIDPPNVEPPPRPSPRDDRVHWEAARDRLPLHDTNRRAHHASLWSAGYPNLALVDPKEKALWMWANVENLDNFLKEVYTYFLGNGIWSILLNRVLSLLTFAFVVGFSIFLTNCIDYHKVRGSRTLDDILIQKCTKQMSMSATFLLWLLSFFWIGKAFQYLLDIRRLKHMHDFYHYLLGISDAEIQSISWQEVVSRLMTLRDSNPATAGAVSAKHRKFMGSQSKQRMDAHDIANRLMRKENYLIALINKDILDLTLPIPFLRNRQLFSRTLEWNINLCIMDYVFNEQGQVRTLFLKDTHRRALSEGLRRRFMFAGIMNIFVAPFIVVYFMMHYFFRYFNEYKKNPSQIGSRQYTPLAEWKFREFNELWHLFERRVNMSYPFASRYVDQFPKDKMVQFAGFVAFVSGALASVLALASVVDPELFLGFEITHDRTVLFYLGVFGSIWAVAQGLVPEETNVFDPEYALLEVINFTHYFPGHWKGRLHSDDVRKDFAVLYQMKIVIFLEEILSMIFTPFILWFSLPKCSDRLIDFFREFTVHVDGMGYLCSFAVFDFKKGTNVISQGDTGRRDAARQDLRADYFSTKDGKMLASYYGFLDNYGANPRSGHPSTKRQFHPPPTFPTLGSPSAIEMGNFGDRPAAAGLMGQQSTYGAAPRFGPAGMGDHLSPAPSMLLDPHHQPSASGFRSTHRANPYPRYRASRPPPTISDPIEDEDPPAGKGRSAVKSSPGVGSSGGGIGTSDSNLGESWRMNLVGDEVEEEDEGGENVDTLAGGGGVLGLIQQFQKVNQDNRGRTTVGI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias24-64Basic and acidic residues
Compositional bias143-157Pro residues
Compositional bias869-889Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NKJJ02000001
EMBL· GenBank· DDBJ
TPR02589.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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