VIPR1_RAT
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 03-AUG-2022, entry version 125.
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}.
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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 BindingDB; P30083; -.
DR ChEMBL; CHEMBL1955712; -.
DR GuidetoPHARMACOLOGY; 371; -.
DR GlyGen; P30083; 4 sites.
DR iPTMnet; P30083; -.
DR PhosphoSitePlus; P30083; -.
DR Ensembl; ENSRNOT00000071573; ENSRNOP00000065438; ENSRNOG00000047457.
DR GeneID; 24875; -.
DR KEGG; rno:24875; -.
DR CTD; 7433; -.
DR RGD; 3961; Vipr1.
DR GeneTree; ENSGT00940000156402; -.
DR InParanoid; P30083; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P30083; -.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR PRO; PR:P30083; -.
DR Proteomes; UP000002494; Chromosome 8.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
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 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; SSF111418; SSF111418; 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
