Detail Information for IndEnz0005001011
IED ID IndEnz0005001011
Enzyme Type ID lipase001011
Protein Name Apolipoprotein C-III
Apo-CIII
ApoC-III
Apolipoprotein C3
Gene Name APOC3
Organism Canis lupus familiaris (Dog) (Canis familiaris)
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 Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris)
Enzyme Sequence MQPRVLLVAALLALLASARALEEEDPSLLGLMQGYMQHATKTAQDTLTSVQESQVAQRARGWMTDSFSSLKDYCSTFKGKFTGFWDSASEAKPTPASDAF
Enzyme Length 100
Uniprot Accession Number P12279
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 63; /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-94 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 -
Motif
Gene Encoded By
Mass 10,906
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda