P32948 (LIP4_CANRU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 57.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Lipase 4 EC=3.1.1.3 | ||
| Gene names |
| ||
| Organism | Candida rugosa (Yeast) (Candida cylindracea) | ||
| Taxonomic identifier | 5481 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida |
Protein attributes
| Sequence length | 549 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. |
| Sequence similarities | Belongs to the type-B carboxylesterase/lipase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Domain | Signal |
| Molecular function | Hydrolase |
| PTM | Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 15 | 15 | |||||||||
| Chain | 16 – 549 | 534 | Lipase 4 | PRO_0000008622 | |||||||
Sites | |||||||||||
| Active site | 224 | 1 | Acyl-ester intermediate By similarity | ||||||||
| Active site | 356 | 1 | Charge relay system By similarity | ||||||||
| Active site | 464 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 366 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 75 ↔ 112 | By similarity | |||||||||
| Disulfide bond | 283 ↔ 292 | By similarity | |||||||||
Sequences
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References
| [1] | "Cloning and analysis of Candida cylindracea lipase sequences." Lotti M., Grandori R., Fusetti F., Longhi S., Brocca S., Tramontano A., Alberghina L. Gene 124:45-55(1993) [PubMed: 8440480] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506. |
| [2] | "Candida rugosa lipases: molecular biology and versatility in biotechnology." Benjamin S., Pandey A. Yeast 14:1069-1087(1998) [PubMed: 9778794] [Abstract] Cited for: REVIEW. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X66007 Genomic DNA. Translation: CAA46806.1. |
| PIR | JN0552. |
3D structure databases | |
| ProteinModelPortal | P32948. |
| SMR | P32948. Positions 16-549. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. IPR019819. Carboxylesterase_B_CS. [Graphical view] |
| Pfam | PF00135. COesterase. 1 hit. [Graphical view] |
| PROSITE | PS00122. CARBOXYLESTERASE_B_1. 1 hit. PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LIP4_CANRU | ||||||||
| Accession | Primary (citable) accession number: P32948 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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