ID GLUC_HUMAN Reviewed; 180 AA. AC P01275; A6NN65; Q53TP6; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 3. DT 13-FEB-2019, entry version 202. DE RecName: Full=Glucagon; DE Contains: DE RecName: Full=Glicentin; DE Contains: DE RecName: Full=Glicentin-related polypeptide; DE Short=GRPP; DE Contains: DE RecName: Full=Oxyntomodulin; DE Short=OXM; DE Short=OXY; DE Contains: DE RecName: Full=Glucagon; DE Contains: DE RecName: Full=Glucagon-like peptide 1; DE Short=GLP-1; DE AltName: Full=Incretin hormone; DE Contains: DE RecName: Full=Glucagon-like peptide 1(7-37); DE Short=GLP-1(7-37); DE Contains: DE RecName: Full=Glucagon-like peptide 1(7-36); DE Short=GLP-1(7-36); DE Contains: DE RecName: Full=Glucagon-like peptide 2; DE Short=GLP-2; DE Flags: Precursor; GN Name=GCG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2901414; RA Drucker D.J., Asa S.; RT "Glucagon gene expression in vertebrate brain."; RL J. Biol. Chem. 263:13475-13478(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3725587; DOI=10.1093/nar/14.12.4719; RA White J.W., Saunders G.F.; RT "Structure of the human glucagon gene."; RL Nucleic Acids Res. 14:4719-4730(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=6877358; DOI=10.1038/304368a0; RA Bell G.I., Sanchez-Pescador R., Laybourn P.J., Najarian R.C.; RT "Exon duplication and divergence in the human preproglucagon gene."; RL Nature 304:368-371(1983). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 53-81. RX PubMed=11946536; DOI=10.1016/0014-5793(72)80192-3; RA Thomsen J., Kristiansen K., Brunfeldt K., Sundby F.; RT "The amino acid sequence of human glucagon."; RL FEBS Lett. 21:315-319(1972). RN [8] RP PROTEIN SEQUENCE OF 98-127, AND AMIDATION AT ARG-127. RX PubMed=2753890; RA Orskov C., Bersani M., Johnsen A.H., Hoejrup P., Holst J.J.; RT "Complete sequences of glucagon-like peptide-1 from human and pig RT small intestine."; RL J. Biol. Chem. 264:12826-12829(1989). RN [9] RP FUNCTION OF GLP1 BIOACTIVE FORMS. RX PubMed=8482423; DOI=10.2337/diab.42.5.658; RA Orskov C., Wettergren A., Holst J.J.; RT "Biological effects and metabolic rates of glucagonlike peptide-1 7-36 RT amide and glucagonlike peptide-1 7-37 in healthy subjects are RT indistinguishable."; RL Diabetes 42:658-661(1993). RN [10] RP FUNCTION OF OXYNTOMODULIN. RX PubMed=14557443; DOI=10.1210/jc.2003-030421; RA Cohen M.A., Ellis S.M., Le Roux C.W., Batterham R.L., Park A., RA Patterson M., Frost G.S., Ghatei M.A., Bloom S.R.; RT "Oxyntomodulin suppresses appetite and reduces food intake in RT humans."; RL J. Clin. Endocrinol. Metab. 88:4696-4701(2003). RN [11] RP FUNCTION OF GLICENTIN. RX PubMed=14632334; DOI=10.1080/08035250310000514; RA Tadokoro R., Shimizu T., Hosaka A., Kaneko N., Satoh Y., Yamashiro Y.; RT "Postnatal and postprandial changes in plasma concentrations of RT glicentin in term and preterm infants."; RL Acta Paediatr. 92:1175-1179(2003). RN [12] RP PROTEOLYTIC PROCESSING BY PCSK2. RX PubMed=9287128; DOI=10.1016/S0014-5793(97)00892-2; RA Rouille Y., Bianchi M., Irminger J.C., Halban P.A.; RT "Role of the prohormone convertase PC2 in the processing of RT proglucagon to glucagon."; RL FEBS Lett. 413:119-123(1997). RN [13] RP PROTEOLYTIC PROCESSING BY PCSK1. RX PubMed=12651102; DOI=10.1016/S1046-5928(02)00653-8; RA Bonic A., Mackin R.B.; RT "Expression, purification, and PC1-mediated processing of human RT proglucagon, glicentin, and major proglucagon fragment."; RL Protein Expr. Purif. 28:15-24(2003). RN [14] RP REVIEW. RX PubMed=14719035; DOI=10.1139/y03-107; RA Brubaker P.L., Anini Y.; RT "Direct and indirect mechanisms regulating secretion of glucagon-like RT peptide-1 and glucagon-like peptide-2."; RL Can. J. Physiol. Pharmacol. 81:1005-1012(2003). RN [15] RP REVIEW. RX PubMed=12554744; DOI=10.1210/me.2002-0306; RA Drucker D.J.; RT "Glucagon-like peptides: regulators of cell proliferation, RT differentiation, and apoptosis."; RL Mol. Endocrinol. 17:161-171(2003). RN [16] RP REVIEW. RX PubMed=12626323; DOI=10.1152/ajpendo.00492.2002; RA Jiang G., Zhang B.B.; RT "Glucagon and regulation of glucose metabolism."; RL Am. J. Physiol. 284:E671-E678(2003). RN [17] RP REVIEW. RX PubMed=10322410; DOI=10.1016/S1043-2760(98)00136-2; RA Drucker D.J.; RT "Glucagon-like peptide 2."; RL Trends Endocrinol. Metab. 10:153-156(1999). RN [18] RP REVIEW. RX PubMed=10605628; DOI=10.1210/edrv.20.6.0385; RA Kieffer T.J., Habener J.F.; RT "The glucagon-like peptides."; RL Endocr. Rev. 20:876-913(1999). RN [19] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 53-81. RX PubMed=9667960; DOI=10.1021/jm980084a; RA Sturm N.S., Lin Y., Burley S.K., Krstenansky J.L., Ahn J.-M., RA Azizeh B.Y., Trivedi D., Hruby V.J.; RT "Structure-function studies on positions 17, 18, and 21 replacement RT analogues of glucagon: the importance of charged residues and salt RT bridges in glucagon biological activity."; RL J. Med. Chem. 41:2693-2700(1998). RN [20] RP STRUCTURE BY NMR OF 98-127. RX PubMed=11943215; DOI=10.1016/S0014-5793(02)02466-3; RA Chang X., Keller D., O'Donoghue S.I., Led J.J.; RT "NMR studies of the aggregation of glucagon-like peptide-1: formation RT of a symmetric helical dimer."; RL FEBS Lett. 515:165-170(2002). RN [21] RP STRUCTURE BY NMR OF GLUCAGON ANTAGONIST. RX PubMed=12627948; DOI=10.1021/bi026629r; RA Ying J., Ahn J.-M., Jacobsen N.E., Brown M.F., Hruby V.J.; RT "NMR solution structure of the glucagon antagonist [desHis1, desPhe6, RT Glu9]glucagon amide in the presence of perdeuterated RT dodecylphosphocholine micelles."; RL Biochemistry 42:2825-2835(2003). CC -!- FUNCTION: Glucagon plays a key role in glucose metabolism and CC homeostasis. Regulates blood glucose by increasing gluconeogenesis CC and decreasing glycolysis. A counterregulatory hormone of insulin, CC raises plasma glucose levels in response to insulin-induced CC hypoglycemia. Plays an important role in initiating and CC maintaining hyperglycemic conditions in diabetes. CC -!- FUNCTION: GLP-1 is a potent stimulator of glucose-dependent CC insulin release. Play important roles on gastric motility and the CC suppression of plasma glucagon levels. May be involved in the CC suppression of satiety and stimulation of glucose disposal in CC peripheral tissues, independent of the actions of insulin. Have CC growth-promoting activities on intestinal epithelium. May also CC regulate the hypothalamic pituitary axis (HPA) via effects on LH, CC TSH, CRH, oxytocin, and vasopressin secretion. Increases islet CC mass through stimulation of islet neogenesis and pancreatic beta CC cell proliferation. Inhibits beta cell apoptosis. CC -!- FUNCTION: GLP-2 stimulates intestinal growth and up-regulates CC villus height in the small intestine, concomitant with increased CC crypt cell proliferation and decreased enterocyte apoptosis. The CC gastrointestinal tract, from the stomach to the colon is the CC principal target for GLP-2 action. Plays a key role in nutrient CC homeostasis, enhancing nutrient assimilation through enhanced CC gastrointestinal function, as well as increasing nutrient CC disposal. Stimulates intestinal glucose transport and decreases CC mucosal permeability. CC -!- FUNCTION: Oxyntomodulin significantly reduces food intake. CC Inhibits gastric emptying in humans. Suppression of gastric CC emptying may lead to increased gastric distension, which may CC contribute to satiety by causing a sensation of fullness. CC -!- FUNCTION: Glicentin may modulate gastric acid secretion and the CC gastro-pyloro-duodenal activity. May play an important role in CC intestinal mucosal growth in the early period of life. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-7629173, EBI-7629173; CC P27487:DPP4; NbExp=4; IntAct=EBI-7629173, EBI-2871277; CC Q12884:FAP; NbExp=4; IntAct=EBI-7629173, EBI-4319803; CC P48546:GIPR; NbExp=2; IntAct=EBI-7629173, EBI-15653881; CC P14735-1:IDE; NbExp=3; IntAct=EBI-7629173, EBI-15607031; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Glucagon is secreted in the A cells of the CC islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin CC are secreted from enteroendocrine cells throughout the CC gastrointestinal tract. GLP-1 and GLP-2 are also secreted in CC selected neurons in the brain. CC -!- INDUCTION: Glucagon release is stimulated by hypoglycemia and CC inhibited by hyperglycemia, insulin, and somatostatin. GLP-1 and CC GLP-2 are induced in response to nutrient ingestion. CC -!- PTM: Proglucagon is post-translationally processed in a tissue- CC specific manner in pancreatic A cells and intestinal L cells. In CC pancreatic A cells, the major bioactive hormone is glucagon CC cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 CC liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is CC further N-terminally truncated by post-translational processing in CC the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. CC The C-terminal amidation is neither important for the metabolism CC of GLP-1 nor for its effects on the endocrine pancreas. CC {ECO:0000269|PubMed:12651102, ECO:0000269|PubMed:2753890, CC ECO:0000269|PubMed:9287128}. CC -!- PHARMACEUTICAL: Available under the names Glucagon (Eli Lilly) and CC GlucaGen or Glucagon Novo Nordisk (Novo Nordisk). Used to treat CC severe hypoglycemia in insulin-dependent diabetics. CC -!- MISCELLANEOUS: In the glucagon antagonist, His-53 and Phe-58 are CC missing. This antagonist has been successfully utilized to reduce CC glucose concentration in vivo. CC -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Glucagon at Eli Lilly; Note=Clinical CC information on Eli Lilly glucagon products; CC URL="http://www.lillyDiabetes.com/Products/PatientInfo.cfm"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; J04040; AAA52567.1; -; mRNA. DR EMBL; X03991; CAA27627.1; -; Genomic_DNA. DR EMBL; V01515; CAA24759.1; -; Genomic_DNA. DR EMBL; BT006813; AAP35459.1; -; mRNA. DR EMBL; AC007750; AAY24204.1; -; Genomic_DNA. DR EMBL; BC005278; AAH05278.1; -; mRNA. DR CCDS; CCDS46439.1; -. DR PIR; A24377; GCHU. DR RefSeq; NP_002045.1; NM_002054.4. DR UniGene; Hs.516494; -. DR UniGene; Hs.741174; -. DR PDB; 1BH0; X-ray; 3.00 A; A=53-81. DR PDB; 1D0R; NMR; -; A=98-127. DR PDB; 1NAU; NMR; -; A=59-81. DR PDB; 2G49; X-ray; 2.50 A; C/D=53-81. DR PDB; 2L63; NMR; -; A=146-178. DR PDB; 2L64; NMR; -; A=146-178. DR PDB; 2M5P; NMR; -; X=53-81. DR PDB; 2M5Q; NMR; -; X=53-81. DR PDB; 3IOL; X-ray; 2.10 A; B=98-128. DR PDB; 4APD; NMR; -; A=98-128. DR PDB; 4ZGM; X-ray; 1.80 A; B=98-128. DR PDB; 5OTU; X-ray; 1.80 A; B/D=98-128. DR PDB; 5OTV; X-ray; 2.00 A; B/D=98-128. DR PDB; 5OTW; X-ray; 2.10 A; B/D=98-128. DR PDB; 5OTX; X-ray; 2.00 A; B/D=98-128. DR PDB; 5VAI; EM; 4.10 A; P=98-128. DR PDB; 5YQZ; X-ray; 3.00 A; P=54-81. DR PDBsum; 1BH0; -. DR PDBsum; 1D0R; -. DR PDBsum; 1NAU; -. DR PDBsum; 2G49; -. DR PDBsum; 2L63; -. DR PDBsum; 2L64; -. DR PDBsum; 2M5P; -. DR PDBsum; 2M5Q; -. DR PDBsum; 3IOL; -. DR PDBsum; 4APD; -. DR PDBsum; 4ZGM; -. DR PDBsum; 5OTU; -. DR PDBsum; 5OTV; -. DR PDBsum; 5OTW; -. DR PDBsum; 5OTX; -. DR PDBsum; 5VAI; -. DR PDBsum; 5YQZ; -. DR ProteinModelPortal; P01275; -. DR SMR; P01275; -. DR BioGrid; 108911; 19. DR DIP; DIP-46470N; -. DR IntAct; P01275; 7. DR MINT; P01275; -. DR STRING; 9606.ENSP00000387662; -. DR BindingDB; P01275; -. DR ChEMBL; CHEMBL5736; -. DR iPTMnet; P01275; -. DR PhosphoSitePlus; P01275; -. DR BioMuta; GCG; -. DR DMDM; 125987831; -. DR jPOST; P01275; -. DR PaxDb; P01275; -. DR PeptideAtlas; P01275; -. DR PRIDE; P01275; -. DR ProteomicsDB; 51367; -. DR DNASU; 2641; -. DR Ensembl; ENST00000375497; ENSP00000364647; ENSG00000115263. DR Ensembl; ENST00000418842; ENSP00000387662; ENSG00000115263. DR GeneID; 2641; -. DR KEGG; hsa:2641; -. DR UCSC; uc002ucc.5; human. DR CTD; 2641; -. DR DisGeNET; 2641; -. DR EuPathDB; HostDB:ENSG00000115263.14; -. DR GeneCards; GCG; -. DR HGNC; HGNC:4191; GCG. DR HPA; CAB000040; -. DR HPA; HPA036760; -. DR HPA; HPA036761; -. DR MIM; 138030; gene. DR neXtProt; NX_P01275; -. DR OpenTargets; ENSG00000115263; -. DR PharmGKB; PA28606; -. DR eggNOG; ENOG410IKZ8; Eukaryota. DR eggNOG; ENOG4111VKC; LUCA. DR GeneTree; ENSGT00390000005372; -. DR HOGENOM; HOG000231876; -. DR HOVERGEN; HBG003010; -. DR InParanoid; P01275; -. DR KO; K05259; -. DR OMA; INWLLQT; -. DR OrthoDB; 1349644at2759; -. DR PhylomeDB; P01275; -. DR TreeFam; TF332333; -. DR Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation. DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1). DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR Reactome; R-HSA-420092; Glucagon-type ligand receptors. DR Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin. DR SIGNOR; P01275; -. DR ChiTaRS; GCG; human. DR EvolutionaryTrace; P01275; -. DR GeneWiki; Glucagon; -. DR GenomeRNAi; 2641; -. DR PMAP-CutDB; P01275; -. DR PRO; PR:P01275; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000115263; Expressed in 66 organ(s), highest expression level in islet of Langerhans. DR Genevisible; P01275; HS. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0031769; F:glucagon receptor binding; IBA:GO_Central. DR GO; GO:0005179; F:hormone activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0008283; P:cell population proliferation; TAS:ProtInc. DR GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome. DR GO; GO:0007631; P:feeding behavior; TAS:ProtInc. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome. DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central. DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IEA:Ensembl. DR GO; GO:0090280; P:positive regulation of calcium ion import; IEA:Ensembl. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:0035948; P:positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IEA:Ensembl. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IBA:GO_Central. DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl. DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl. DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl. DR GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl. DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central. DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR015550; Glucagon. DR InterPro; IPR000532; Glucagon_GIP_secretin_VIP. DR PANTHER; PTHR11418; PTHR11418; 1. DR Pfam; PF00123; Hormone_2; 3. DR PRINTS; PR00275; GLUCAGON. DR SMART; SM00070; GLUCA; 3. DR PROSITE; PS00260; GLUCAGON; 4. PE 1: Evidence at protein level; KW 3D-structure; Amidation; Cleavage on pair of basic residues; KW Complete proteome; Direct protein sequencing; Hormone; Pharmaceutical; KW Phosphoprotein; Polymorphism; Reference proteome; Secreted; Signal. FT SIGNAL 1 20 FT PEPTIDE 21 89 Glicentin. {ECO:0000250}. FT /FTId=PRO_0000011253. FT PEPTIDE 21 50 Glicentin-related polypeptide. FT {ECO:0000250}. FT /FTId=PRO_0000011254. FT PEPTIDE 53 89 Oxyntomodulin. {ECO:0000250}. FT /FTId=PRO_0000011255. FT PEPTIDE 53 81 Glucagon. FT /FTId=PRO_0000011256. FT PROPEP 84 89 FT /FTId=PRO_0000011257. FT PEPTIDE 92 128 Glucagon-like peptide 1. FT /FTId=PRO_0000011258. FT PEPTIDE 98 128 Glucagon-like peptide 1(7-37). FT /FTId=PRO_0000011259. FT PEPTIDE 98 127 Glucagon-like peptide 1(7-36). FT /FTId=PRO_0000011260. FT PROPEP 131 145 {ECO:0000250}. FT /FTId=PRO_0000011261. FT PEPTIDE 146 178 Glucagon-like peptide 2. {ECO:0000250}. FT /FTId=PRO_0000011262. FT SITE 52 53 Cleavage; by PCSK2. FT SITE 83 84 Cleavage; by PCSK1 and PCSK2. FT SITE 91 92 Cleavage; by PCSK1. FT SITE 97 98 Cleavage; by PCSK1. FT SITE 130 131 Cleavage; by PCSK1. FT SITE 145 146 Cleavage; by PCSK1. FT MOD_RES 54 54 Phosphoserine. FT {ECO:0000250|UniProtKB:P55095}. FT MOD_RES 105 105 Phosphoserine. FT {ECO:0000250|UniProtKB:P55095}. FT MOD_RES 108 108 Phosphoserine. FT {ECO:0000250|UniProtKB:P55095}. FT MOD_RES 127 127 Arginine amide. FT {ECO:0000269|PubMed:2753890}. FT MOD_RES 150 150 Phosphoserine. FT {ECO:0000250|UniProtKB:P55095}. FT MOD_RES 152 152 Phosphoserine. FT {ECO:0000250|UniProtKB:P55095}. FT VARIANT 115 115 A -> V (in dbSNP:rs5650). FT /FTId=VAR_014596. FT CONFLICT 82 82 K -> N (in Ref. 2; CAA27627). FT {ECO:0000305}. FT TURN 55 57 {ECO:0000244|PDB:2M5Q}. FT TURN 59 62 {ECO:0000244|PDB:1BH0}. FT STRAND 63 65 {ECO:0000244|PDB:2M5Q}. FT HELIX 68 70 {ECO:0000244|PDB:2M5P}. FT TURN 71 73 {ECO:0000244|PDB:2M5P}. FT STRAND 76 78 {ECO:0000244|PDB:2G49}. FT HELIX 104 124 {ECO:0000244|PDB:4ZGM}. FT HELIX 150 153 {ECO:0000244|PDB:2L63}. FT HELIX 154 156 {ECO:0000244|PDB:2L63}. FT HELIX 157 172 {ECO:0000244|PDB:2L63}. FT TURN 173 177 {ECO:0000244|PDB:2L63}. SQ SEQUENCE 180 AA; 20909 MW; 7A99EEC629B2862C CRC64; MKSIYFVAGL FVMLVQGSWQ RSLQDTEEKS RSFSASQADP LSDPDQMNED KRHSQGTFTS DYSKYLDSRR AQDFVQWLMN TKRNRNNIAK RHDEFERHAE GTFTSDVSSY LEGQAAKEFI AWLVKGRGRR DFPEEVAIVE ELGRRHADGS FSDEMNTILD NLAARDFINW LIQTKITDRK //