Detail Information for IndEnz0005000660
IED ID IndEnz0005000660
Enzyme Type ID lipase000660
Protein Name Apolipoprotein C-I
Apo-CI
ApoC-I
Apolipoprotein C1
Liver regeneration-related protein LRRG04

Cleaved into: Truncated apolipoprotein C-I
Gene Name Apoc1
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 MRLFIALPVLIVVVAMALEGPAPAQAAPDFSSAMESLPDKLKEFGNTLEDKARAAIEHIKQKEIMIKTRNWFSETLNKMKEKLKTTFA
Enzyme Length 88
Uniprot Accession Number P19939
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein. {ECO:0000250|UniProtKB:P02654, ECO:0000250|UniProtKB:P33047}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (2); Signal peptide (1)
Keywords Lipid transport;Reference proteome;Secreted;Signal;Transport;VLDL
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02654}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..26
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 16282639;
Motif
Gene Encoded By
Mass 9,861
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda