title: Primary structure of helodermin, a VIP-secretin-like peptide isolated from Gila monster venom.
abstract: The complete amino acid sequence of helodermin isolated from the venom of Gila monster was elucidated. The peptide was shown to be a basic pentatriacontapeptide amide: His-Ser-Asp-Ala-Ile-Phe-Thr-Gln-Gln-Tyr-Ser-Lys-Leu-Leu-Ala-Lys-Leu-Ala- Leu-Gln-Lys- Tyr-Leu-Ala-Ser-Ile-Leu-Gly-Ser-Arg-Thr-Ser-Pro-Pro-Pro-NH2. A high degree of sequence similarities to secretin/VIP/PHI/(PHM)/GRF from mammal and bird was observed over the entire N-terminal 1-27 sequence. In particular, the amino acid residues in positions 3, 6 and 7 were found to be common to 9 peptides of the family. Another interesting feature of the structure of helodermin was its C-terminal -Pro-Pro-Pro-NH2 sequence. Isolation of helodermin was the first demonstration of the existence of a secretin/VIP-related peptide in an animal that is neither mammal nor bird.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D002918:Chymotrypsin; D013007:Growth Hormone-Releasing Hormone; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D008116:Lizards; D010446:Peptide Fragments; D010451:Peptide PHI; D010455:Peptides / Q000302:isolation & purification; D012633:Secretin; D014357:Trypsin; D014660:Vasoactive Intestinal Peptide; D014688:Venoms / Q000032:analysis*
chemical_list: D036341:Intercellular Signaling Peptides and Proteins; D010446:Peptide Fragments; D010451:Peptide PHI; D010455:Peptides; D014688:Venoms; D012633:Secretin; D014660:Vasoactive Intestinal Peptide; C040442:heliodermin; D013007:Growth Hormone-Releasing Hormone; D002918:Chymotrypsin; D014357:Trypsin