IED ID | IndEnz0005001430 |
Enzyme Type ID | lipase001430 |
Protein Name |
Apolipoprotein C-I Apo-CI ApoC-I Apolipoprotein C1 Cleaved into: Truncated apolipoprotein C-I |
Gene Name | APOC1 |
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 | MRLILSLPVLVVVLSMVLEGPAPAQAAGEISSTFERIPDKLKEFGNTLEDKARAAIESIKKSDIPAKTRNWFSEAFKKVKEHLKTAFS |
Enzyme Length | 88 |
Uniprot Accession Number | P56595 |
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 | Direct protein sequencing;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; /evidence=ECO:0000269|PubMed:20483223 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 9,741 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |