Detail Information for IndEnz0005001457
IED ID IndEnz0005001457
Enzyme Type ID lipase001457
Protein Name Apolipoprotein C-II
Apo-CII
ApoC-II
Apolipoprotein C2

Cleaved into: Proapolipoprotein C-II
ProapoC-II
Gene Name Apoc2
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 MGSRFFLALFLALLVLGNEVQGTEEDDPGSSALLDTVQEHLFSYWNSAKAAAGELYQKTYLTSVDEKLRDMYSKSSAAMTTYAGIFTDQLLTLLKGE
Enzyme Length 97
Uniprot Accession Number G3V8D4
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. {ECO:0000250|UniProtKB:P02655}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (2); Region (2); Signal peptide (1)
Keywords Chylomicron;HDL;LDL;Lipid degradation;Lipid metabolism;Lipid transport;Reference proteome;Secreted;Signal;Transport;VLDL
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02655}.
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:0000250|UniProtKB:P02655}.; PTM: Proapolipoprotein C-II, the major form found in plasma undergoes proteolytic cleavage of its N-terminal hexapeptide to generate the mature form apolipoprotein C-II, which occurs as the minor form in plasma. {ECO:0000250|UniProtKB:P02655}.
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 4020294; 9888873;
Motif
Gene Encoded By
Mass 10,695
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda