IED ID | IndEnz0005001008 |
Enzyme Type ID | lipase001008 |
Protein Name |
Apolipoprotein C-II Apo-CII ApoC-II Apolipoprotein C2 Cleaved into: Proapolipoprotein C-II ProapoC-II |
Gene Name | APOC2 APC2 |
Organism | Homo sapiens (Human) |
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MGTRLLPALFLVLLVLGFEVQGTQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE |
Enzyme Length | 101 |
Uniprot Accession Number | P02655 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. In normolipidemic individuals, it is mainly distributed in the HDL, whereas in hypertriglyceridemic individuals, predominantly found in the VLDL and LDL. {ECO:0000269|PubMed:2209608, ECO:0000303|PubMed:22304839}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (4); Chain (2); Helix (3); Natural variant (4); Region (3); Sequence conflict (2); Signal peptide (1); Turn (4) |
Keywords | 3D-structure;Chylomicron;Direct protein sequencing;Disease variant;Glycoprotein;HDL;Hyperlipidemia;LDL;Lipid degradation;Lipid metabolism;Lipid transport;Reference proteome;Secreted;Sialic acid;Signal;Transport;VLDL |
Interact With | P49638; Itself |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3525527}. |
Modified Residue | |
Post Translational Modification | PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing glycoprotein which is subsequently desialylated prior to its proteolytic processing. {ECO:0000269|PubMed:3525527}.; PTM: Proapolipoprotein C-II, the major form found in plasma undergoes proteolytic cleavage of its N-terminal hexapeptide to generate apolipoprotein C-II, which occurs as the minor form in plasma. {ECO:0000269|PubMed:3525527}. |
Signal Peptide | SIGNAL 1..22; /evidence="ECO:0000269|PubMed:194244, ECO:0000269|PubMed:6706938" |
Structure 3D | NMR spectroscopy (4) |
Cross Reference PDB | 1BY6; 1I5J; 1O8T; 1SOH; |
Mapped Pubmed ID | 10335523; 10903476; 11060341; 11331005; 11751863; 11930616; 12032151; 12220441; 12450397; 12590574; 12682050; 12782148; 1279089; 14746139; 15031287; 15174051; 15209504; 15583000; 15778093; 16200213; 16432277; 16459141; 16763159; 16968945; 17018885; 17174330; 17222387; 17429947; 17717288; 17855807; 18005990; 18193044; 18206908; 18507396; 1856611; 18660489; 18802019; 18852267; 19034041; 19060906; 19197348; 19336370; 19336475; 19534808; 19878569; 19913121; 19948975; 20031551; 20042600; 20331378; 20430392; 20498921; 20571754; 20628086; 20634891; 20714348; 20864672; 20972250; 21146539; 21321243; 21476595; 21666694; 21943158; 21985034; 22239554; 22244853; 22262056; 22808166; 23300094; 23631828; 25172036; 26026161; 26196342; 2793848; 28229588; 28534127; 2892779; 29371683; 29791776; 30686043; 31133485; 31935511; 31975384; 32205061; 32332429; 32332431; 33934596; 34556808; 3942763; 4345202; 5057882; 7683668; 8245722; 8530039; 8728311; 9064379; 9792993; 9925661; |
Motif | |
Gene Encoded By | |
Mass | 11,284 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |