Reviewed,
UniProtKB/Swiss-Prot A6REI4 (ATG15_AJECN)
Last modified
November 3, 2009.
Version 20.
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 |
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| Organism | Ajellomyces capsulata (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum) | ||||
| Taxonomic identifier | 339724 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › Ajellomycetaceae › Ajellomyces |
Protein attributes
| Sequence length | 585 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Sequence caution | The sequence EDN04383.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Autophagy Lipid degradation |
| Cellular component | Endoplasmic reticulum Endosome Golgi apparatus Membrane |
| Domain | Signal-anchor Transmembrane |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| 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 – 585 | 585 | Putative lipase ATG15 | PRO_0000317957 | |||||
Regions | |||||||||
| Transmembrane | 1 – 21 | 21 | Signal-anchor for type II membrane protein | ||||||
| Topological domain | 22 – 585 | 564 | Lumenal By similarity | ||||||
| Compositional bias | 439 – 575 | 137 | Thr-rich | ||||||
Sites | |||||||||
| Active site | 291 | 1 | Charge relay system By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 171 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 193 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 275 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 340 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 437 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives." Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. Taylor J.W.Genome Res. 19:1722-1731(2009) [PubMed: 19717792] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CH476664 Genomic DNA. Translation: EDN04383.1. Sequence problems. | |
| RefSeq | XP_001536940.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5443371. |
Family and domain databases | |
| InterPro | IPR008262. Lipase_Ser_AS. [Graphical view] |
| PROSITE | PS00120. LIPASE_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ATG15_AJECN | ||||||||
| Accession | Primary (citable) accession number: A6REI4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


