Detail Information for IndEnz0005000093
IED ID IndEnz0005000093
Enzyme Type ID lipase000093
Protein Name Neutral cholesterol ester hydrolase 1
NCEH
EC 3.1.1.-
Arylacetamide deacetylase-like 1
Gene Name NCEH1 AADACL1 KIAA1363
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MRSSCVLLTALVALAAYYVYIPLPGSVSDPWKLMLLDATFRGAQQVSNLIHYLGLSHHLLALNFIIVSFGKKSAWSSAQVKVTDTDFDGVEVRVFEGPPKPEEPLKRSVVYIHGGGWALASAKIRYYDELCTAMAEELNAVIVSIEYRLVPKVYFPEQIHDVVRATKYFLKPEVLQKYMVDPGRICISGDSAGGNLAAALGQQFTQDASLKNKLKLQALIYPVLQALDFNTPSYQQNVNTPILPRYVMVKYWVDYFKGNYDFVQAMIVNNHTSLDVEEAAAVRARLNWTSLLPASFTKNYKPVVQTTGNARIVQELPQLLDARSAPLIADQAVLQLLPKTYILTCEHDVLRDDGIMYAKRLESAGVEVTLDHFEDGFHGCMIFTSWPTNFSVGIRTRNSYIKWLDQNL
Enzyme Length 408
Uniprot Accession Number Q6PIU2
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=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:0000269|PubMed:17052608};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38564; Evidence={ECO:0000305|PubMed:17052608}; 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};
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 (PubMed:17052608). May be responsible for cholesterol ester hydrolysis in macrophages (By similarity). Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds (By similarity). May contribute to cancer pathogenesis by promoting tumor cell migration (PubMed:17052608). {ECO:0000250|UniProtKB:Q8BLF1, ECO:0000269|PubMed:17052608}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (2); Chain (1); Erroneous initiation (8); Glycosylation (3); Motif (1); Natural variant (3); Sequence conflict (6); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;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:0000269|PubMed:17052608, ECO:0000305|PubMed:12149457}; Single-pass type II membrane protein {ECO:0000305|PubMed:12149457}. Microsome {ECO:0000250|UniProtKB:Q8BLF1}.
Modified Residue
Post Translational Modification PTM: N-glycosylated. {ECO:0000269|PubMed:12149457, ECO:0000269|PubMed:19159218}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 17052604; 19592704; 19851296; 20198315; 20217867; 20353815; 20947831; 23993462; 24868095; 25280398; 26496610; 26617293; 27015452; 28934392; 32321446; 33219617;
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 45,808
Kinetics
Metal Binding
Rhea ID RHEA:38563; RHEA:38564; RHEA:33875; RHEA:33876
Cross Reference Brenda 3.1.1.13;