Detail Information for IndEnz0005001008
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