VIPR1_HUMAN
ID VIPR1_HUMAN Reviewed; 457 AA.
AC P32241; A5JUT9; B3KPV1; B4DEB5; B4DGI4; F5H1F5; G3V0I1; Q15871; Q6P2M6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 198.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM SHORT).
RC TISSUE=Intestine;
RX PubMed=8390245; DOI=10.1006/bbrc.1993.1658;
RA Sreedharan S.P., Patel D.R., Huang J.-X., Goetzl E.J.;
RT "Cloning and functional expression of a human neuroendocrine vasoactive
RT intestinal peptide receptor.";
RL Biochem. Biophys. Res. Commun. 193:546-553(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT AND LONG), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Intestine;
RX PubMed=8179610; DOI=10.1006/bbrc.1994.1517;
RA Couvineau A., Rouyer-Fessard C., Darmoul D., Maoret J.J., Carrero I.,
RA Ogier-Denis E., Laburthe M.;
RT "Human intestinal VIP receptor: cloning and functional expression of two
RT cDNA encoding proteins with different N-terminal domains.";
RL Biochem. Biophys. Res. Commun. 200:769-776(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC TISSUE=Lung;
RA Martin A.L., Kaighin V.A., Aronstam R.S.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SHORT; 3; 4 AND 5).
RC TISSUE=Brain, Cerebellum, Lung, and Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT), AND VARIANT
RP MET-341.
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-457.
RC TISSUE=Liver;
RX PubMed=7917790; DOI=10.1016/0898-6568(94)90037-x;
RA Gagnon A.W., Aiyar N., Elshourbagy N.A.;
RT "Molecular cloning and functional characterization of a human liver
RT vasoactive intestinal peptide receptor.";
RL Cell. Signal. 6:321-333(1994).
RN [10]
RP INTERACTION WITH VIP.
RX PubMed=7818527; DOI=10.1006/bbrc.1995.1034;
RA Couvineau A., Gaudin P., Maoret J.J., Rouyer-Fessard C., Nicole P.,
RA Laburthe M.;
RT "Highly conserved aspartate 68, tryptophan 73 and glycine 109 in the N-
RT terminal extracellular domain of the human VIP receptor are essential for
RT its ability to bind VIP.";
RL Biochem. Biophys. Res. Commun. 206:246-252(1995).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8926282; DOI=10.1007/bf01540969;
RA Xia M., Sreedharan S.P., Goetzl E.J.;
RT "Predominant expression of type II vasoactive intestinal peptide receptors
RT by human T lymphoblastoma cells: transduction of both Ca2+ and cyclic AMP
RT signals.";
RL J. Clin. Immunol. 16:21-30(1996).
RN [12]
RP DISULFIDE BOND.
RX PubMed=9928020; DOI=10.1111/j.1749-6632.1998.tb11186.x;
RA Knudsen S.M., Tams J.W., Wulff B.S., Fahrenkrug J.;
RT "Importance of conserved cysteines in the extracellular loops of human
RT PACAP/VIP1 receptor for ligand binding and stimulation of cAMP
RT production.";
RL Ann. N. Y. Acad. Sci. 865:259-265(1998).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 400-408 IN COMPLEX WITH MHC.
RX PubMed=14734527; DOI=10.1084/jem.20031690;
RA Hulsmeyer M., Fiorillo M.T., Bettosini F., Sorrentino R., Saenger W.,
RA Ziegler A., Uchanska-Ziegler B.;
RT "Dual, HLA-B27 subtype-dependent conformation of a self-peptide.";
RL J. Exp. Med. 199:271-281(2004).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 400-408 IN COMPLEX WITH MHC.
RX PubMed=18650441; DOI=10.1074/jbc.m802818200;
RA Beltrami A., Rossmann M., Fiorillo M.T., Paladini F., Sorrentino R.,
RA Saenger W., Kumar P., Ziegler A., Uchanska-Ziegler B.;
RT "Citrullination-dependent differential presentation of a self-peptide by
RT HLA-B27 subtypes.";
RL J. Biol. Chem. 283:27189-27199(2008).
CC -!- FUNCTION: This is a receptor for VIP. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase. The affinity is
CC VIP = PACAP-27 > PACAP-38. {ECO:0000269|PubMed:8926282}.
CC -!- INTERACTION:
CC P32241; Q9NQX1-2: PRDM5; NbExp=3; IntAct=EBI-3917984, EBI-12859340;
CC P32241; PRO_0000011460 [P01282]: VIP; NbExp=2; IntAct=EBI-3917984, EBI-6656819;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=Short; Synonyms=hIVR8;
CC IsoId=P32241-1; Sequence=Displayed;
CC Name=Long; Synonyms=hIVR5;
CC IsoId=P32241-2; Sequence=VSP_002010;
CC Name=3;
CC IsoId=P32241-3; Sequence=VSP_045143;
CC Name=4;
CC IsoId=P32241-4; Sequence=VSP_047271, VSP_047273;
CC Name=5;
CC IsoId=P32241-5; Sequence=VSP_047272;
CC -!- TISSUE SPECIFICITY: In lung, HT-29 colonic epithelial cells, Raji B-
CC lymphoblasts. Lesser extent in brain, heart, kidney, liver and
CC placenta. Not expressed in CD4+ or CD8+ T-cells. Expressed in the T-
CC cell lines HARRIS, HuT 78, Jurkat and SUP-T1, but not in the T-cell
CC lines Peer, MOLT-4, HSB and YT. {ECO:0000269|PubMed:8926282}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; L13288; AAA36805.1; -; mRNA.
DR EMBL; U11087; AAB60362.1; -; Genomic_DNA.
DR EMBL; U11079; AAB60362.1; JOINED; Genomic_DNA.
DR EMBL; U11080; AAB60362.1; JOINED; Genomic_DNA.
DR EMBL; U11081; AAB60362.1; JOINED; Genomic_DNA.
DR EMBL; U11083; AAB60362.1; JOINED; Genomic_DNA.
DR EMBL; U11084; AAB60362.1; JOINED; Genomic_DNA.
DR EMBL; U11085; AAB60362.1; JOINED; Genomic_DNA.
DR EMBL; U11086; AAB60362.1; JOINED; Genomic_DNA.
DR EMBL; X75299; CAA53046.1; -; mRNA.
DR EMBL; X77777; CAA54814.1; -; mRNA.
DR EMBL; AB065669; BAC05895.1; -; Genomic_DNA.
DR EMBL; EF577396; ABQ52416.1; -; mRNA.
DR EMBL; AK314334; BAG36980.1; -; mRNA.
DR EMBL; AK293548; BAG57026.1; -; mRNA.
DR EMBL; AK294609; BAG57795.1; -; mRNA.
DR EMBL; AK056819; BAG51813.1; -; mRNA.
DR EMBL; AC092047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64649.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW64650.1; -; Genomic_DNA.
DR EMBL; BC064424; AAH64424.1; -; mRNA.
DR EMBL; L20295; AAA36802.1; -; mRNA.
DR CCDS; CCDS2698.1; -. [P32241-1]
DR CCDS; CCDS58827.1; -. [P32241-4]
DR CCDS; CCDS58828.1; -. [P32241-5]
DR CCDS; CCDS58829.1; -. [P32241-3]
DR PIR; JC2194; JC2194.
DR PIR; JC2195; JC2195.
DR RefSeq; NP_001238811.1; NM_001251882.1. [P32241-5]
DR RefSeq; NP_001238812.1; NM_001251883.1. [P32241-3]
DR RefSeq; NP_001238813.1; NM_001251884.1. [P32241-4]
DR RefSeq; NP_001238814.1; NM_001251885.1.
DR RefSeq; NP_004615.2; NM_004624.3. [P32241-1]
DR RefSeq; XP_005265495.1; XM_005265438.3. [P32241-5]
DR RefSeq; XP_011532381.1; XM_011534079.1. [P32241-5]
DR PDB; 1OF2; X-ray; 2.20 A; C=400-408.
DR PDB; 1OGT; X-ray; 1.47 A; C=400-408.
DR PDB; 3B3I; X-ray; 1.86 A; C=400-408.
DR PDB; 3B6S; X-ray; 1.80 A; C=400-408.
DR PDB; 3DTX; X-ray; 2.10 A; C=400-408.
DR PDB; 3HCV; X-ray; 1.95 A; C=400-408.
DR PDB; 5DEF; X-ray; 1.60 A; C=400-408.
DR PDB; 5DEG; X-ray; 1.83 A; C=400-408.
DR PDB; 5IB1; X-ray; 1.91 A; C=400-408.
DR PDB; 5IB2; X-ray; 1.44 A; C=400-408.
DR PDB; 5IB3; X-ray; 1.91 A; C=400-408.
DR PDB; 5IB4; X-ray; 1.95 A; C=400-408.
DR PDB; 5IB5; X-ray; 2.49 A; C/F=400-408.
DR PDB; 6VN7; EM; 3.20 A; R=31-437.
DR PDB; 7ALO; X-ray; 1.80 A; C/F=400-408.
DR PDBsum; 1OF2; -.
DR PDBsum; 1OGT; -.
DR PDBsum; 3B3I; -.
DR PDBsum; 3B6S; -.
DR PDBsum; 3DTX; -.
DR PDBsum; 3HCV; -.
DR PDBsum; 5DEF; -.
DR PDBsum; 5DEG; -.
DR PDBsum; 5IB1; -.
DR PDBsum; 5IB2; -.
DR PDBsum; 5IB3; -.
DR PDBsum; 5IB4; -.
DR PDBsum; 5IB5; -.
DR PDBsum; 6VN7; -.
DR PDBsum; 7ALO; -.
DR AlphaFoldDB; P32241; -.
DR SMR; P32241; -.
DR BioGRID; 113274; 245.
DR IntAct; P32241; 27.
DR MINT; P32241; -.
DR STRING; 9606.ENSP00000327246; -.
DR BindingDB; P32241; -.
DR ChEMBL; CHEMBL5144; -.
DR DrugCentral; P32241; -.
DR GuidetoPHARMACOLOGY; 371; -.
DR TCDB; 9.A.14.4.9; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P32241; 4 sites.
DR iPTMnet; P32241; -.
DR PhosphoSitePlus; P32241; -.
DR SwissPalm; P32241; -.
DR BioMuta; VIPR1; -.
DR DMDM; 418253; -.
DR jPOST; P32241; -.
DR MassIVE; P32241; -.
DR PaxDb; P32241; -.
DR PeptideAtlas; P32241; -.
DR PRIDE; P32241; -.
DR ProteomicsDB; 25640; -.
DR ProteomicsDB; 32204; -.
DR ProteomicsDB; 3938; -.
DR ProteomicsDB; 54848; -. [P32241-1]
DR ProteomicsDB; 54849; -. [P32241-2]
DR ABCD; P32241; 2 sequenced antibodies.
DR Antibodypedia; 12331; 441 antibodies from 37 providers.
DR DNASU; 7433; -.
DR Ensembl; ENST00000325123.5; ENSP00000327246.4; ENSG00000114812.13. [P32241-1]
DR Ensembl; ENST00000433647.5; ENSP00000394950.1; ENSG00000114812.13. [P32241-5]
DR Ensembl; ENST00000438259.6; ENSP00000415371.2; ENSG00000114812.13. [P32241-3]
DR Ensembl; ENST00000543411.5; ENSP00000445701.1; ENSG00000114812.13. [P32241-4]
DR GeneID; 7433; -.
DR KEGG; hsa:7433; -.
DR MANE-Select; ENST00000325123.5; ENSP00000327246.4; NM_004624.4; NP_004615.2.
DR UCSC; uc003clf.3; human. [P32241-1]
DR CTD; 7433; -.
DR DisGeNET; 7433; -.
DR GeneCards; VIPR1; -.
DR HGNC; HGNC:12694; VIPR1.
DR HPA; ENSG00000114812; Tissue enhanced (lung).
DR MIM; 192321; gene.
DR neXtProt; NX_P32241; -.
DR OpenTargets; ENSG00000114812; -.
DR PharmGKB; PA37313; -.
DR VEuPathDB; HostDB:ENSG00000114812; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000156402; -.
DR HOGENOM; CLU_1124194_0_0_1; -.
DR InParanoid; P32241; -.
DR OMA; YHHPSVG; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P32241; -.
DR TreeFam; TF315710; -.
DR PathwayCommons; P32241; -.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-420092; Glucagon-type ligand receptors.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P32241; -.
DR SIGNOR; P32241; -.
DR BioGRID-ORCS; 7433; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; VIPR1; human.
DR EvolutionaryTrace; P32241; -.
DR GeneWiki; VIPR1; -.
DR GenomeRNAi; 7433; -.
DR Pharos; P32241; Tchem.
DR PRO; PR:P32241; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P32241; protein.
DR Bgee; ENSG00000114812; Expressed in right lung and 141 other tissues.
DR ExpressionAtlas; P32241; baseline and differential.
DR Genevisible; P32241; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; IPI:GO_Central.
DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; IDA:GO_Central.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IDA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
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 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..457
FT /note="Vasoactive intestinal polypeptide receptor 1"
FT /id="PRO_0000012855"
FT TOPO_DOM 31..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..167
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..194
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..240
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..276
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..316
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..361
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..373
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..393
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 394..457
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 290
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 215..285
FT /evidence="ECO:0000269|PubMed:9928020"
FT VAR_SEQ 1..263
FT /note="MRPPSPLPARWLCVLAGALAWALGPAGGQAARLQEECDYVQMIEVQHKQCLE
FT EAQLENETIGCSKMWDNLTCWPATPRGQVVVLACPLIFKLFSSIQGRNVSRSCTDEGWT
FT HLEPGPYPIACGLDDKAASLDEQQTMFYGSVKTGYTIGYGLSLATLLVATAILSLFRKL
FT HCTRNYIHMHLFISFILRAAAVFIKDLALFDSGESDQCSEGSVGCKAAMVFFQYCVMAN
FT FFWLLVEGLYLYTLLAVSFFSERKYFWGYILIGW -> MTRQRVWMRWAVRQPWSFSNI
FT VSWLTSSGCWWRASTCTPCLPSPSSLSGSTSG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045143"
FT VAR_SEQ 1..61
FT /note="MRPPSPLPARWLCVLAGALAWALGPAGGQAARLQEECDYVQMIEVQHKQCLE
FT EAQLENETI -> MRAGRRPRLGPWAG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047271"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047272"
FT VAR_SEQ 1..32
FT /note="MRPPSPLPARWLCVLAGALAWALGPAGGQAAR -> MPPPPLLSLRRLGGGW
FT SAVTRLVVAAAGARSRGGRGGSRGAGGGGRGGVARRRRLELRAARSLLGSS (in
FT isoform Long)"
FT /evidence="ECO:0000303|PubMed:8179610"
FT /id="VSP_002010"
FT VAR_SEQ 134
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047273"
FT VARIANT 341
FT /note="R -> M (in dbSNP:rs17855906)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055041"
FT VARIANT 445
FT /note="R -> L (in dbSNP:rs3733055)"
FT /id="VAR_020021"
FT CONFLICT 80
FT /note="Q -> R (in Ref. 5; BAG57795)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="G -> GLLR (in Ref. 2; CAA54814/CAA53046)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="L -> F (in Ref. 5; BAG51813)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="K -> R (in Ref. 5; BAG57795)"
FT /evidence="ECO:0000305"
FT HELIX 130..166
FT /evidence="ECO:0007829|PDB:6VN7"
FT HELIX 173..200
FT /evidence="ECO:0007829|PDB:6VN7"
FT HELIX 213..245
FT /evidence="ECO:0007829|PDB:6VN7"
FT HELIX 251..280
FT /evidence="ECO:0007829|PDB:6VN7"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6VN7"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:6VN7"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:6VN7"
FT HELIX 299..323
FT /evidence="ECO:0007829|PDB:6VN7"
FT HELIX 336..344
FT /evidence="ECO:0007829|PDB:6VN7"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:6VN7"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:6VN7"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6VN7"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:6VN7"
FT HELIX 366..388
FT /evidence="ECO:0007829|PDB:6VN7"
FT HELIX 393..408
FT /evidence="ECO:0007829|PDB:6VN7"
SQ SEQUENCE 457 AA; 51547 MW; DAA40CF5BEC47D7D CRC64;
MRPPSPLPAR WLCVLAGALA WALGPAGGQA ARLQEECDYV QMIEVQHKQC LEEAQLENET
IGCSKMWDNL TCWPATPRGQ VVVLACPLIF KLFSSIQGRN VSRSCTDEGW THLEPGPYPI
ACGLDDKAAS LDEQQTMFYG SVKTGYTIGY GLSLATLLVA TAILSLFRKL HCTRNYIHMH
LFISFILRAA AVFIKDLALF DSGESDQCSE GSVGCKAAMV FFQYCVMANF FWLLVEGLYL
YTLLAVSFFS ERKYFWGYIL IGWGVPSTFT MVWTIARIHF EDYGCWDTIN SSLWWIIKGP
ILTSILVNFI LFICIIRILL QKLRPPDIRK SDSSPYSRLA RSTLLLIPLF GVHYIMFAFF
PDNFKPEVKM VFELVVGSFQ GFVVAILYCF LNGEVQAELR RKWRRWHLQG VLGWNPKYRH
PSGGSNGATC STQVSMLTRV SPGARRSSSF QAEVSLV
