| IED ID | IndEnz0005001453 |
| Enzyme Type ID | lipase001453 |
| Protein Name |
Apolipoprotein C-III Apo-CIII ApoC-III Apolipoprotein C3 |
| Gene Name | Apoc3 |
| 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 | MQPRMLLIVALVALLASARADEGEGSLLLGSMQGYMEQASKTVQDALSSMQESDIAVVASRGWMDNRFKSLKGYWSKFTDKFTGLWESGPEDQLTTPTLEP |
| Enzyme Length | 101 |
| Uniprot Accession Number | P06759 |
| 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); Glycosylation (1); Modified residue (1); Region (1); Signal peptide (1); Site (1) |
| Keywords | Chylomicron;Glycoprotein;Lipid degradation;Lipid metabolism;Lipid transport;Oxidation;Reference proteome;Secreted;Sialic acid;Signal;Transport;VLDL |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}. |
| Modified Residue | MOD_RES 64; /note=Methionine sulfoxide; /evidence=ECO:0000250|UniProtKB:P33622 |
| Post Translational Modification | PTM: The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-96 with a core 1 or possibly core 8 glycan. {ECO:0000250|UniProtKB:P02656}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10386582; 11177239; 15007394; 17201892; 20938723; 21183731; 21670290; 23542898; 24234421; 24804986; 28255847; 28473603; 4020294; 6419747; 6698975; 7811230; 8429259; 8491512; 9888873; |
| Motif | |
| Gene Encoded By | |
| Mass | 11,117 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |