Reviewed,
UniProtKB/Swiss-Prot Q71DJ5 (LIP1_ARATH)
Last modified
November 3, 2009.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Triacylglycerol lipase 1 EC=3.1.1.3 | ||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Complete proteome] | ||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis |
Protein attributes
| Sequence length | 393 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Triacylglycerol (TAG) lipase active on triolein, trioctanoin, tributyrin and 1,3-Diolein, but not on phospho- and galactolipids. May be involved but dispensable for TAG storage breakdown during seed germination. Ref.1 |
| Catalytic activity | Triacylglycerol + H2O = diacylglycerol + a carboxylate. |
| Subcellular location | Secreted Probable. |
| Tissue specificity | Expressed in seedlings, roots, leaves, flowers and siliques. Ref.1 |
| Sequence similarities | Belongs to the AB hydrolase superfamily. Lipase family. |
| Biophysicochemical properties | Kinetic parameters: Vmax=45 µmol/min/mg enzyme with triolein as a substrate pH dependence: Optimum pH is 6. Active between pH 4-7. |
| Sequence caution | The sequence AAD25569.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular space Ref.1 Traceable author statement. Source: TAIR |
| Molecular function | triglyceride lipase activity Ref.1 Inferred from direct assay. Source: TAIR |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 20 | 20 | Ref.1 | ||||||
| Chain | 21 – 393 | 373 | Triacylglycerol lipase 1 | PRO_0000234336 | |||||
Sites | |||||||||
| Active site | 166 | 1 | Nucleophile By similarity | ||||||
| Active site | 334 | 1 | Charge relay system By similarity | ||||||
| Active site | 363 | 1 | Charge relay system By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 41 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 261 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification and characterization of a triacylglycerol lipase in Arabidopsis homologous to mammalian acid lipases." El-Kouhen K., Blangy S., Ortiz E., Gardies A.-M., Ferte N., Arondel V. FEBS Lett. 579:6067-6073(2005) [PubMed: 16226259] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-28, FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. |
| [2] | "Triacylglycerol (steryl ester) hydrolase from Arabidopsis thaliana is involved in lipid homeostasy." Benveniste P., Noiriel A., Nave P., Schaller H. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. |
| [3] | "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. Venter J.C.Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
Cross-references
Sequence databases | |
|---|---|
| AF530477 mRNA. Translation: AAN77143.1. AC006298 Genomic DNA. Translation: AAD25569.1. Sequence problems. | |
| IPI | IPI00539331. |
| PIR | E84526. |
| RefSeq | NP_179126.2. |
| UniGene | At.40439 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1K8Q based on UniProtKB P80035. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 816012. |
| GenomeReviews | Gene locus AT2G15230 in contig CT485783_GR. |
| KEGG | ath:AT2G15230. |
| NMPDR | fig|3702.1.peg.8526. |
Organism-specific databases | |
| TAIR | At2g15230. |
Phylogenomic databases | |
| OMA | PIIERIN. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.3. 302. |
Gene expression databases | |
| Genevestigator | Q71DJ5. |
| GermOnline | AT2G15230. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR006693. AB_hydro_lipase. IPR000073. AB_hydrolase_1. IPR008262. Lipase_Ser_AS. [Graphical view] |
| Pfam | PF04083. Abhydro_lipase. 1 hit. PF00561. Abhydrolase_1. 1 hit. [Graphical view] |
| PROSITE | PS00120. LIPASE_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LIP1_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q71DJ5 Secondary accession number(s): Q9SKL5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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