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Glucagon [Cleaved into: Glicentin; Glicentin-related polypeptide (GRPP); Oxyntomodulin (OXM) (OXY); Glucagon; Glucagon-like peptide 1 (GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-like peptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)]

 GLUC_MOUSE              Reviewed;         180 AA.
P55095; Q3UFE9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
12-SEP-2018, entry version 146.
RecName: Full=Glucagon;
Contains:
RecName: Full=Glicentin;
Contains:
RecName: Full=Glicentin-related polypeptide;
Short=GRPP;
Contains:
RecName: Full=Oxyntomodulin;
Short=OXM;
Short=OXY;
Contains:
RecName: Full=Glucagon;
Contains:
RecName: Full=Glucagon-like peptide 1;
Short=GLP-1;
Contains:
RecName: Full=Glucagon-like peptide 1(7-37);
Short=GLP-1(7-37);
Contains:
RecName: Full=Glucagon-like peptide 1(7-36);
Short=GLP-1(7-36);
Contains:
RecName: Full=Glucagon-like peptide 2;
Short=GLP-2;
Flags: Precursor;
Name=Gcg;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreatic islet;
PubMed=7730317; DOI=10.1074/jbc.270.17.10136;
Rothenberg M.E., Eilertson C.D., Klein K., Zhou Y., Linberg I.,
McDonald J.K., Mackin R.B., Noe B.D.;
"Processing of mouse proglucagon by recombinant prohormone convertase
1 and immunopurified prohormone convertase 2 in vitro.";
J. Biol. Chem. 270:10136-10146(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Shamsadin R., Knepel W.;
"Mouse glucagon full length cDNA.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION OF GLP-1 AND GLP-1(7-36) AMIDE.
PubMed=1886889;
Fridolf T., Bottcher G., Sundler F., Ahren B.;
"GLP-1 and GLP-1(7-36) amide: influences on basal and stimulated
insulin and glucagon secretion in the mouse.";
Pancreas 6:208-215(1991).
[6]
PROTEOLYTIC PROCESSING BY PCSK1.
PubMed=9407057; DOI=10.1074/jbc.272.52.32810;
Rouille Y., Kantengwa S., Irminger J.C., Halban P.A.;
"Role of the prohormone convertase PC3 in the processing of
proglucagon to glucagon-like peptide 1.";
J. Biol. Chem. 272:32810-32816(1997).
[7]
PROTEOLYTIC PROCESSING BY PCSK2.
PubMed=11356850; DOI=10.1074/jbc.M103362200;
Furuta M., Zhou A., Webb G., Carroll R., Ravazzola M., Orci L.,
Steiner D.F.;
"Severe defect in proglucagon processing in islet A-cells of
prohormone convertase 2 null mice.";
J. Biol. Chem. 276:27197-27202(2001).
[8]
REVIEW.
PubMed=12554744; DOI=10.1210/me.2002-0306;
Drucker D.J.;
"Glucagon-like peptides: regulators of cell proliferation,
differentiation, and apoptosis.";
Mol. Endocrinol. 17:161-171(2003).
[9]
REVIEW.
PubMed=12626323; DOI=10.1152/ajpendo.00492.2002;
Jiang G., Zhang B.B.;
"Glucagon and regulation of glucose metabolism.";
Am. J. Physiol. 284:E671-E678(2003).
[10]
REVIEW.
PubMed=10322410; DOI=10.1016/S1043-2760(98)00136-2;
Drucker D.J.;
"Glucagon-like peptide 2.";
Trends Endocrinol. Metab. 10:153-156(1999).
[11]
REVIEW.
PubMed=10605628; DOI=10.1210/edrv.20.6.0385;
Kieffer T.J., Habener J.F.;
"The glucagon-like peptides.";
Endocr. Rev. 20:876-913(1999).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-105; SER-108;
SER-150 AND SER-152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Glucagon plays a key role in glucose metabolism and
homeostasis. Regulates blood glucose by increasing gluconeogenesis
and decreasing glycolysis. A counterregulatory hormone of insulin,
raises plasma glucose levels in response to insulin-induced
hypoglycemia (By similarity). {ECO:0000250}.
-!- FUNCTION: GLP-1 is a potent stimulator of glucose-dependent
insulin release. Play important roles on gastric motility and the
suppression of plasma glucagon levels. May be involved in the
suppression of satiety and stimulation of glucose disposal in
peripheral tissues, independent of the actions of insulin. Have
growth-promoting activities on intestinal epithelium. May also
regulate the hypothalamic pituitary axis (HPA) via effects on LH,
TSH, CRH, oxytocin, and vasopressin secretion. Increases islet
mass through stimulation of islet neogenesis and pancreatic beta
cell proliferation (By similarity). {ECO:0000250}.
-!- FUNCTION: GLP-2 stimulates intestinal growth and up-regulates
villus height in the small intestine, concomitant with increased
crypt cell proliferation and decreased enterocyte apoptosis. The
gastrointestinal tract, from the stomach to the colon is the
principal target for GLP-2 action. Plays a key role in nutrient
homeostasis, enhancing nutrient assimilation through enhanced
gastrointestinal function, as well as increasing nutrient
disposal. Stimulates intestinal glucose transport and decreases
mucosal permeability (By similarity). {ECO:0000250}.
-!- FUNCTION: Oxyntomodulin significantly reduces food intake.
{ECO:0000250}.
-!- FUNCTION: Glicentin may modulate gastric acid secretion and
gastro-pyloro-duodenal activity. {ECO:0000269|PubMed:1886889}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Glucagon is secreted in the A cells of the
islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin
are secreted from enteroendocrine cells throughout the
gastrointestinal tract. GLP-1 and GLP-2 are also secreted in
selected neurons in the brain.
-!- INDUCTION: Glucagon release is stimulated by hypoglycemia and
inhibited by hyperglycemia, insulin, and somatostatin. GLP-1 and
GLP-2 are induced in response to nutrient ingestion (By
similarity). {ECO:0000250}.
-!- PTM: Proglucagon is post-translationally processed in a tissue-
specific manner in pancreatic A cells and intestinal L cells. In
pancreatic A cells, the major bioactive hormone is glucagon
cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1
liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is
further N-terminally truncated by post-translational processing in
the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide.
The C-terminal amidation is neither important for the metabolism
of GLP-1 nor for its effects on the endocrine pancreas (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; Z46845; CAA86902.1; -; mRNA.
EMBL; AF276754; AAK96898.1; -; mRNA.
EMBL; AK007911; BAB25344.1; -; mRNA.
EMBL; AK148544; BAE28612.1; -; mRNA.
EMBL; BC012975; AAH12975.1; -; mRNA.
CCDS; CCDS16066.1; -.
PIR; A57294; A57294.
RefSeq; NP_032126.1; NM_008100.4.
UniGene; Mm.45494; -.
ProteinModelPortal; P55095; -.
SMR; P55095; -.
STRING; 10090.ENSMUSP00000099794; -.
iPTMnet; P55095; -.
PhosphoSitePlus; P55095; -.
MaxQB; P55095; -.
PaxDb; P55095; -.
PRIDE; P55095; -.
Ensembl; ENSMUST00000102733; ENSMUSP00000099794; ENSMUSG00000000394.
GeneID; 14526; -.
KEGG; mmu:14526; -.
UCSC; uc008jvj.1; mouse.
CTD; 2641; -.
MGI; MGI:95674; Gcg.
eggNOG; ENOG410IKZ8; Eukaryota.
eggNOG; ENOG4111VKC; LUCA.
GeneTree; ENSGT00390000005372; -.
HOGENOM; HOG000231876; -.
HOVERGEN; HBG003010; -.
InParanoid; P55095; -.
KO; K05259; -.
OMA; TRDFINW; -.
OrthoDB; EOG091G0PJK; -.
PhylomeDB; P55095; -.
TreeFam; TF332333; -.
Reactome; R-MMU-163359; Glucagon signaling in metabolic regulation.
Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-MMU-416476; G alpha (q) signalling events.
Reactome; R-MMU-418555; G alpha (s) signalling events.
Reactome; R-MMU-420092; Glucagon-type ligand receptors.
Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
ChiTaRS; Gcg; mouse.
PMAP-CutDB; P55095; -.
PRO; PR:P55095; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000000394; Expressed in 51 organ(s), highest expression level in islet of Langerhans.
CleanEx; MM_GCG; -.
ExpressionAtlas; P55095; baseline and differential.
Genevisible; P55095; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0031769; F:glucagon receptor binding; ISO:MGI.
GO; GO:0005179; F:hormone activity; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0032099; P:negative regulation of appetite; ISO:MGI.
GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IDA:MGI.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0090280; P:positive regulation of calcium ion import; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0035948; P:positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IGI:MGI.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; IDA:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0010737; P:protein kinase A signaling; IMP:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; IDA:MGI.
GO; GO:0042594; P:response to starvation; IBA:GO_Central.
InterPro; IPR015550; Glucagon.
InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
PANTHER; PTHR11418; PTHR11418; 1.
Pfam; PF00123; Hormone_2; 3.
PRINTS; PR00275; GLUCAGON.
SMART; SM00070; GLUCA; 3.
PROSITE; PS00260; GLUCAGON; 4.
1: Evidence at protein level;
Amidation; Cleavage on pair of basic residues; Complete proteome;
Hormone; Phosphoprotein; Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000250}.
PEPTIDE 21 89 Glicentin. {ECO:0000250}.
/FTId=PRO_0000011273.
PEPTIDE 21 50 Glicentin-related polypeptide.
{ECO:0000250}.
/FTId=PRO_0000011274.
PEPTIDE 53 89 Oxyntomodulin. {ECO:0000250}.
/FTId=PRO_0000011275.
PEPTIDE 53 81 Glucagon. {ECO:0000250}.
/FTId=PRO_0000011276.
PROPEP 84 89 {ECO:0000250}.
/FTId=PRO_0000011277.
PEPTIDE 92 128 Glucagon-like peptide 1. {ECO:0000250}.
/FTId=PRO_0000011278.
PEPTIDE 98 128 Glucagon-like peptide 1(7-37).
{ECO:0000250}.
/FTId=PRO_0000011279.
PEPTIDE 98 127 Glucagon-like peptide 1(7-36).
{ECO:0000250}.
/FTId=PRO_0000011280.
PROPEP 131 145 {ECO:0000250}.
/FTId=PRO_0000011281.
PEPTIDE 146 178 Glucagon-like peptide 2. {ECO:0000250}.
/FTId=PRO_0000011282.
SITE 52 53 Cleavage; by PCSK2.
SITE 83 84 Cleavage; by PCSK1 and PCSK2.
SITE 91 92 Cleavage; by PCSK1.
SITE 97 98 Cleavage; by PCSK1.
SITE 130 131 Cleavage; by PCSK1.
SITE 145 146 Cleavage; by PCSK1.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 127 127 Arginine amide. {ECO:0000250}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
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


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