| IED ID | IndEnz0005000881 |
| Enzyme Type ID | lipase000881 |
| Protein Name |
Neutral cholesterol ester hydrolase 1 NCEH EC 3.1.1.- Arylacetamide deacetylase-like 1 |
| Gene Name | Nceh1 Aadacl1 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MRSSCVLLAALLALVAYYVYIPLPSAVSDPWKLMLLDATFRGAQQVSNLIHSLGLSHHLITLNFIIISFGKKSARSSPRVKVTDTDFDGVEVRVFEGPPKPDEPLRRSVVYIHGGGWALASAKISYYDQLCTAMAEELNAVIVSIEYRLVPQVYFPEQIHDVIRATKYFLQPEVLDKYKVDPGRVGVSGDSAGGNLAAALGQQFTYVESLKNKLKLQALIYPVLQALDFNTPSYQQSMNTPILPRHVMVRYWVDYFKGNYDFVEAMIVNNHTSLDVERAAALRARLDWTSLLPSSIKKNYKPVLQTIGDARIVKEIPQLLDAAASPLIAEQEVLQALPKTYILTCEHDVLRDDGIMYAKRLESAGVNVTLDHFEDGFHGCMIFTSWPTNFSVGIRTRDSYFKWLDQNL |
| Enzyme Length | 408 |
| Uniprot Accession Number | B2GV54 |
| Absorption | |
| Active Site | ACT_SITE 191; /evidence=ECO:0000255|PROSITE-ProRule:PRU10038; ACT_SITE 348; /evidence=ECO:0000255|PROSITE-ProRule:PRU10038; ACT_SITE 378; /evidence=ECO:0000255|PROSITE-ProRule:PRU10038 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate + cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823, ChEBI:CHEBI:46898; Evidence={ECO:0000250|UniProtKB:Q8BLF1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876; Evidence={ECO:0000250|UniProtKB:Q8BLF1}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + H2O = 1-O-hexadecyl-sn-glycerol + acetate + H(+); Xref=Rhea:RHEA:38563, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:34115, ChEBI:CHEBI:75936; Evidence={ECO:0000250|UniProtKB:Q8BLF1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38564; Evidence={ECO:0000250|UniProtKB:Q8BLF1}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Hydrolyzes 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor (By similarity). May be responsible for cholesterol ester hydrolysis in macrophages (By similarity). Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds (By similarity). {ECO:0000250|UniProtKB:Q8BLF1}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (3); Motif (1); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Endoplasmic reticulum;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Microsome;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6PIU2}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6PIU2}. Microsome {ECO:0000250|UniProtKB:Q8BLF1}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6PIU2}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 113..115; /note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole; /evidence=ECO:0000250|UniProtKB:Q5NUF3 |
| Gene Encoded By | |
| Mass | 45,822 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:33875; RHEA:33876; RHEA:38563; RHEA:38564 |
| Cross Reference Brenda |