| Primary information |
|---|
| ID | 13212 |
| Uniprot ID | P04203 |
| Description | Exendin-1 (Helospectin I) (Helospectin-1) (VIP-like 1) [Cleaved into- Exendin-1b (Helospectin II) (Helospectin-2)] |
| Organism | Heloderma suspectum |
| Txonomy | Eukaryota; Opisthokonta; Metazoa; Eumetazoa; Bilateria; Deuterostomia; Chordata; Craniata; Vertebrata; Gnathostomata (jawed vertebrates); Teleostomi; Euteleostomi; Sarcopterygii; Dipnotetrapodomorpha; Tetrapoda; Amniota; Sauropsida; Sauria (diapsids); Lepidosauria (lepidosaurs); Squamata (squamates); Bifurcata (split-tongued squamates); Unidentata; Episquamata; Toxicofera; Anguimorpha (anguimorph lizards); Neoanguimorpha (New World anguimorph lizards); Helodermatidae (beaded lizards); Heloderma; |
| Subcellular Location | Secreted |
| Developmental Stage | NA |
| Similarity | Belongs to the glucagon family. |
| Tissue Specificity | Expressed by the venom gland. |
| Post Translational Modification | Thr-32 is glycosylated by N-acetylgalactosamine and a hexose; probably Glu-GalNAc-Thr; a mucin type O-glycosylation which may affect the biological stability of exendin-1 and exendin-1b. |
| Function | O-linked and free exendin-1 and exendin-1b have vasoactive intestinal peptide(VIP)/secretin-like biological activities. They interact with rat and human VIP receptors 1 (VIPR1) and 2 (VIPR2); with the highest affinity for the human VIPR2. They induce hypotension that is mediated by relaxation of cardiac smooth muscle. |
| Length | 38 |
| Molecular Weight | 4 |
| Name | Exendin-1 |
| Sequence | HSDATFTAEYSKLLAKLALQKYLESILGSSTSPRPPS |
| Sequence map | 888 |
| PDB ID | 6207171; 10880980; 9928018; 15003357; 19837656 |
| Drugpedia | NA |
| Receptor | NA |
| Domain | NA |
| Pharmaceutical Use | NA
|