| IED ID | IndEnz0010000434 |
| Enzyme Type ID | esterase000434 |
| Protein Name |
Lysophospholipase NTE1 EC 3.1.1.5 Intracellular phospholipase B Neuropathy target esterase homolog |
| Gene Name | NTE1 YML059C YM9958.03C |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MRSMNCTTNNTNNTGQNTKNSLGSSFNSSNYTSYRFQTCLTDQIISEAQTWSLSSLFNFSWVVSYFVMGASRMIFRYGWYLATLSLLRIPKWIFFKLHHVQFTLSFWLILFALAVIVFVTYTIMKERILSQYKRLTPEFLPLENTGKSGSSANINAASTQSANAPPAIGSSTTGASSIIDSKKHSLKDGNENETFLSSYLDQFLSAIKIFGYLEKPVFHDLTKNMKTQKMDEGEILLLDSTIGFAIVVEGTLQLYHEVDHSDKDHGDETDHSDTDGLDDQDRDEEDEEEDDDIDNYDTKSCSSNLIDEEDESVGYIHLKNGLGNFQLLNTVKPGNPLTSLVSILNLFTHSMSSYGNSNFPSELSSPIDTTVSVNNMFCSSEQNFSNTDSMTNSTNSFPTFPSSMPKLVARAATDCTIGIIPPQSFAKLTAKYPRSASHIIQMVLTKLYHVTFQTAHDYLGLTKEIMDIEVLLNKSIVYELPYYLKEAVIRKFKTVDKSSGSADLEPKPKNSNASSKLKKPPKAKPSDGIIQSLKIANANANTSSNSLSLKPEFTHHPSSRHVVLGSRDQFNPGDLLSNVPLSRTMDILSPNPIHNNNRNKSNGINTSTSNQHKRSSRSSSNNASVHSKKFSSLSPELRNAQLSTSPLSLDNTSVHDHIHPSPVHLKGRVSPRPNLLPTTSFSAAQEETEDSALRMALVEAMLTYLGVNKSNMSVSSSSIANMSSLNSPQLNEMYSRRPSNASFLMSPHCTPSDISVASSFASPQTQPTMLRILPKEYTISNKRHNKSKSQDKKKPRAYKEELTPNLDFEDVKKDFAQGIQLKFFKKGTTIVEQNARGKGLFYIISGKVNVTTNSSSSVVSSMSKPEQVSAQSSHKGENPHHTQHLLYSVGSGGIVGYLSSLIGYKSFVNIVAKSDVYVGFLSSATLERLFDKYFLIYLRISDSLTKLLSSRLLKLDHALEWVHLRASETLFSQGDSANGIYVVLNGRLRQLQQQSLSNSNTSSEEVETQNIILGELAQGESFGEVEVLTAMNRYSTIVAVRDSELARIPRTLFELLALEHPSIMIRVSRLVAKKIVGDRTVPALTGDPLSIKENDFTSLIPPTKASYSSSLSHKPQNITSGTITFRTITILPITSGLPVEAFAMKLVQAFKQVGRTTIGLNQRTTLTHLGRHAFDRLSKLKQSGYFAELEEMYQTVVYISDTPVKSNWTRTCIAQGDCILLLADARSPSAEIGEYEKLLLNSKTTARTELILLHPERYVEPGLTHKWLRYRPWVHSHHHIQFSLTGTTLMNEGKMHVLNNGALALMDKLIQTEFSRKTQQNISKLLPDSIKNTVENFSSRFMKSKRQYYTPVHRHKNDFLRLARILSGQAIGLVLGGGGARGISHLGVIQAIEEQGIPVDVIGGTSIGSFVGGLYAKDYDLVPIYGRVKKFAGRISSIWRMLTDLTWPVTSYTTGHEFNRGIWKTFGDTRIEDFWIQYYCNSTNITDSVQEIHSFGYAWRYIRASMSLAGLLPPLEENGSMLLDGGYVDNLPVTEMRARGCQTIFAVDVGSADDRTPMEYGDSLNGFWIIFNRWNPFSSHPNIPNMAEIQVRLGYVASVNALEKAKNTPGVVYVRPPIEEYATLDFSKFEEIYHVGVDYGRIFLQGLIDDDKMPYIPGSQETTLNSQVPEFLLHRRNSI |
| Enzyme Length | 1679 |
| Uniprot Accession Number | Q04958 |
| Absorption | |
| Active Site | ACT_SITE 1406; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1524; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Activity Regulation | ACTIVITY REGULATION: Positively regulated by SEC14. Inhibited by organophosphorus esters in the order phenyl saligenin phosphate (PSP) > phenyldipentyl phosphinate (PDPP) = diisopropyl fluorophosphate (DFP) > and paraoxon (PXN). {ECO:0000269|PubMed:15044461, ECO:0000269|PubMed:15611060}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000269|PubMed:15044461};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000305|PubMed:15044461}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + 2 H2O = 2 a carboxylate + 2 H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:32907, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:29067, ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:15044461};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32908; Evidence={ECO:0000305|PubMed:15044461}; |
| DNA Binding | |
| EC Number | 3.1.1.5 |
| Enzyme Function | FUNCTION: Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium (PubMed:15044461, PubMed:15611060, PubMed:16777854). NTE1 activity impacts the repressing transcriptional activity of OPI1, the main regulator of phospholipid synthesis gene transcription (PubMed:19841481). {ECO:0000269|PubMed:15044461, ECO:0000269|PubMed:15611060, ECO:0000269|PubMed:16777854, ECO:0000269|PubMed:19841481}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 803..947; /note=cNMP 1; NP_BIND 943..1074; /note=cNMP 2 |
| Features | Active site (2); Chain (1); Compositional bias (4); Domain (1); Modified residue (10); Motif (3); Mutagenesis (1); Nucleotide binding (2); Region (6); Topological domain (3); Transmembrane (2) |
| Keywords | Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome;Repeat;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15044461}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15044461}. Lipid droplet {ECO:0000269|PubMed:24868093}. |
| Modified Residue | MOD_RES 300; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 312; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 632; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 634; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"; MOD_RES 653; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 661; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 670; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 680; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 739; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19779198"; MOD_RES 803; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18407956" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11805826; 16137924; 16267052; 16429126; 16554755; 16731034; 16781190; 16845888; 16884526; 17010666; 17559233; 17951629; 18367008; 18842580; 19536198; 22345606; 22989772; 23027642; 23139841; 23631861; 24040173; 24520995; 26819558; 9020587; |
| Motif | MOTIF 1377..1382; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1404..1408; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1524..1526; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 187,133 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177; RHEA:15178; RHEA:32907; RHEA:32908 |
| Cross Reference Brenda |