| IED ID | IndEnz0005000221 |
| Enzyme Type ID | lipase000221 |
| Protein Name |
Apolipoprotein A-IV Apo-AIV ApoA-IV Apolipoprotein A4 |
| Gene Name | Apoa4 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MFLKAAVLTLALVAITGTRAEVTSDQVANVVWDYFTQLSNNAKEAVEQFQKTDVTQQLSTLFQDKLGDASTYADGVHNKLVPFVVQLSGHLAQETERVKEEIKKELEDLRDRMMPHANKVTQTFGENMQKLQEHLKPYAVDLQDQINTQTQEMKLQLTPYIQRMQTTIKENVDNLHTSMMPLATNLKDKFNRNMEELKGHLTPRANELKATIDQNLEDLRRSLAPLTVGVQEKLNHQMEGLAFQMKKNAEELQTKVSAKIDQLQKNLAPLVEDVQSKVKGNTEGLQKSLEDLNRQLEQQVEEFRRTVEPMGEMFNKALVQQLEQFRQQLGPNSGEVESHLSFLEKSLREKVNSFMSTLEKKGSPDQPQALPLPEQAQEQAQEQAQEQVQPKPLES |
| Enzyme Length | 395 |
| Uniprot Accession Number | P06728 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Natural variant (1); Region (2); Repeat (13); Sequence conflict (9); Signal peptide (1) |
| Keywords | Chylomicron;Direct protein sequencing;HDL;Lipid transport;Reference proteome;Repeat;Secreted;Signal;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10632725; 10926756; 11217851; 11478940; 11983814; 12105231; 12466851; 12810823; 14660441; 14974682; 14983036; 14999024; 15254593; 15306172; 15466464; 15928313; 15997185; 16109169; 16497661; 16498401; 16602821; 16615898; 16929032; 17222401; 17363460; 17641001; 17916774; 18188184; 18617288; 18678879; 19389805; 19968565; 21267068; 21356380; 21386911; 21840868; 22207575; 22209087; 22461023; 22619326; 23027805; 23132909; 23599044; 23684747; 23729668; 24030551; 24311788; 24598141; 24838500; 24929016; 25157093; 25209997; 2575592; 26294669; 27131369; 27655915; 28768657; 29263093; 29684311; 30190457; 31408538; 31462513; 31706944; 32410861; 33276196; 33444292; 33513710; 4000948; 6099394; 7798939; 8020488; 8354955; 9109435; 9186920; 9300780; 9323588; 9494081; 9616220; 9832509; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,029 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |