{PDOC00233}
{PS00260; GLUCAGON}
{BEGIN}
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* Glucagon / GIP / secretin / VIP family signature *
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A number of polypeptidic hormones,  mainly  expressed  in the intestine or the
pancreas, belong to a group of structurally related peptides [1,2]. Members of
this family are:

 - Glucagon, which promotes hydrolysis of glycogen  and lipids, and raises the
   blood sugar level.
 - Glucagon-like peptide 1 (GLP-1), a  peptide of  unknown  function processed
   from the same precursor protein as that of glucagon.
 - Glucagon-like  peptide  2  (GLP-2),   a  peptide of  unknown  function also
   processed from  the  glucagon  precursor  protein but which, in contrast to
   GLP-1, is only found in mammals.
 - Gastric inhibitory  polypeptide (GIP),  which  is a  potent  stimulator  of
   insulin  secretion  and   a   relatively  poor  inhibitor  of  gastric acid
   secretion.
 - Secretin, which stimulates formation of NaHCO(3)-rich pancreatic juice  and
   secretion of NaHCO(3)-rich bile as well as inhibiting HCl production by the
   stomach.
 - Vasoactive  intestinal  peptide (VIP), which  causes vasodilatation, lowers
   arterial blood  pressure,  stimulates  myocardial contractility,  increases
   glycogenolysis and relaxes some smooth muscles.
 - Peptide PHI-27, a vasodilator peptide which is coded by the  same precursor
   protein as that of VIP.
 - Growth  hormone-releasing factor (GRF) (also known as somatoliberin), which
   is released by the hypothalamus and acts on the adenohypophyse to stimulate
   the secretion of growth hormone.
 - Pituitary adenylate cyclase activating polypeptide (PACAP) [3].
 - Helospectin (exendin-1),  helodermin (exendin-2),  exendin-3, and exendin-4
   from the venom of gila monsters.  The  exendins  are  peptides  with a VIP/
   secretin biological activity [4].
 - A peptide produced by the X-cells of the islets of ratfish pancreas [5].

As a pattern for this  family of peptides  (which are from 30 to 45 amino acid
residues long), we used the  more or less conserved first ten positions of the
N-terminal as well as a conserved hydrophobic residue in position 23.

-Consensus pattern: [YH]-[STAIVGD]-[DEQ]-[AGF]-[LIVMSTE]-[FYLR]-x-[DENSTAK]-
                    [DENSTA]-[LIVMFYG]-x(8)-{K}-[KREQL]-[KRDENQL]-[LVFYWG]-
                    [LIVQ]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 1.
-Last update: December 2004 / Pattern and text revised.

[ 1] Mutt V.
     "Vasoactive intestinal polypeptide and related peptides. Isolation and
     chemistry."
     Ann. N.Y. Acad. Sci. 527:1-19(1988).
     PubMed=3133967
[ 2] Bataille D., Blache P., Mercier F., Jarrousse C., Kervran A., Dufour M.,
     Mangeat P., Dubrasquet M., Mallat A., Lotersztajn S., Pavoine C.,
     Pecker F.
     Ann. N.Y. Acad. Sci. 527:169-185(1988).
[ 3] Miyata A., Arimura A., Dahl R.R., Minamino N., Uehara A., Jiang L.,
     Culler M.D., Coy D.H.
     "Isolation of a novel 38 residue-hypothalamic polypeptide which
     stimulates adenylate cyclase in pituitary cells."
     Biochem. Biophys. Res. Commun. 164:567-574(1989).
     PubMed=2803320
[ 4] Eng J., Kleinman W.A., Singh L., Singh G., Raufman J.-P.
     "Isolation and characterization of exendin-4, an exendin-3 analogue,
     from Heloderma suspectum venom. Further evidence for an exendin
     receptor on dispersed acini from guinea pig pancreas."
     J. Biol. Chem. 267:7402-7405(1992).
     PubMed=1313797
[ 5] Conlon J.M., Dafgard E., Falkmer S., Thim L.
     "A glucagon-like peptide, structurally related to mammalian
     oxyntomodulin, from the pancreas of a holocephalan fish, Hydrolagus
     colliei."
     Biochem. J. 245:851-855(1987).
     PubMed=3311036

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