Reviewed,
UniProtKB/Swiss-Prot Q9P8W2 (LIP3_CANAL)
Last modified
June 16, 2009.
Version 31.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Lipase 3 EC=3.1.1.3 | ||
| Gene names |
| ||
| Organism | Candida albicans (Yeast) | ||
| Taxonomic identifier | 5476 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida |
Protein attributes
| Sequence length | 471 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Triacylglycerol + H2O = diacylglycerol + a carboxylate. |
| Subcellular location | |
| Sequence similarities | Belongs to the AB hydrolase superfamily. Lipase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 16 | 16 | Potential | ||||||
| Chain | 17 – 471 | 455 | Lipase 3 | PRO_0000017822 | |||||
Sites | |||||||||
| Active site | 196 | 1 | Charge relay system By similarity | ||||||
| Active site | 344 | 1 | Charge relay system By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 231 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 319 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 417 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 422 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 451 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Secreted lipases of Candida albicans: cloning, characterisation and expression analysis of a new gene family with at least ten members." Hube B., Stehr F., Bossenz M., Mazur A., Kretschmar M., Schaefer W. Arch. Microbiol. 174:362-374(2000) [PubMed: 11131027] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION. Strain: 1161. |
Cross-references
Sequence databases | |
|---|---|
| AF191316 Genomic DNA. Translation: AAF69520.2. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.3. 1124. |
Family and domain databases | |
| InterPro | IPR005152. Lipase_secreted. [Graphical view] |
| Pfam | PF03583. LIP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LIP3_CANAL | ||||||||
| Accession | Primary (citable) accession number: Q9P8W2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Candida albicans Candida albicans: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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