IED ID | IndEnz0005000129 |
Enzyme Type ID | lipase000129 |
Protein Name |
Triacylglycerol lipase 1 EC 3.1.1.3 |
Gene Name | LIP1 At2g15230 F15A23.3 |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
Enzyme Sequence | MKWLLVAVLTSLTIFSALTQSHLLHGSPVNSLCADLIHPANYSCTEHSIQTKDGYILALQRVASLGPRLQSGPPVLLQHGLFMAGDVWFLNSPKESLGFILADHGFDVWVGNVRGTRYSYGHVTLSDTDKEFWDWSWQDLAMYDLAEMIQYLYSISNSKIFLVGHSQGTIMSFAALTQPHVAEMVEAAALLCPISYLDHVTAPLVERMVFMHLDQMVVALGLHQINFRSDMLVKLVDSLCEGHMDCTDFLTSITGTNCCFNASKIEYYLDYEPHPSSVKNIRHLFQMIRKGTFAQYDYGYFKNLRTYGLSKPPEFILSHIPASLPMWMGYGGTDGLADVTDVEHTLAELPSSPELLYLEDYGHIDFVLGSSAKEDVYKHMIQFFRAKVKSSSW |
Enzyme Length | 393 |
Uniprot Accession Number | Q71DJ5 |
Absorption | |
Active Site | ACT_SITE 166; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 334; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 363; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:16226259};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000269|PubMed:16226259}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:16226259};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000269|PubMed:16226259}; CATALYTIC ACTIVITY: Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) + octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978, ChEBI:CHEBI:88066; Evidence={ECO:0000269|PubMed:16226259};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865; Evidence={ECO:0000269|PubMed:16226259}; |
DNA Binding | |
EC Number | 3.1.1.3 |
Enzyme Function | FUNCTION: Triacylglycerol (TAG) lipase active on triolein, trioctanoin, tributyrin and 1,3-Diolein, but not on phospho- and galactolipids (PubMed:16226259). Involved but dispensable for TAG storage breakdown during seed germination (PubMed:16226259, PubMed:24989044). {ECO:0000269|PubMed:16226259, ECO:0000269|PubMed:24989044}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. Active between pH 4-7. {ECO:0000269|PubMed:16226259}; |
Pathway | PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000269|PubMed:16226259}. |
nucleotide Binding | |
Features | Active site (3); Chain (1); Erroneous gene model prediction (1); Glycosylation (2); Signal peptide (1) |
Keywords | Direct protein sequencing;Gibberellin signaling pathway;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal |
Interact With | |
Induction | INDUCTION: Stimulated during seed imbibition (PubMed:24989044). Induced by gibberellins (GAs) and repressed by DELLA proteins (e.g. GAI/RGA2, RGA/RGA1/GRS and RGL2/SCL19) in an ATML1- and PDF2-dependent manner (PubMed:24989044). Upon seed imbibition, increased GA levels in the epidermis reduce DELLA proteins abundance and release, in turn, ATML1 and PDF2 which activate LIP1 expression, thus enhancing germination potential (PubMed:24989044). {ECO:0000269|PubMed:24989044}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000269|PubMed:16226259 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 44,231 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=45 umol/min/mg enzyme with triolein as a substrate {ECO:0000269|PubMed:16226259}; |
Metal Binding | |
Rhea ID | RHEA:12044; RHEA:12045; RHEA:40475; RHEA:40476; RHEA:47864; RHEA:47865 |
Cross Reference Brenda | 3.1.1.3; |