| IED ID | IndEnz0005000293 |
| Enzyme Type ID | lipase000293 |
| Protein Name |
Angiopoietin-related protein 4 425O18-1 Angiopoietin-like protein 4 Fasting-induced adipose factor Hepatic fibrinogen/angiopoietin-related protein HFARP Secreted protein Bk89 Cleaved into: ANGPTL4 N-terminal chain; ANGPTL4 C-terminal chain |
| Gene Name | Angptl4 Farp Fiaf Ng27 |
| 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 | MRCAPTAGAALVLCAATAGLLSAQGRPAQPEPPRFASWDEMNLLAHGLLQLGHGLREHVERTRGQLGALERRMAACGNACQGPKGKDAPFKDSEDRVPEGQTPETLQSLQTQLKAQNSKIQQLFQKVAQQQRYLSKQNLRIQNLQSQIDLLAPTHLDNGVDKTSRGKRLPKMTQLIGLTPNATHLHRPPRDCQELFQEGERHSGLFQIQPLGSPPFLVNCEMTSDGGWTVIQRRLNGSVDFNQSWEAYKDGFGDPQGEFWLGLEKMHSITGNRGSQLAVQLQDWDGNAKLLQFPIHLGGEDTAYSLQLTEPTANELGATNVSPNGLSLPFSTWDQDHDLRGDLNCAKSLSGGWWFGTCSHSNLNGQYFHSIPRQRQERKKGIFWKTWKGRYYPLQATTLLIQPMEATAAS |
| Enzyme Length | 410 |
| Uniprot Accession Number | Q9Z1P8 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism (PubMed:15837923, PubMed:17609370, PubMed:29899519). May also play a role in regulating glucose homeostasis and insulin sensitivity (PubMed:15837923, PubMed:29899519). Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage (PubMed:14583458, PubMed:17130448, PubMed:21832056). Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro) (By similarity). Depending on context, may modulate tumor-related angiogenesis (Probable). {ECO:0000250|UniProtKB:Q9BY76, ECO:0000269|PubMed:14583458, ECO:0000269|PubMed:15837923, ECO:0000269|PubMed:17130448, ECO:0000269|PubMed:17609370, ECO:0000269|PubMed:21832056, ECO:0000269|PubMed:29899519, ECO:0000305|PubMed:14583458, ECO:0000305|PubMed:17130448}.; FUNCTION: [ANGPTL4 N-terminal chain]: Mediates inactivation of the lipoprotein lipase LPL, and thereby plays an important role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. Has higher activity in LPL inactivation than the uncleaved protein. {ECO:0000250|UniProtKB:Q9BY76}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Coiled coil (1); Disulfide bond (2); Domain (1); Glycosylation (3); Region (1); Sequence conflict (5); Signal peptide (1); Site (1) |
| Keywords | Angiogenesis;Coiled coil;Disulfide bond;Extracellular matrix;Glycoprotein;Lipid metabolism;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Induced in interstitial capillaries in response to hind leg ischemia (PubMed:17068295). Alterations in nutrition and leptin administration are found to modulate the expression in vivo. {ECO:0000269|PubMed:10866690, ECO:0000269|PubMed:17068295}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14583458, ECO:0000269|PubMed:15837923}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9BY76}. Note=The unprocessed form interacts with the extracellular matrix. This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4. {ECO:0000250|UniProtKB:Q9BY76}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9BY76}.; PTM: [ANGPTL4 N-terminal chain]: Forms disulfide-linked dimers and tetramers. {ECO:0000250|UniProtKB:Q9BY76}.; PTM: Cleaved into a smaller N-terminal chain and a larger chain that contains the fibrinogen C-terminal domain; both cleaved and uncleaved forms are detected in the extracellular space. The cleaved form is not present within the cell. {ECO:0000250|UniProtKB:Q9BY76}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11953136; 12401877; 12466851; 14610273; 15190076; 15292369; 15505215; 15659544; 15863837; 16081640; 16272564; 16602821; 16717449; 16837853; 16870142; 17088546; 17202268; 17210919; 17213385; 17579277; 17761937; 18340008; 18728224; 19094966; 19246456; 19318355; 19498055; 19542565; 19805517; 20043872; 20378851; 20472602; 20729546; 20798332; 20927337; 20952587; 21109191; 21151138; 21267068; 21398697; 21549101; 21966511; 22068616; 22086875; 22350948; 22538368; 22639947; 22815920; 22967998; 23176178; 23328524; 23640487; 23686315; 23959876; 24194600; 24220340; 24565756; 24591600; 24634819; 24726386; 24815769; 24932810; 24952961; 25660016; 25685701; 25864912; 25871848; 26069075; 26476336; 26621734; 26670924; 26671148; 26687026; 27034464; 27460411; 27573470; 27577973; 27624101; 27626380; 27694478; 27754788; 28143927; 28188788; 28215713; 28287161; 28412693; 28733267; 28740178; 28743803; 28752045; 28849063; 29436683; 29449313; 29502266; 29563332; 29627378; 29739862; 29952246; 29986868; 30021841; 30215691; 30518876; 30698048; 30905785; 30911775; 31053639; 31164474; 31409739; 31545295; 32195030; 32638512; 32686149; 33846453; 34396783; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,538 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |