Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
Atypical angiopoietin-like protein that regulates ANGPTL3.
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ANGPTL8 coexpression with ANGPTL3 causes hypertriglyceridemia.
"Plasma TAG level did not change in mice expressing ANGPTL3 alone, whereas coexpression with ANGPTL8 resulted in hypertriglyceridemia, despite a reduction in circulating ANGPTL3."
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ANGPTL8 increases N-terminal ANGPTL3 release.
"In cultured hepatocytes, ANGPTL8 expression increased the appearance of N-terminal ANGPTL3 in the medium, suggesting ANGPTL8 may activate ANGPTL3."
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ANGPTL8 needs ANGPTL3 to raise triglycerides.
"Consistent with this scenario, expression of ANGPTL8 in Angptl3(-/-) mice failed to promote hypertriglyceridemia."
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ANGPTL8 circulates in human plasma.
"ANGPTL8 is expressed in liver and adipose tissue, and circulates in plasma of humans."
ANGPTL8 requires ANGPTL3 to inhibit lipoprotein lipase and plasma triglyceride clearance.
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ANGPTL8 has a functional LPL inhibitory motif, active only with ANGPTL3.
"ANGPTL8 has a functional LPL inhibitory motif, but only inhibits LPL and increases plasma TG levels in mice in the presence of ANGPTL3"
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The complex's inhibitory activity mainly derives from ANGPTL8.
"suggesting the major inhibitory activity of this complex derives from ANGPTL8"
ANGPTL8 promotes the ability of ANGPTL3 to bind and inhibit lipoprotein lipase.
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ANGPTL3-ANGPTL8 complexes inhibit LPL much more than either alone.
"Importantly, ANGPTL3-ANGPTL8 complexes had a dramatically increased ability to inhibit LPL compared to either protein alone."
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ANGPTL8 increases ANGPTL3 binding to LPL.
"Protein interaction assays showed that ANGPTL8 greatly increased the ability of ANGPTL3 to bind LPL."
ANGPTL8 has both endocrine and autocrine effects on substrate utilization.
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Hepatic ANGPTL8 acts endocrinally; adipose ANGPTL8 acts locally on ANGPTL4.
"Thus, hepatic A8 (with A3) acts in an endocrine fashion to inhibit intravascular LPL in oxidative tissues, whereas A8 in adipose tissue enhances LPL activity by autocrine/paracrine inhibition of A4."
Angptl8 mediates food-driven resetting of hepatic circadian clock in mice.
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ANGPTL8 resets the liver clock via the membrane receptor PirB.
"Mechanistically, the resetting function of Angptl8 is dependent on the signal relay of the membrane receptor PirB, phosphorylation of kinases and transcriptional factors, and consequently transient activation of the central clock gene Per1."
ANGPTL8 is a negative regulator in pathological cardiac hypertrophy.
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ANGPTL8 binds LILRB3 (PIRB).
"Moreover, we demonstrated that ANGPTL8 directly bound to the paired Ig-like receptor PIRB (LILRB3) by RNA-seq and immunoprecipitation-mass screening."
Inhibition of ANGPTL8 protects against diabetes-associated cognitive dysfunction by reducing synaptic loss via the PirB signaling pathway.
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PirB knockout mice resist ANGPTL8-induced neuroinflammation.
"In vivo, PirB-/- mice exhibited resistance to ANGPTL8-induced neuroinflammation and synaptic damage."
The Arg59Trp variant in ANGPTL8 (betatrophin) is associated with total and HDL-cholesterol in American Indians and Mexican Americans and differentially affects cleavage of ANGPTL3.
ANGPTL8/betatrophin does not control pancreatic beta cell expansion.
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ANGPTL8 does not control beta cell expansion.
"ANGPTL8/betatrophin does not control pancreatic beta cell expansion."
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Angptl8 knockouts have low triglycerides but normal glucose homeostasis.
"revealed profound reduction of triglyceride levels, but no abnormalities in glucose homeostasis"
Toward an understanding of the protein interaction network of the human liver.
Affinage mechanistic annotation for ANGPTL8 (human)