Q99156 (LIP1_YARLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 59.
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 1 EC=3.1.1.3 | ||||
| Gene names |
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| Organism | Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) | ||||
| Taxonomic identifier | 284591 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia |
Protein attributes
| Sequence length | 486 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 |
| Technical term | Complete proteome Reference proteome |
| 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 – ? | Potential | |||||||||
| Chain | ? – 486 | Lipase 1 | PRO_0000008627 | ||||||||
Sites | |||||||||||
| Active site | 193 | 1 | Acyl-ester intermediate By similarity | ||||||||
| Active site | 303 | 1 | Charge relay system By similarity | ||||||||
| Active site | 392 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 332 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 58 ↔ 82 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 31 – 32 | 2 | IP → RR in CAA90323. Ref.1 | ||||||||
| Sequence conflict | 237 | 1 | N → D in CAA90323. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Gonzalez F. Thesis (1996), University of Salamanca, Spain Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 90811 / CLIB 163 / JM12. |
| [2] | "Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L.Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z50020 Genomic DNA. Translation: CAA90323.1. CR382131 Genomic DNA. Translation: CAG79381.1. |
| RefSeq | XP_503790.1. XM_503790.1. |
3D structure databases | |
| ProteinModelPortal | Q99156. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2912789. |
| GenomeReviews | Gene locus YALI0E10659g in contig CR382131_GR. |
| KEGG | yli:YALI0E10659g. |
Phylogenomic databases | |
| eggNOG | fuNOG11170. |
| HOGENOM | HBG272480. |
| OrthoDB | EOG4V9XZX. |
Family and domain databases | |
| InterPro | IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. [Graphical view] |
| Pfam | PF00135. COesterase. 1 hit. [Graphical view] |
| PROSITE | PS00122. CARBOXYLESTERASE_B_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LIP1_YARLI | ||||||||
| Accession | Primary (citable) accession number: Q99156 Secondary accession number(s): Q6C6C2 | ||||||||
| 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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