ID VIPR1_RAT Reviewed; 459 AA. AC P30083; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 24-JAN-2024, entry version 132. DE RecName: Full=Vasoactive intestinal polypeptide receptor 1; DE Short=VIP-R-1; DE AltName: Full=Pituitary adenylate cyclase-activating polypeptide type II receptor; DE Short=PACAP type II receptor; DE Short=PACAP-R-2; DE Short=PACAP-R2; DE Flags: Precursor; GN Name=Vipr1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung; RX PubMed=1314625; DOI=10.1016/0896-6273(92)90101-i; RA Ishihara T., Shigemoto R., Mori K., Takahashi K., Nagata S.; RT "Functional expression and tissue distribution of a novel receptor for RT vasoactive intestinal polypeptide."; RL Neuron 8:811-819(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE OF 1-26, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=8948424; DOI=10.1042/bj3080719; RA Pei L., Melmed S.; RT "Characterization of the rat vasoactive intestinal polypeptide receptor RT gene 5' region."; RL Biochem. J. 308:719-723(1995). CC -!- FUNCTION: This is a receptor for VIP. The activity of this receptor is CC mediated by G proteins which activate adenylyl cyclase. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: In liver, lung, intestines, thymus and brain CC (mostly in the cerebral cortex and hippocampus). CC {ECO:0000269|PubMed:8948424}. CC -!- DEVELOPMENTAL STAGE: Not expressed in the fetal lung, but is expressed CC at high levels 2 weeks after birth. {ECO:0000269|PubMed:8948424}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M86835; AAA42331.1; -; mRNA. DR EMBL; BC087136; AAH87136.1; -; mRNA. DR EMBL; U10635; AAB48185.1; -; Genomic_DNA. DR PIR; JH0594; JH0594. DR RefSeq; NP_036817.1; NM_012685.2. DR AlphaFoldDB; P30083; -. DR SMR; P30083; -. DR BioGRID; 246988; 1. DR STRING; 10116.ENSRNOP00000065438; -. DR BindingDB; P30083; -. DR ChEMBL; CHEMBL1955712; -. DR GuidetoPHARMACOLOGY; 371; -. DR GlyCosmos; P30083; 4 sites, No reported glycans. DR GlyGen; P30083; 4 sites. DR iPTMnet; P30083; -. DR PhosphoSitePlus; P30083; -. DR Ensembl; ENSRNOT00000071573.3; ENSRNOP00000065438.3; ENSRNOG00000047457.3. DR Ensembl; ENSRNOT00055004078; ENSRNOP00055003082; ENSRNOG00055002566. DR Ensembl; ENSRNOT00060036359; ENSRNOP00060029924; ENSRNOG00060020985. DR Ensembl; ENSRNOT00065000695; ENSRNOP00065000569; ENSRNOG00065000481. DR GeneID; 24875; -. DR KEGG; rno:24875; -. DR AGR; RGD:3961; -. DR CTD; 7433; -. DR RGD; 3961; Vipr1. DR GeneTree; ENSGT00940000156402; -. DR InParanoid; P30083; -. DR OMA; SKSQHPW; -. DR OrthoDB; 4209391at2759; -. DR PhylomeDB; P30083; -. DR Reactome; R-RNO-420092; Glucagon-type ligand receptors. DR PRO; PR:P30083; -. DR Proteomes; UP000002494; Chromosome 8. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0043235; C:receptor complex; ISO:RGD. DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central. DR GO; GO:0017046; F:peptide hormone binding; ISO:RGD. DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; IDA:RGD. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro. DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISO:RGD. DR CDD; cd15269; 7tmB1_VIP-R1; 1. DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR017981; GPCR_2-like_7TM. DR InterPro; IPR036445; GPCR_2_extracell_dom_sf. DR InterPro; IPR001879; GPCR_2_extracellular_dom. DR InterPro; IPR000832; GPCR_2_secretin-like. DR InterPro; IPR017983; GPCR_2_secretin-like_CS. DR InterPro; IPR001571; GPCR_2_VIP_rcpt. DR InterPro; IPR001771; GPCR_2_VIP_rcpt_1. DR PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 1. DR PANTHER; PTHR45620:SF24; VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 1; 1. DR Pfam; PF00002; 7tm_2; 1. DR Pfam; PF02793; HRM; 1. DR PRINTS; PR00249; GPCRSECRETIN. DR PRINTS; PR00491; VASOACTVEIPR. DR PRINTS; PR01154; VIP1RECEPTOR. DR SMART; SM00008; HormR; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR SUPFAM; SSF111418; Hormone receptor domain; 1. DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1. DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1. DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. PE 2: Evidence at transcript level; KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..30 FT /evidence="ECO:0000255" FT CHAIN 31..459 FT /note="Vasoactive intestinal polypeptide receptor 1" FT /id="PRO_0000012858" FT TOPO_DOM 31..143 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 144..168 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 169..175 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 176..195 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 196..217 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 218..241 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 242..255 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 256..277 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 278..294 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 295..318 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 319..343 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 344..363 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 364..375 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 376..395 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 396..459 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 58 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 69 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 100 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 292 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 50..72 FT /evidence="ECO:0000250" FT DISULFID 63..105 FT /evidence="ECO:0000250" FT DISULFID 86..122 FT /evidence="ECO:0000250" FT DISULFID 216..286 FT /evidence="ECO:0000250" SQ SEQUENCE 459 AA; 52058 MW; 99E8957DA86698D2 CRC64; MRPPSPPHVR WLCVLAGALA CALRPAGSQA ASPQHECEYL QLIEIQRQQC LEEAQLENET TGCSKMWDNL TCWPTTPRGQ AVVLDCPLIF QLFAPIHGYN ISRSCTEEGW SQLEPGPYHI ACGLNDRASS LDEQQQTKFY NTVKTGYTIG YSLSLASLLV AMAILSLFRK LHCTRNYIHM HLFMSFILRA TAVFIKDMAL FNSGEIDHCS EASVGCKAAV VFFQYCVMAN FFWLLVEGLY LYTLLAVSFF SERKYFWGYI LIGWGVPSVF ITIWTVVRIY FEDFGCWDTI INSSLWWIIK APILLSILVN FVLFICIIRI LVQKLRPPDI GKNDSSPYSR LAKSTLLLIP LFGIHYVMFA FFPDNFKAQV KMVFELVVGS FQGFVVAILY CFLNGEVQAE LRRKWRRWHL QGVLGWSSKS QHPWGGSNGA TCSTQVSMLT RVSPSARRSS SFQAEVSLV //