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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)] (Fragment)

 GLUC_SHEEP              Reviewed;         176 AA.
Q8MJ25;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-OCT-2017, entry version 58.
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; Fragment;
Name=GCG;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
Limesand S.W., Hay W.W. Jr.;
"Characterization of the endocrine pancreas in an ovine placental
insufficiency IUGR fetus.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
-!- 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 (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.
-!- 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}.
-!- MISCELLANEOUS: GLP-2 does not have cleavage on a pair of basic
residues at C-terminus as in other mammals.
-!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF529185; AAM94409.1; -; mRNA.
UniGene; Oar.981; -.
ProteinModelPortal; Q8MJ25; -.
SMR; Q8MJ25; -.
HOVERGEN; HBG003010; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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.
2: Evidence at transcript level;
Amidation; Cleavage on pair of basic residues; Complete proteome;
Hormone; Phosphoprotein; Reference proteome; Secreted; Signal.
SIGNAL 1 20
PEPTIDE 21 89 Glicentin. {ECO:0000250}.
/FTId=PRO_0000011313.
PEPTIDE 21 50 Glicentin-related polypeptide.
{ECO:0000250}.
/FTId=PRO_0000011314.
PEPTIDE 53 89 Oxyntomodulin. {ECO:0000250}.
/FTId=PRO_0000011315.
PEPTIDE 53 81 Glucagon.
/FTId=PRO_0000011316.
PROPEP 84 89 {ECO:0000250}.
/FTId=PRO_0000011317.
PEPTIDE 92 128 Glucagon-like peptide 1. {ECO:0000250}.
/FTId=PRO_0000011318.
PEPTIDE 98 128 Glucagon-like peptide 1(7-37).
{ECO:0000250}.
/FTId=PRO_0000011319.
PEPTIDE 98 127 Glucagon-like peptide 1(7-36).
{ECO:0000250}.
/FTId=PRO_0000011320.
PROPEP 131 145 {ECO:0000250}.
/FTId=PRO_0000011321.
PEPTIDE 146 >176 Glucagon-like peptide 2. {ECO:0000250}.
/FTId=PRO_0000011322.
SITE 52 53 Cleavage; by PCSK2. {ECO:0000250}.
SITE 83 84 Cleavage; by PCSK1 and PCSK2.
{ECO:0000250}.
SITE 91 92 Cleavage; by PCSK1. {ECO:0000250}.
SITE 97 98 Cleavage; by PCSK1. {ECO:0000250}.
SITE 130 131 Cleavage; by PCSK1. {ECO:0000250}.
SITE 145 146 Cleavage; by PCSK1. {ECO:0000250}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000250|UniProtKB:P55095}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000250|UniProtKB:P55095}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000250|UniProtKB:P55095}.
MOD_RES 127 127 Arginine amide. {ECO:0000250}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000250|UniProtKB:P55095}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000250|UniProtKB:P55095}.
NON_TER 176 176
SEQUENCE 176 AA; 20336 MW; 13174039BD6CE2B3 CRC64;
MKSLYFVAGL LVMLAQGSWQ HSLQNTEEKS SSFPAPQTDP LGDPDQISED KRHSQGTFTS
DYSKYLDSRR AQDFVQWLMN TKRNKNNIAK RHDEFERHAE GTFTSDVSSY LEGQAAKEFI
AWLVKGRGRR DFPEEVNIVE ELRRRHADGS FSDEMNTVLD SLATRDFINW LLQTKI


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