| Identification |
|---|
| HMDB Protein ID
| HMDBP12711 |
| Secondary Accession Numbers
| None |
| Name
| VIP peptides |
| Synonyms
|
Not Available
|
| Gene Name
| VIP |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitonin (By similarity). PHI also causes vasodilation. |
| Pathways
|
- cAMP signaling pathway
- Neuroactive ligand-receptor interaction
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| positive regulation of protein catabolic process |
| learning or memory |
| negative regulation of apoptotic process |
| phospholipase C-activating G-protein coupled receptor signaling pathway |
| regulation of protein localization |
| mRNA stabilization |
| prolactin secretion |
| epinephrine secretion |
| positive regulation of epinephrine secretion |
| positive regulation of penile erection |
| regulation of signal transduction |
| negative regulation of smooth muscle cell proliferation |
| negative regulation of potassium ion transport |
| regulation of sensory perception of pain |
| positive regulation of endothelial cell proliferation |
| adenylate cyclase-activating G-protein coupled receptor signaling pathway |
| Cellular Component |
| perikaryon |
| extracellular region |
| neuronal cell body |
| neuron projection |
| Molecular Function |
| receptor binding |
| hormone activity |
| neuropeptide hormone activity |
| peptide hormone receptor binding |
|
| 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
| 170 |
| Molecular Weight
| 19079.155 |
| Theoretical pI
| 6.045 |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P01283 |
| UniProtKB/Swiss-Prot Entry Name
| VIP_RAT |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Lundby A, Secher A, Lage K, Nordsborg NB, Dmytriyev A, Lundby C, Olsen JV: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun. 2012 Jun 6;3:876. doi: 10.1038/ncomms1871. [PubMed:22673903 ]
- Lamperti ED, Rosen KM, Villa-Komaroff L: Characterization of the gene and messages for vasoactive intestinal polypeptide (VIP) in rat and mouse. Brain Res Mol Brain Res. 1991 Feb;9(3):217-31. doi: 10.1016/0169-328x(91)90005-i. [PubMed:1851524 ]
- Wershil BK, Turck CW, Sreedharan SP, Yang J, An S, Galli SJ, Goetzl EJ: Variants of vasoactive intestinal peptide in mouse mast cells and rat basophilic leukemia cells. Cell Immunol. 1993 Oct 15;151(2):369-78. doi: 10.1006/cimm.1993.1246. [PubMed:8402943 ]
- Giladi E, Shani Y, Gozes I: The complete structure of the rat VIP gene. Brain Res Mol Brain Res. 1990 Apr;7(3):261-7. doi: 10.1016/0169-328x(90)90036-d. [PubMed:2159586 ]
- Nishizawa M, Hayakawa Y, Yanaihara N, Okamoto H: Nucleotide sequence divergence and functional constraint in VIP precursor mRNA evolution between human and rat. FEBS Lett. 1985 Apr 8;183(1):55-9. doi: 10.1016/0014-5793(85)80953-4. [PubMed:3838518 ]
- Goetzl EJ, Sreedharan SP, Turck CW: Structurally distinctive vasoactive intestinal peptides from rat basophilic leukemia cells. J Biol Chem. 1988 Jul 5;263(19):9083-6. [PubMed:3379062 ]
|
