IED ID | IndEnz0010001938 |
Enzyme Type ID | esterase001938 |
Protein Name |
Putative lysosomal acid lipase/cholesteryl ester hydrolase Acid cholesteryl ester hydrolase LAL EC 3.1.1.13 Cholesteryl esterase Lipase A Sterol esterase |
Gene Name | |
Organism | Crotalus adamanteus (Eastern diamondback rattlesnake) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Crotalinae (pit vipers) Crotalus Crotalus adamanteus (Eastern diamondback rattlesnake) |
Enzyme Sequence | MWRLIIIAILFQGLVNSAMLERRKRGVDPETAMNISEIILFRGYPSEEYEVVTGDGYILCLNRIPYGKISQKTKEPKPAVFLQHGLLADGSNWVTNLDYNSLGFALADAGFDVWLGNSRGNTWSQKHINYTIKQKEFWMFSFNEMAMYDIPASVNFVLNKTGQEQLFYVGHSQGTTIGFIAFSVLPELAKKIKMFFGLAPVMTVKFSSGGLVKLGELPEFLLKEIFGTKQIFPQNAVIKWLATHVCGQVLIDELCGNFFFLLCGFNEKNLNMSRVEIYSTHCPAGTSVQNMLHWSQAVKSGEVRAFDWGSRKENMAHYKQPTPPPYKMERMLVPTALWTGGHDWLSDRKDIAILLTLIPNLIYHKEIPEWEHLDFIWGLDAPQRMFRDMIQMMHKVQYAH |
Enzyme Length | 400 |
Uniprot Accession Number | J3SDX8 |
Absorption | |
Active Site | ACT_SITE 172; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 372; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=a sterol ester + H2O = a fatty acid + a sterol + H(+); Xref=Rhea:RHEA:10100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15889, ChEBI:CHEBI:28868, ChEBI:CHEBI:35915; EC=3.1.1.13; |
DNA Binding | |
EC Number | 3.1.1.13 |
Enzyme Function | FUNCTION: In physiological conditions, is crucial for intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor-mediated endocytosis of lipoprotein particles. In venom, the biological contribution is unknown. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (1); Glycosylation (4); Signal peptide (1) |
Keywords | Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 45,807 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:10100 |
Cross Reference Brenda |