Reviewed,
UniProtKB/Swiss-Prot Q5B0L1 (ATG15_EMENI)
Last modified
January 19, 2010.
Version 39.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative lipase atg15 EC=3.1.1.3 Alternative name(s): Autophagy-related protein 15 | ||||
| Gene names |
| ||||
| Organism | Emericella nidulans (Aspergillus nidulans) [Complete proteome] | ||||
| Taxonomic identifier | 162425 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella |
Protein attributes
| Sequence length | 590 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | May be involved in lysis of subvacuolar cytoplasm to vacuole targeted bodies, intravacuolar autophagic bodies and of intravacuolar multivesicular body (MVB) vesicles By similarity. |
| Catalytic activity | Triacylglycerol + H2O = diacylglycerol + a carboxylate. |
| Subcellular location | Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity. Golgi apparatus membrane; Single-pass type II membrane protein By similarity. Endosome › multivesicular body membrane; Single-pass type II membrane protein By similarity. Prevacuolar compartment membrane; Single-pass type II membrane protein By similarity. Note: From ER, targeted to vacuolar lumen at the MVB vesicles via the Golgi and the prevacuolar compartment (PVC) By similarity. |
| Sequence similarities | Belongs to the AB hydrolase superfamily. Lipase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Autophagy Lipid degradation |
| Cellular component | Endoplasmic reticulum Endosome Golgi apparatus Membrane |
| Domain | Signal-anchor Transmembrane |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | autophagy Inferred from electronic annotation. Source: UniProtKB-KW lipid catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulumInferred from electronic annotation. Source: UniProtKB-KW endosomeInferred from electronic annotation. Source: UniProtKB-KW integral to membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | triglyceride lipase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 590 | 590 | Putative lipase atg15 | PRO_0000090368 | |||||
Regions | |||||||||
| Topological domain | 1 – 7 | 7 | Cytoplasmic Potential | ||||||
| Transmembrane | 8 – 28 | 21 | Signal-anchor for type II membrane protein Potential | ||||||
| Topological domain | 29 – 590 | 562 | Lumenal Potential | ||||||
| Compositional bias | 459 – 563 | 105 | Thr-rich | ||||||
Sites | |||||||||
| Active site | 308 | 1 | Charge relay system By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 153 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 188 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 210 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 268 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 292 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 454 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. Birren B.W.Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / M139. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AACD01000101 Genomic DNA. Translation: EAA57782.1. |
| RefSeq | XP_663523.1. |
3D structure databases | |
| SMR | Q5B0L1. Positions 154-321. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2870991. |
| KEGG | ani:AN5919.2. |
Phylogenomic databases | |
| PhylomeDB | Q5B0L1. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.3. 3859. |
Family and domain databases | |
| InterPro | IPR002921. Lipase_3. [Graphical view] |
| Pfam | PF01764. Lipase_3. 1 hit. [Graphical view] |
| PROSITE | PS00120. LIPASE_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ATG15_EMENI | ||||||||
| Accession | Primary (citable) accession number: Q5B0L1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


