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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
UniProtKB entry P01275 (GLUC_HUMAN), Pro-glucagon
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Proglucagon is processed tissue-specifically; glucagon predominates in pancreatic A cells (PCSK2/PC2), while GLP-1, GLP-2, glicentin and oxyntomodulin are liberated in intestinal L cells (PCSK1/PC1).
"Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells"
Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism.
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Glucagon is one of four substrates co-crystallized with insulin-degrading enzyme (IDE), supporting glucagon as an IDE degradation substrate.
"structures of human IDE in complex with four substrates (insulin B chain, amyloid-beta peptide (1-40), amylin and glucagon)"
Crystal structure of the incretin-bound extracellular domain of a G protein-coupled receptor.
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Structural study of the GIP receptor extracellular domain bound to the incretin GIP; the structural principles are stated to be conserved among related class B hormone receptors such as GLP1R.
"the crystal structure of the complex of human GIP receptor extracellular domain (ECD) with its agonist, the incretin GIP(1-42)"
Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-α.
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GLP-1 is a (slow) substrate of fibroblast activation protein (FAP), in addition to being an efficient DPP4 substrate.
"FAP slowly hydrolysed other hormone peptides, such as the incretins glucagon-like peptide-1 and glucose-dependent insulinotropic peptide"
Interleukin-6 enhances insulin secretion by increasing glucagon-like peptide-1 secretion from L cells and alpha cells.
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IL-6 increases GLP-1 production from alpha cells by upregulating proglucagon (GCG) and prohormone convertase 1/3, enhancing insulin secretion.
"IL-6 increased GLP-1 production from alpha cells through increased proglucagon (which is encoded by GCG) and prohormone convertase 1/3 expression"
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GLP-1 is a hormone that induces insulin secretion (incretin).
"Glucagon-like peptide-1 (GLP-1) is a hormone that induces insulin secretion"
Mapping out the multistage fibrillation of glucagon.
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Glucagon self-assembles into multiple morphological types of amyloid-like fibrils in vitro, the basis of the identical protein binding annotation.
"The 29-residue peptide hormone glucagon forms many different morphological types of amyloid-like fibrils"
A microbial amino-acid-conjugated bile acid, tryptophan-cholic acid, improves glucose homeostasis via the orphan receptor MRGPRE.
Synergistic activation of the type I adenylyl cyclase by Ca2+ and Gs-coupled receptors in vivo.
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Glucagon, acting through its Gs-coupled receptor, synergizes with Ca2+ to activate type I adenylyl cyclase; used here as a Gs-coupled receptor agonist.
"500 nM glucagon alone did not stimulate the enzyme but the combination of A23187 and glucagon activated the enzyme"
A role for glucagon-like peptide-1 in the central regulation of feeding.
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Central (ICV) GLP-1 inhibits feeding and is a physiological mediator of satiety, establishing GLP-1's role in feeding behavior.
"central GLP-1 is a new physiological mediator of satiety"
Prototypic G protein-coupled receptor for the intestinotrophic factor glucagon-like peptide 2.
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GLP-2 is intestinotrophic and acts through its own distinct receptor (GLP2R), stimulating villus growth, crypt proliferation, and reduced enterocyte apoptosis.
"GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis"
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GLP-2 exerts its actions through a distinct, specific receptor expressed in the gut, like glucagon and GLP-1 acting through their own receptors.
"GLP-2, like glucagon and GLP-1, exerts its actions through a distinct and specific novel receptor expressed in its principal target tissue"
Glucagon binds to Glucagon receptor
Liganded Gs-activating GPCR acts as a GEF for Gs
Liganded Gq/11-activating GPCRs act as GEFs for Gq/11
Glucagon-like Peptide-1 (GLP1) regulates insulin secretion
Synthesis of Preproglucagon in intestinal L cells
Glucagon-like Peptide 1 is secreted from intestinal L cells
Glucagon-like receptor 2 binds GLP2
Proglucagon translocates from the ER Lumen to secretory granules
The Ligand:GPCR:Gs complex dissociates
Liganded Gs-activating GPCRs bind inactive heterotrimeric Gs
Liganded Gq-activating GPCRs bind inactive heterotrimeric Gq
The Ligand:GPCR:Gq complex dissociates
Glucagon:GCGR mediates GTP-GDP exchange
DPP4(39-766) hydrolyzes Glucagon-like Peptide-1 (GLP-1)
DPP4(1-766) hydrolyzes Glucagon-like Peptide-1 (GLP-1)