VIPR2_MOUSE
ID VIPR2_MOUSE Reviewed; 437 AA.
AC P41588; P97750;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Vasoactive intestinal polypeptide receptor 2;
DE Short=VIP-R-2;
DE AltName: Full=Pituitary adenylate cyclase-activating polypeptide type III receptor;
DE Short=PACAP type III receptor;
DE Short=PACAP-R-3;
DE Short=PACAP-R3;
DE Flags: Precursor;
GN Name=Vipr2;
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 [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=8146174; DOI=10.1073/pnas.91.7.2679;
RA Inagaki N., Yoshida H., Mizuta M., Mizuno N., Fujii Y., Gonoi T.,
RA Miyazaki J., Seino S.;
RT "Cloning and functional characterization of a third pituitary adenylate
RT cyclase-activating polypeptide receptor subtype expressed in insulin-
RT secreting cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2679-2683(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-407.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=8784257; DOI=10.1016/0165-5728(96)00063-x;
RA Delgado M., Martinez C., Johnson M.C., Gomariz R.P., Ganea D.;
RT "Differential expression of vasoactive intestinal peptide receptors 1 and 2
RT (VIP-R1 and VIP-R2) mRNA in murine lymphocytes.";
RL J. Neuroimmunol. 68:27-38(1996).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
CC -!- FUNCTION: This is a receptor for VIP as well as PACAP-38 and -27, the
CC activity of this receptor is mediated by G proteins which activate
CC adenylyl cyclase. Can be coupled to phospholipase C.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the MIN6 cells, at
CC moderate levels in pancreatic islets, insulin-secreting cells, lung,
CC brain, stomach, and colon, and at low levels in the heart.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; D28132; BAA05674.1; -; mRNA.
DR EMBL; S82966; AAN86758.1; -; Genomic_DNA.
DR CCDS; CCDS26210.1; -.
DR PIR; A53471; JU0185.
DR RefSeq; NP_033537.1; NM_009511.2.
DR AlphaFoldDB; P41588; -.
DR SMR; P41588; -.
DR STRING; 10090.ENSMUSP00000011315; -.
DR GlyGen; P41588; 3 sites.
DR iPTMnet; P41588; -.
DR PhosphoSitePlus; P41588; -.
DR SwissPalm; P41588; -.
DR PaxDb; P41588; -.
DR PRIDE; P41588; -.
DR ProteomicsDB; 300169; -.
DR Antibodypedia; 18979; 329 antibodies from 35 providers.
DR DNASU; 22355; -.
DR Ensembl; ENSMUST00000011315; ENSMUSP00000011315; ENSMUSG00000011171.
DR GeneID; 22355; -.
DR KEGG; mmu:22355; -.
DR UCSC; uc007phe.2; mouse.
DR CTD; 7434; -.
DR MGI; MGI:107166; Vipr2.
DR VEuPathDB; HostDB:ENSMUSG00000011171; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000158089; -.
DR HOGENOM; CLU_002753_4_4_1; -.
DR InParanoid; P41588; -.
DR OMA; KACTGVW; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P41588; -.
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; 22355; 3 hits in 70 CRISPR screens.
DR PRO; PR:P41588; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P41588; protein.
DR Bgee; ENSMUSG00000011171; Expressed in retinal neural layer and 60 other tissues.
DR ExpressionAtlas; P41588; baseline and differential.
DR Genevisible; P41588; MM.
DR GO; GO:0005929; C:cilium; ISO:MGI.
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:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; ISO:MGI.
DR GO; GO:0007190; P:activation of adenylate cyclase 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:0048662; P:negative regulation of smooth muscle cell proliferation; 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; IPR002284; GPCR_2_VIP_rcpt_2.
DR PANTHER; PTHR45620:SF22; PTHR45620:SF22; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR00491; VASOACTVEIPR.
DR PRINTS; PR01155; VIP2RECEPTOR.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..437
FT /note="Vasoactive intestinal polypeptide receptor 2"
FT /id="PRO_0000012861"
FT TOPO_DOM 23..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..150
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..177
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..226
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..261
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..302
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..347
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..359
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..379
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..60
FT /evidence="ECO:0000250"
FT DISULFID 51..92
FT /evidence="ECO:0000250"
FT DISULFID 74..108
FT /evidence="ECO:0000250"
FT DISULFID 201..270
FT /evidence="ECO:0000250"
FT CONFLICT 397
FT /note="A -> P (in Ref. 2; AAN86758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 49474 MW; CCC870A094F9DC90 CRC64;
MRASVVLTCY CWLLVRVSSI HPECRFHLEI QEEETKCAEL LSSQTENQRA CSGVWDNITC
WRPADVGETV TVPCPKVFSN FYSRPGNISK NCTSDGWSET FPDFIDACGY NDPEDESKIS
FYILVKAIYT LGYSVSLMSL TTGSIIICLF RKLHCTRNYI HLNLFLSFML RAISVLVKDS
VLYSSSGLLR CHDQPASWVG CKLSLVFFQY CIMANFYWLL VEGLYLHTLL VAILPPSRCF
LAYLLIGWGI PSVCIGAWTA TRLSLEDTGC WDTNDHSIPW WVIRMPILIS IVVNFALFIS
IVRILLQKLT SPDVGGNDQS QYKRLAKSTL LLIPLFGVHY MVFAAFPIGI SSTYQILFEL
CVGSFQGLVV AVLYCFLNSE VQCELKRRWR GLCLTQAGSR DYRLHSWSMS RNGSESALQI
HRGSRTQSFL QSETSVI
