Biomaterial Database

The amino acid sequence of porcine glicentin. 1981

L Thim, and A J Moody

Glicentin or gut GLI-1 has previously been isolated from porcine small intestine. On the basis of the available chemical data, the molecule was thought to contain 100 amino acid residues. A redetermination of the amino acid composition of the molecule has shown it to contain 69 amino acid residues, and the full sequence has been established. The sequence of glicentin can be outlined as: GRPP1--30-Lys-Arg-Glucagon33--61-Lys-Arg-Hexapeptide64--69 where GRPP1--30 probably corresponds to the glicentin related pancreatic peptide previously isolated from porcine pancreas. In the pancreas, the two dibasic sequences (Lys31-Arg32 and Lys62-Arg63) probably represent sites of post-synthetic enzymatic cleavages by analogy with the two dibasic sequences of proinsulin. Glicentin thus fulfills the structural requirements for being all or a part of porcine proglucagon. In the intestine, glicentin could be the precursor of oxyntomodulin, a small molecular weight gut GLI presumably identical to glicentin 33--69, i.e., glucagon extended at the C-terminal end by an octapeptide.

UI	MeSH Term	Description	Entries
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010450	Endopeptidases	A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.	Endopeptidase,Peptide Peptidohydrolases
D011498	Protein Precursors		Precursors, Protein
D003546	Cysteine Endopeptidases	ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
D004763	Glucagon-Like Peptides	Peptides derived from proglucagon which is also the precursor of pancreatic GLUCAGON. Despite expression of proglucagon in multiple tissues, the major production site of glucagon-like peptides (GLPs) is the INTESTINAL L CELLS. GLPs include glucagon-like peptide 1, glucagon-like peptide 2, and the various truncated forms.	Enteroglucagon,Enteroglucagons,Glucagon-Like Peptide,Glucagon-Like Polypeptide,Gut Glucagon,Glucagon-Like Polypeptides,Glucagon Like Peptide,Glucagon Like Peptides,Glucagon Like Polypeptide,Glucagon Like Polypeptides,Glucagon, Gut,Peptide, Glucagon-Like,Polypeptide, Glucagon-Like
D005934	Glucagon	A 29-amino acid pancreatic peptide derived from proglucagon which is also the precursor of intestinal GLUCAGON-LIKE PEPTIDES. Glucagon is secreted by PANCREATIC ALPHA CELLS and plays an important role in regulation of BLOOD GLUCOSE concentration, ketone metabolism, and several other biochemical and physiological processes. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p1511)	Glucagon (1-29),Glukagon,HG-Factor,Hyperglycemic-Glycogenolytic Factor,Proglucagon (33-61),HG Factor,Hyperglycemic Glycogenolytic Factor
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D052336	Proglucagon	The common precursor polypeptide of pancreatic GLUCAGON and intestinal GLUCAGON-LIKE PEPTIDES. Proglucagon is the 158-amino acid segment of preproglucagon without the N-terminal signal sequence. Proglucagon is expressed in the PANCREAS; INTESTINES; and the CENTRAL NERVOUS SYSTEM. Posttranslational processing of proglucagon is tissue-specific yielding numerous bioactive peptides.	Glucagon Precursor,Glucagon Precursors,Pre-Proglucagons,Preproglucagon,Preproglucagons,Pro-Glucagon,Pro Glucagon
D053771	Glicentin	A 69-amino acid peptide derived from the N-terminal of PROGLUCAGON. It is mainly produced by the INTESTINAL L CELLS. Further processing of glicentin yield a 30-amino acid N-terminal peptide (glicentin-related polypeptide) and a 37-amino acid peptide OXYNTOMODULIN. Both glicentin and oxyntomodulin can reduce digestive secretions and delay gastric emptying.	Glicentine,Proglucagon (1-69)