Hmdb loader
Identification
HMDB Protein ID HMDBP14613
Secondary Accession Numbers None
Name Exendin-2-long
Synonyms Not Available
Gene Name Not Available
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Has vasoactive intestinal peptide(VIP)/secretin-like biological activity. Interacts with rat and human VIP receptors 1 (VIPR1) and 2 (VIPR2), with the highest affinity for the human VIPR2. Induces hypotension that is mediated by relaxation of cardiac smooth muscle. This vasodilation may not be transduced by VIP or PACAP receptors.
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
regulation of blood pressure
Cellular Component
extracellular region
Molecular Function
toxin activity
hormone activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues Not Available
Molecular Weight 9530.965
Theoretical pI Not Available
Pfam Domain Function
Signals
  • 1-23;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P04204
UniProtKB/Swiss-Prot Entry Name EXE2_HELSU
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Fry BG, Roelants K, Winter K, Hodgson WC, Griesman L, Kwok HF, Scanlon D, Karas J, Shaw C, Wong L, Norman JA: Novel venom proteins produced by differential domain-expression strategies in beaded lizards and gila monsters (genus Heloderma). Mol Biol Evol. 2010 Feb;27(2):395-407. doi: 10.1093/molbev/msp251. Epub 2009 Oct 15. [PubMed:19837656 ]
  2. Pohl M, Wank SA: Molecular cloning of the helodermin and exendin-4 cDNAs in the lizard. Relationship to vasoactive intestinal polypeptide/pituitary adenylate cyclase activating polypeptide and glucagon-like peptide 1 and evidence against the existence of mammalian homologues. J Biol Chem. 1998 Apr 17;273(16):9778-84. doi: 10.1074/jbc.273.16.9778. [PubMed:9545315 ]
  3. Vandermeers-Piret MC, Vandermeers A, Gourlet P, Ali MH, Waelbroeck M, Robberecht P: Evidence that the lizard helospectin peptides are O-glycosylated. Eur J Biochem. 2000 Jul;267(14):4556-60. doi: 10.1046/j.1432-1327.2000.01506.x. [PubMed:10880980 ]
  4. Gourlet P, Vandermeers A, Van Rampelbergh J, De Neef P, Cnudde J, Waelbroeck M, Robberecht P: Analogues of VIP, helodermin, and PACAP discriminate between rat and human VIP1 and VIP2 receptors. Ann N Y Acad Sci. 1998 Dec 11;865:247-52. doi: 10.1111/j.1749-6632.1998.tb11184.x. [PubMed:9928018 ]
  5. Tsueshita T, Onyukusel H, Sethi V, Gandhi S, Rubinstein I: Helospectin I and II evoke vasodilation in the intact peripheral microcirculation. Peptides. 2004 Jan;25(1):65-9. doi: 10.1016/j.peptides.2003.11.010. [PubMed:15003357 ]
  6. Hoshino M, Yanaihara C, Hong YM, Kishida S, Katsumaru Y, Vandermeers A, Vandermeers-Piret MC, Robberecht P, Christophe J, Yanaihara N: Primary structure of helodermin, a VIP-secretin-like peptide isolated from Gila monster venom. FEBS Lett. 1984 Dec 10;178(2):233-9. doi: 10.1016/0014-5793(84)80607-9. [PubMed:6439576 ]
  7. Vandermeers A, Gourlet P, Vandermeers-Piret MC, Cauvin A, De Neef P, Rathe J, Svoboda M, Robberecht P, Christophe J: Chemical, immunological and biological properties of peptides like vasoactive-intestinal-peptide and peptide-histidine-isoleucinamide extracted from the venom of two lizards (Heloderma horridum and Heloderma suspectum). Eur J Biochem. 1987 Apr 15;164(2):321-7. doi: 10.1111/j.1432-1033.1987.tb11061.x. [PubMed:3569266 ]
  8. Blankenfeldt W, Nokihara K, Naruse S, Lessel U, Schomburg D, Wray V: NMR spectroscopic evidence that helodermin, unlike other members of the secretin/VIP family of peptides, is substantially structured in water. Biochemistry. 1996 May 14;35(19):5955-62. doi: 10.1021/bi9601520. [PubMed:8634236 ]