ID   GLUC_MOUSE              Reviewed;         180 AA.
AC   P55095; Q3UFE9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Pro-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   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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreatic islet;
RX   PubMed=7730317; DOI=10.1074/jbc.270.17.10136;
RA   Rothenberg M.E., Eilertson C.D., Klein K., Zhou Y., Linberg I.,
RA   McDonald J.K., Mackin R.B., Noe B.D.;
RT   "Processing of mouse proglucagon by recombinant prohormone convertase 1 and
RT   immunopurified prohormone convertase 2 in vitro.";
RL   J. Biol. Chem. 270:10136-10146(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Shamsadin R., Knepel W.;
RT   "Mouse glucagon full length cDNA.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION OF GLP-1 AND GLP-1(7-36) AMIDE.
RX   PubMed=1886889;
RA   Fridolf T., Bottcher G., Sundler F., Ahren B.;
RT   "GLP-1 and GLP-1(7-36) amide: influences on basal and stimulated insulin
RT   and glucagon secretion in the mouse.";
RL   Pancreas 6:208-215(1991).
RN   [6]
RP   PROTEOLYTIC PROCESSING BY PCSK1.
RX   PubMed=9407057; DOI=10.1074/jbc.272.52.32810;
RA   Rouille Y., Kantengwa S., Irminger J.C., Halban P.A.;
RT   "Role of the prohormone convertase PC3 in the processing of proglucagon to
RT   glucagon-like peptide 1.";
RL   J. Biol. Chem. 272:32810-32816(1997).
RN   [7]
RP   PROTEOLYTIC PROCESSING BY PCSK2.
RX   PubMed=11356850; DOI=10.1074/jbc.m103362200;
RA   Furuta M., Zhou A., Webb G., Carroll R., Ravazzola M., Orci L.,
RA   Steiner D.F.;
RT   "Severe defect in proglucagon processing in islet A-cells of prohormone
RT   convertase 2 null mice.";
RL   J. Biol. Chem. 276:27197-27202(2001).
RN   [8]
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   [9]
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   [10]
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   [11]
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   [12]
RP   REVIEW.
RX   PubMed=12554744; DOI=10.1210/me.2002-0306;
RA   Drucker D.J.;
RT   "Glucagon-like peptides: regulators of cell proliferation, differentiation,
RT   and apoptosis.";
RL   Mol. Endocrinol. 17:161-171(2003).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-105; SER-108; SER-150
RP   AND SER-152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [14]
RP   INDUCTION BY EXERCISE (GLUCAGON-LIKE PEPTIDE 1), FUNCTION (GLUCAGON-LIKE
RP   PEPTIDE 1), AND TISSUE SPECIFICITY (GLUCAGON-LIKE PEPTIDE 1).
RX   PubMed=22037645; DOI=10.1038/nm.2513;
RA   Ellingsgaard H., Hauselmann I., Schuler B., Habib A.M., Baggio L.L.,
RA   Meier D.T., Eppler E., Bouzakri K., Wueest S., Muller Y.D., Hansen A.M.,
RA   Reinecke M., Konrad D., Gassmann M., Reimann F., Halban P.A., Gromada J.,
RA   Drucker D.J., Gribble F.M., Ehses J.A., Donath M.Y.;
RT   "Interleukin-6 enhances insulin secretion by increasing glucagon-like
RT   peptide-1 secretion from L cells and alpha cells.";
RL   Nat. Med. 17:1481-1489(2011).
CC   -!- FUNCTION: [Glucagon]: Plays a key role in glucose metabolism and
CC       homeostasis. Regulates blood glucose by increasing gluconeogenesis and
CC       decreasing glycolysis. A counterregulatory hormone of insulin, raises
CC       plasma glucose levels in response to insulin-induced hypoglycemia.
CC       Plays an important role in initiating and maintaining hyperglycemic
CC       conditions in diabetes. {ECO:0000305|PubMed:10605628,
CC       ECO:0000305|PubMed:12626323}.
CC   -!- FUNCTION: [Glucagon-like peptide 1]: Potent stimulator of glucose-
CC       dependent insulin release. Also stimulates insulin release in response
CC       to IL6 (PubMed:22037645). Plays important roles on gastric motility and
CC       the 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. Has growth-
CC       promoting activities on intestinal epithelium. May also regulate the
CC       hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH,
CC       oxytocin, and vasopressin secretion. Increases islet mass through
CC       stimulation of islet neogenesis and pancreatic beta cell proliferation.
CC       Inhibits beta cell apoptosis (Probable). {ECO:0000269|PubMed:22037645,
CC       ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744,
CC       ECO:0000305|PubMed:14719035}.
CC   -!- FUNCTION: [Glucagon-like peptide 2]: Stimulates intestinal growth and
CC       up-regulates villus height in the small intestine, concomitant with
CC       increased crypt cell proliferation and decreased enterocyte apoptosis.
CC       The 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 disposal.
CC       Stimulates intestinal glucose transport and decreases mucosal
CC       permeability. {ECO:0000305|PubMed:10322410,
CC       ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744,
CC       ECO:0000305|PubMed:14719035}.
CC   -!- FUNCTION: [Oxyntomodulin]: Significantly reduces food intake. Inhibits
CC       gastric emptying in humans. Suppression of gastric emptying may lead to
CC       increased gastric distension, which may contribute to satiety by
CC       causing a sensation of fullness. {ECO:0000305|PubMed:10605628,
CC       ECO:0000305|PubMed:12554744}.
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       {ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12554744}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22037645}.
CC   -!- SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted
CC       {ECO:0000269|PubMed:22037645}.
CC   -!- TISSUE SPECIFICITY: [Glucagon]: Secreted in the A cells of the islets
CC       of Langerhans. {ECO:0000269|PubMed:22037645}.
CC   -!- TISSUE SPECIFICITY: [Glucagon-like peptide 1]: Secreted in the A cells
CC       of the islets of Langerhans (PubMed:22037645). Secreted from
CC       enteroendocrine L cells throughout the gastrointestinal tract
CC       (PubMed:22037645). Also secreted in selected neurons in the brain.
CC       {ECO:0000269|PubMed:22037645}.
CC   -!- TISSUE SPECIFICITY: [Glucagon-like peptide 2]: Secreted from
CC       enteroendocrine cells throughout the gastrointestinal tract. Also
CC       secreted in selected neurons in the brain.
CC   -!- TISSUE SPECIFICITY: [Glicentin]: Secreted from enteroendocrine cells
CC       throughout the gastrointestinal tract.
CC   -!- TISSUE SPECIFICITY: [Oxyntomodulin]: Secreted from enteroendocrine
CC       cells throughout the gastrointestinal tract.
CC   -!- INDUCTION: [Glucagon]: Release is stimulated by hypoglycemia and
CC       inhibited by hyperglycemia, insulin, and somatostatin.
CC       {ECO:0000305|PubMed:10605628, ECO:0000305|PubMed:12626323}.
CC   -!- INDUCTION: [Glucagon-like peptide 1]: Production by pancreatic and
CC       inestinal L cells is increased by exercise in an IL6-dependent manner
CC       (PubMed:22037645). High-fat diet increases pancreatic content
CC       (PubMed:22037645). {ECO:0000269|PubMed:22037645}.
CC   -!- INDUCTION: [Glucagon-like peptide 2]: Induced in response to nutrient
CC       ingestion. {ECO:0000305|PubMed:10322410, ECO:0000305|PubMed:10605628,
CC       ECO:0000305|PubMed:12554744, ECO:0000305|PubMed:14719035}.
CC   -!- PTM: Proglucagon is post-translationally processed in a tissue-specific
CC       manner in pancreatic A cells and intestinal L cells. In pancreatic A
CC       cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In
CC       the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and
CC       oxyntomodulin. GLP-1 is further N-terminally truncated by post-
CC       translational processing in the intestinal L cells resulting in GLP-
CC       1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither
CC       important for the metabolism of GLP-1 nor for its effects on the
CC       endocrine pancreas (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR   EMBL; Z46845; CAA86902.1; -; mRNA.
DR   EMBL; AF276754; AAK96898.1; -; mRNA.
DR   EMBL; AK007911; BAB25344.1; -; mRNA.
DR   EMBL; AK148544; BAE28612.1; -; mRNA.
DR   EMBL; BC012975; AAH12975.1; -; mRNA.
DR   CCDS; CCDS16066.1; -.
DR   PIR; A57294; A57294.
DR   RefSeq; NP_032126.1; NM_008100.4.
DR   AlphaFoldDB; P55095; -.
DR   SMR; P55095; -.
DR   STRING; 10090.ENSMUSP00000099794; -.
DR   iPTMnet; P55095; -.
DR   PhosphoSitePlus; P55095; -.
DR   MaxQB; P55095; -.
DR   PaxDb; 10090-ENSMUSP00000099794; -.
DR   ProteomicsDB; 271001; -.
DR   ABCD; P55095; 1 sequenced antibody.
DR   Antibodypedia; 3506; 2088 antibodies from 46 providers.
DR   DNASU; 14526; -.
DR   Ensembl; ENSMUST00000102733.10; ENSMUSP00000099794.4; ENSMUSG00000000394.16.
DR   GeneID; 14526; -.
DR   KEGG; mmu:14526; -.
DR   UCSC; uc008jvj.1; mouse.
DR   AGR; MGI:95674; -.
DR   CTD; 2641; -.
DR   MGI; MGI:95674; Gcg.
DR   VEuPathDB; HostDB:ENSMUSG00000000394; -.
DR   eggNOG; ENOG502RYPR; Eukaryota.
DR   GeneTree; ENSGT00390000005372; -.
DR   InParanoid; P55095; -.
DR   OMA; MNTKRNX; -.
DR   OrthoDB; 5318261at2759; -.
DR   PhylomeDB; P55095; -.
DR   TreeFam; TF332333; -.
DR   Reactome; R-MMU-163359; Glucagon signaling in metabolic regulation.
DR   Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR   Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR   BioGRID-ORCS; 14526; 0 hits in 62 CRISPR screens.
DR   ChiTaRS; Gcg; mouse.
DR   PRO; PR:P55095; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P55095; Protein.
DR   Bgee; ENSMUSG00000000394; Expressed in dorsal pancreas and 41 other cell types or tissues.
DR   ExpressionAtlas; P55095; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0031767; F:gastric inhibitory polypeptide receptor binding; ISO:MGI.
DR   GO; GO:0031769; F:glucagon receptor binding; ISO:MGI.
DR   GO; GO:0005179; F:hormone activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0048018; F:receptor ligand activity; IDA:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0071377; P:cellular response to glucagon stimulus; IDA:MGI.
DR   GO; GO:0006094; P:gluconeogenesis; IDA:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0032099; P:negative regulation of appetite; ISO:MGI.
DR   GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IDA:MGI.
DR   GO; GO:0090280; P:positive regulation of calcium ion import; IDA:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; IDA:MGI.
DR   GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IGI:MGI.
DR   GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0032092; P:positive regulation of protein binding; IDA:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0010737; P:protein kinase A signaling; IMP:UniProtKB.
DR   GO; GO:0050796; P:regulation of insulin secretion; IDA:UniProtKB.
DR   GO; GO:0014823; P:response to activity; IDA:UniProtKB.
DR   Gene3D; 6.10.250.590; -; 3.
DR   InterPro; IPR015550; Glucagon.
DR   InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
DR   PANTHER; PTHR11418; GLUCAGON; 1.
DR   PANTHER; PTHR11418:SF0; PRO-GLUCAGON; 1.
DR   Pfam; PF00123; Hormone_2; 3.
DR   PRINTS; PR00275; GLUCAGON.
DR   SMART; SM00070; GLUCA; 3.
DR   PROSITE; PS00260; GLUCAGON; 4.
DR   Genevisible; P55095; MM.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Hormone; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250|UniProtKB:P01274"
FT   PEPTIDE         21..89
FT                   /note="Glicentin"
FT                   /evidence="ECO:0000250|UniProtKB:P01274"
FT                   /id="PRO_0000011273"
FT   PEPTIDE         21..50
FT                   /note="Glicentin-related polypeptide"
FT                   /evidence="ECO:0000250|UniProtKB:P09686"
FT                   /id="PRO_0000011274"
FT   PEPTIDE         53..89
FT                   /note="Oxyntomodulin"
FT                   /evidence="ECO:0000250|UniProtKB:P06883"
FT                   /id="PRO_0000011275"
FT   PEPTIDE         53..81
FT                   /note="Glucagon"
FT                   /evidence="ECO:0000250|UniProtKB:P01275"
FT                   /id="PRO_0000011276"
FT   PROPEP          84..89
FT                   /evidence="ECO:0000250|UniProtKB:P01275"
FT                   /id="PRO_0000011277"
FT   PEPTIDE         92..128
FT                   /note="Glucagon-like peptide 1"
FT                   /evidence="ECO:0000250|UniProtKB:P01275"
FT                   /id="PRO_0000011278"
FT   PEPTIDE         98..128
FT                   /note="Glucagon-like peptide 1(7-37)"
FT                   /evidence="ECO:0000250|UniProtKB:P01275"
FT                   /id="PRO_0000011279"
FT   PEPTIDE         98..127
FT                   /note="Glucagon-like peptide 1(7-36)"
FT                   /evidence="ECO:0000250|UniProtKB:P01275"
FT                   /id="PRO_0000011280"
FT   PROPEP          131..145
FT                   /evidence="ECO:0000250|UniProtKB:P15438"
FT                   /id="PRO_0000011281"
FT   PEPTIDE         146..178
FT                   /note="Glucagon-like peptide 2"
FT                   /evidence="ECO:0000250|UniProtKB:P15438"
FT                   /id="PRO_0000011282"
FT   REGION          25..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            52..53
FT                   /note="Cleavage; by PCSK2"
FT   SITE            83..84
FT                   /note="Cleavage; by PCSK1 and PCSK2"
FT   SITE            91..92
FT                   /note="Cleavage; by PCSK1"
FT   SITE            97..98
FT                   /note="Cleavage; by PCSK1"
FT   SITE            130..131
FT                   /note="Cleavage; by PCSK1"
FT   SITE            145..146
FT                   /note="Cleavage; by PCSK1"
FT   MOD_RES         54
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         108
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         127
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         150
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   180 AA;  20906 MW;  595AA6DD9A589950 CRC64;
     MKTIYFVAGL LIMLVQGSWQ HALQDTEENP RSFPASQTEA HEDPDEMNED KRHSQGTFTS
     DYSKYLDSRR AQDFVQWLMN TKRNRNNIAK RHDEFERHAE GTFTSDVSSY LEGQAAKEFI
     AWLVKGRGRR DFPEEVAIAE ELGRRHADGS FSDEMSTILD NLATRDFINW LIQTKITDKK
//