A0A3F3RV15 · A0A3F3RV15_ASPNG
- ProteinAutophagy-related protein 9
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids941 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)(out)
- a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out)
- a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out)
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | mitochondrion | |
Cellular Component | phagophore | |
Cellular Component | phagophore assembly site membrane | |
Molecular Function | phospholipid scramblase activity | |
Molecular Function | transaminase activity | |
Biological Process | mitophagy | |
Biological Process | piecemeal microautophagy of the nucleus | |
Biological Process | protein localization to phagophore assembly site | |
Biological Process | reticulophagy |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAutophagy-related protein 9
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionA0A3F3RV15
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Preautophagosomal structure membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 236-256 | Helical | ||||
Sequence: LLNRVLSLLTFAFVVGFSIFL | ||||||
Transmembrane | 289-307 | Helical | ||||
Sequence: FLLWLLSFFWIGKAFQYLL | ||||||
Transmembrane | 456-480 | Helical | ||||
Sequence: FMFAGIMNIFVAPFIVVYFMMHYFF | ||||||
Transmembrane | 539-559 | Helical | ||||
Sequence: MVQFAGFVAFVSGALASVLAL | ||||||
Transmembrane | 579-597 | Helical | ||||
Sequence: VLFYLGVFGSIWAVAQGLV | ||||||
Transmembrane | 645-666 | Helical | ||||
Sequence: IVIFLEEILSMIFTPFILWFSL |
Keywords
- Cellular component
Interaction
Subunit
Homotrimer; forms a homotrimer with a central pore that forms a path between the two membrane leaflets.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-164 | Disordered | ||||
Sequence: MMTSNILSRFLPPNGSPSVYETIRQHDNHSDASDVEERAGMAFEDEHGDRFSDRELEDALADAGRDDSPGPSEPFLPRSPPTKRDEGGFLKAGSRRRKFSRSGRIHAASPRHKFDDSDDDVPPSLLVEGDQDDDDVLRSKLPPPPRSIDPPNVEPPPRPSPRDD | ||||||
Compositional bias | 24-64 | Basic and acidic residues | ||||
Sequence: RQHDNHSDASDVEERAGMAFEDEHGDRFSDRELEDALADAG | ||||||
Compositional bias | 143-157 | Pro residues | ||||
Sequence: PPPRSIDPPNVEPPP | ||||||
Region | 795-889 | Disordered | ||||
Sequence: GAAPRFGPAGMGDHLSPAPSMLLDPHHQPSASGFRSTHRANPYPRYRASRPPPTISDPIEDEDPPAGKGRSAVKSSPGVGSSGGGIGTSDSNLGE | ||||||
Compositional bias | 869-889 | Polar residues | ||||
Sequence: SSPGVGSSGGGIGTSDSNLGE |
Sequence similarities
Belongs to the ATG9 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length941
- Mass (Da)106,681
- Last updated2019-01-16 v1
- ChecksumB3B11FD93BEAA795
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 24-64 | Basic and acidic residues | ||||
Sequence: RQHDNHSDASDVEERAGMAFEDEHGDRFSDRELEDALADAG | ||||||
Compositional bias | 143-157 | Pro residues | ||||
Sequence: PPPRSIDPPNVEPPP | ||||||
Compositional bias | 869-889 | Polar residues | ||||
Sequence: SSPGVGSSGGGIGTSDSNLGE |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NKJJ02000001 EMBL· GenBank· DDBJ | TPR02589.1 EMBL· GenBank· DDBJ | Genomic DNA |