VIPR1_MOUSE
ID VIPR1_MOUSE Reviewed; 459 AA.
AC P97751; Q9JI40; Q9R1T8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 159.
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 AltName: Full=VPAC1;
DE Flags: Precursor;
GN Name=Vipr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10331949; DOI=10.1006/geno.1999.5805;
RA Hashimoto H., Nishino A., Shintani N., Hagihara N., Copeland N.G.,
RA Jenkins N.A., Yamamoto K., Matsuda T., Ishihara T., Nagata S., Baba A.;
RT "Genomic organization and chromosomal location of the mouse vasoactive
RT intestinal polypeptide 1 (VPAC1) receptor.";
RL Genomics 58:90-93(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FVB/N;
RA Karacay B., O'Dorisio M.S., Kasow K., Krahe R.;
RT "Cloning and fine mapping of the vasoactive intestinal peptide receptor I
RT (VPAC1): a comparative analysis of human, rat and murine genes.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-398.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=8784267; DOI=10.1016/0165-5728(96)00085-9;
RA Johnson M.C., McCormack R.J., Delgado M., Martinez C., Ganea D.;
RT "Murine T-lymphocytes express vasoactive intestinal peptide receptor 1
RT (VIP-R1) mRNA.";
RL J. Neuroimmunol. 68:109-119(1996).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; AB022860; BAA81896.1; -; Genomic_DNA.
DR EMBL; AF266282; AAF77053.1; -; mRNA.
DR EMBL; AK052465; BAC35004.1; -; mRNA.
DR EMBL; S82970; AAN86759.1; -; Genomic_DNA.
DR CCDS; CCDS23633.1; -.
DR RefSeq; NP_035833.2; NM_011703.4.
DR AlphaFoldDB; P97751; -.
DR SMR; P97751; -.
DR BioGRID; 204526; 3.
DR STRING; 10090.ENSMUSP00000035115; -.
DR GlyGen; P97751; 5 sites.
DR iPTMnet; P97751; -.
DR PhosphoSitePlus; P97751; -.
DR MaxQB; P97751; -.
DR PaxDb; P97751; -.
DR PRIDE; P97751; -.
DR ProteomicsDB; 297575; -.
DR Antibodypedia; 12331; 441 antibodies from 37 providers.
DR DNASU; 22354; -.
DR Ensembl; ENSMUST00000035115; ENSMUSP00000035115; ENSMUSG00000032528.
DR GeneID; 22354; -.
DR KEGG; mmu:22354; -.
DR UCSC; uc009sdl.2; mouse.
DR CTD; 7433; -.
DR MGI; MGI:109272; Vipr1.
DR VEuPathDB; HostDB:ENSMUSG00000032528; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000156402; -.
DR HOGENOM; CLU_002753_4_4_1; -.
DR InParanoid; P97751; -.
DR OMA; YHHPSVG; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P97751; -.
DR TreeFam; TF315710; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR BioGRID-ORCS; 22354; 2 hits in 71 CRISPR screens.
DR PRO; PR:P97751; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P97751; protein.
DR Bgee; ENSMUSG00000032528; Expressed in small intestine Peyer's patch and 76 other tissues.
DR Genevisible; P97751; MM.
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:MGI.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; ISO:MGI.
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:MGI.
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 1: Evidence at protein 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_0000012856"
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 104
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"
FT CONFLICT 59
FT /note="E -> K (in Ref. 1; BAA81896)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 52096 MW; 9D1ADFB8567D4D7F CRC64;
MRPPSLPPAR WLCVLAGALA CALGPAGSRA ASPHQECEYL QMIEKQRQQC LEEAQLENET
TGCSKMWDNL TCWPTTPWGQ VVVLDCPLIF QLFSPIHGYN ISRNCTEEGW SQLEPGPYHI
ACGLNDRASS MDEQQQTEFY DAVKTGYTIG YSLSLASLLV AMAILSLFRK LHCTRNYIHM
HLFMSFILRA TAVFIKDMAL FNNGETDHCS EASVSCKAAV VFFQYCVMAN FFWLLVEGLY
LHTLLAVSFF SERKYFWGYI LIGWGVPSVF IMIWTIVRIH FEDFGCWDTI INSSLWWIIK
GPILISILVN FILFICIIRI LVQKLRPPDI GKNDSSPYSR LAKSTLLLIP LFGVHYVMFA
FFPDNFKAQV KMVFELVVGS FQGFVVAILY CFLNGEVQAE LRRKWRRWHL QGVLGWSSKS
QHPWGGSNGV SCSTQVSMLT RVSPSARRSS SFQAEVSLV
