VIPR1
VIPR1 (vasoactive intestinal peptide receptor 1, also known as VPAC1, RDC1, HVR1 and VPAC1R) is a cell-membrane G protein-coupled receptor for the neuropeptides VIP and PACAP. Ligand binding activates the cAMP-dependent signalling pathway. Browse Assay Genie's current range of VIPR1 research reagents below, or read on for the biology behind the target.
VIPR1 is a G protein-coupled receptor activated by two neuropeptides: vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating polypeptide (ADCYAP1, also called PACAP). It binds VIP and both bioactive forms of PACAP, PACAP27 and PACAP38, with an order of affinity of VIP = PACAP27 > PACAP38. Ligand binding causes a conformational change in the receptor. This triggers signalling through guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, including activation of the cAMP-dependent pathway.
The VIPR1 gene encodes a receptor for VIP, a small neuropeptide. According to the NCBI Gene summary, VIP is involved in smooth muscle relaxation, exocrine and endocrine secretion, and water and ion flux in lung and intestinal epithelia. Its actions are mediated by integral membrane receptors coupled to a guanine nucleotide binding protein, which activates adenylate cyclase. The receptor is found at the cell membrane. It belongs to the G protein-coupled receptor 2 family, and HGNC places it in the vasoactive intestinal peptide family receptors gene group. Several transcript variants encoding different isoforms have been reported for the VIPR1 gene.
The receptor is also known as VPAC1, and the aliases RDC1, HVR1 and VPAC1R appear in the literature. Orthologous genes, both named Vipr1, are present in mouse and rat, which supports comparative work in rodent models. VIPR2 is the related VIP receptor, and researchers studying VIP and PACAP signalling often consider the two receptors together when working on the VIPR1 protein.
VIPR1 mediates responses to VIP and PACAP, making it a central receptor for studying neuropeptide signalling through G proteins.
Ligand binding to VIPR1 activates the cAMP-dependent pathway, and the receptor is used to study adenylate cyclase-coupled GPCR signalling.
VIP is involved in smooth muscle relaxation and in exocrine and endocrine secretion, processes that are effected through its receptors.
VIP influences water and ion flux in lung and intestinal epithelia, which makes VIPR1 relevant to epithelial physiology.
VIPR1 is a G protein-coupled receptor on the cell membrane. It binds VIP and PACAP, then signals through G proteins to activate the cAMP-dependent pathway. The VIP signalling it mediates is linked to smooth muscle relaxation, secretion, and water and ion flux in lung and intestinal epithelia.
VIPR1 is also called VPAC1, RDC1, HVR1 and VPAC1R, and its full name is vasoactive intestinal peptide receptor 1. NCBI Gene reports several transcript variants that encode different isoforms, so check which isoform an assay or reagent is intended to detect.
Mouse and rat both have a Vipr1 ortholog. VIPR1 and VIPR2 are related receptors in the vasoactive intestinal peptide receptor family. Check the datasheet of any product for its validated reactivity.
VIPR2, the related vasoactive intestinal peptide receptor, and other targets in VIP and PACAP signalling with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P32241; product specifications from Assay Genie datasheets.