Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person UniProt:Q9BY76-3 ANGPTL4
| Class:Id | ReferenceIsoform:8975871 |
|---|---|
| _chainChangeLog | signal peptide:1-25 added on Fri February 17 2017;chain:26-406 added on Fri February 17 2017;chain:26-163 for 8975871 added on Thu May 2 2019;chain:164-406 for 8975871 added on Thu May 2 2019 |
| _displayName | UniProt:Q9BY76-3 ANGPTL4 |
| _timestamp | 2024-11-03 20:17:52 |
| chain | signal peptide:1-25 chain:26-406 chain:26-163 chain:164-406 |
| checksum | 219E56FEB3F602AF |
| comment | 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:19270337, PubMed:21398697, PubMed:27929370, PubMed:29899144). May also play a role in regulating glucose homeostasis and insulin sensitivity (Probable). Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage (PubMed:14583458, PubMed:17068295). 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) (PubMed:17068295). Depending on context, may modulate tumor-related angiogenesis (By similarity).FUNCTION 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 (PubMed:19270337, PubMed:21398697, PubMed:27929370, PubMed:29899144). Has higher activity in LPL inactivation than the uncleaved protein (PubMed:19270337, PubMed:21398697).SUBUNIT Homooligomer; disulfide-linked via Cys residues in the N-terminal part of the protein (PubMed:19270337). The homooligomer undergoes proteolytic processing to release the ANGPTL4 C-terminal chain, which circulates as a monomer (PubMed:19270337). The homooligomer unprocessed form is able to interact with the extracellular matrix (PubMed:21398697).INTERACTION The unprocessed form interacts with the extracellular matrix (PubMed:17068295, PubMed:21398697). This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4 (Probable).ALTERNATIVE PRODUCTS Detected in blood plasma (at protein level) (PubMed:29899519). Detected in liver (PubMed:10698685). Detected in white fat tissue and placenta (PubMed:10866690). Expressed at high levels in the placenta, heart, liver, muscle, pancreas and lung but expressed poorly in the brain and kidney.INDUCTION Up-regulated when cells are exposed to severe hypoxia (in vitro).PTM N-glycosylated.PTM Forms disulfide-linked dimers and tetramers.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.POLYMORPHISM Genetic variations in ANGPTL4 are associated with low plasma triglyceride levels and define the plasma triglyceride level quantitative trait locus (TGQTL) [MIM:615881]. |
| created | [InstanceEdit:8964659] Weiser, JD |
| description | recommendedName: Angiopoietin-related protein 4 alternativeName: Angiopoietin-like protein 4 alternativeName: fullName evidence="18"Hepatic fibrinogen/angiopoietin-related protein shortName evidence="18"HFARP component recommendedName: ANGPTL4 N-terminal chain /component component recommendedName: ANGPTL4 C-terminal chain /component |
| geneName | ANGPTL4 ARP4 HFARP PGAR PP1158 PSEC0166 UNQ171/PRO197 |
| identifier | Q9BY76 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing Angiogenesis Coiled coil Direct protein sequencing Disulfide bond Extracellular matrix Glycoprotein Lipid metabolism Proteomics identification Reference proteome Secreted Signal |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | ANGPTL4 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:5640187] ENSEMBL:ENSG00000167772 ANGPTL4 [Homo sapiens] |
| secondaryIdentifier | ANGL4_HUMAN A8MY84 B4E089 D6W670 F5H0I2 Q53HQ6 Q53HU1 Q6UXN0 Q9HBV4 Q9NZU4 Q9Y5B3 |
| sequenceLength | 406 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | Q9BY76-3 |
| [Change default viewing format] | |
No pathways have been reviewed or authored by UniProt:Q9BY76-3 ANGPTL4 (8975871)
