VIPR2_RAT
ID VIPR2_RAT Reviewed; 437 AA.
AC P35000;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 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 STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
RX PubMed=8224221; DOI=10.1016/0014-5793(93)81668-p;
RA Lutz E.-M., Sheward W.J., West K.M., Morrow J.A., Fink G., Harmar A.J.;
RT "The VIP2 receptor: molecular characterisation of a cDNA encoding a novel
RT receptor for vasoactive intestinal peptide.";
RL FEBS Lett. 334:3-8(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain cortex;
RX PubMed=7988457; DOI=10.1210/endo.135.6.7988457;
RA Usdin T.B., Bonner T.I., Mezey E.;
RT "Two receptors for vasoactive intestinal polypeptide with similar
RT specificity and complementary distributions.";
RL Endocrinology 135:2662-2680(1994).
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 -!- 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; Z25885; CAA81104.1; -; mRNA.
DR EMBL; U09631; AAB60459.1; -; mRNA.
DR PIR; S39069; S39069.
DR RefSeq; NP_058934.1; NM_017238.1.
DR AlphaFoldDB; P35000; -.
DR SMR; P35000; -.
DR BioGRID; 248189; 1.
DR STRING; 10116.ENSRNOP00000005876; -.
DR BindingDB; P35000; -.
DR GuidetoPHARMACOLOGY; 372; -.
DR GlyGen; P35000; 3 sites.
DR iPTMnet; P35000; -.
DR PhosphoSitePlus; P35000; -.
DR PaxDb; P35000; -.
DR Ensembl; ENSRNOT00000005876; ENSRNOP00000005876; ENSRNOG00000004317.
DR GeneID; 29555; -.
DR KEGG; rno:29555; -.
DR UCSC; RGD:3962; rat.
DR CTD; 7434; -.
DR RGD; 3962; Vipr2.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000158089; -.
DR HOGENOM; CLU_002753_4_4_1; -.
DR InParanoid; P35000; -.
DR OMA; KACTGVW; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P35000; -.
DR TreeFam; TF315710; -.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR PRO; PR:P35000; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004317; Expressed in thymus and 15 other tissues.
DR Genevisible; P35000; RN.
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; IDA:RGD.
DR GO; GO:0007190; P:activation of adenylate cyclase 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:0048662; P:negative regulation of smooth muscle cell proliferation; IMP: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; 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 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..437
FT /note="Vasoactive intestinal polypeptide receptor 2"
FT /id="PRO_0000012862"
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 383
FT /note="C -> R (in Ref. 2; AAB60459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 49553 MW; 7E10218A9EE31360 CRC64;
MRASVVLTCY CWLLVRVSSI HPECRFHLEI QEEETKCAEL LSSQMENHRA CSGVWDNITC
WRPADIGETV TVPCPKVFSN FYSRPGNISK NCTSDGWSET FPDFIDACGY NDPEDESKIT
FYILVKAIYT LGYSVSLMSL TTGSIIICLF RKLHCTRNYI HLNLFLSFML RAISVLVKDS
VLYSSSGTLR CHDQPGSWVG CKLSLVFFQY CIMANFYWLL VEGLYLHTLL VAILPPSRCF
LAYLLIGWGI PSVCIGAWIA TRLSLEDTGC WDTNDHSIPW WVIRMPILIS IVVNFALFIS
IVRILLQKLT SPDVGGNDQS QYKRLAKSTL LLIPLFGVHY MVFAAFPIGI SSTYQILFEL
CVGSFQGLVV AVLYCFLNSE VQCELKRRWR GLCLTQPGSR DYRLHSWSMS RNGSESALQI
HRGSRTQSFL QSETSVI
