| IED ID | IndEnz0005001009 |
| Enzyme Type ID | lipase001009 |
| Protein Name |
Apolipoprotein C-III Apo-CIII ApoC-III Apolipoprotein C3 |
| Gene Name | APOC3 |
| Organism | Sus scrofa (Pig) |
| 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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MQPRVLLVAGLLVLLACAQAIEAEDTSLLDKMQDYVKQATRTAQDALTSVKESEVAQQARGWVTDSISSLKDYWSTFKGKFTDFWDYTPKPEPSSS |
| Enzyme Length | 96 |
| Uniprot Accession Number | P27917 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners. {ECO:0000250|UniProtKB:P02656}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Region (1); Signal peptide (1) |
| Keywords | Chylomicron;Direct protein sequencing;Lipid degradation;Lipid metabolism;Lipid transport;Reference proteome;Secreted;Signal;Transport;VLDL |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 10,704 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |