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   24-JAN-2024, entry version 156.
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}.
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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   GlyCosmos; P35000; 3 sites, No reported glycans.
DR   GlyGen; P35000; 3 sites.
DR   iPTMnet; P35000; -.
DR   PhosphoSitePlus; P35000; -.
DR   PaxDb; 10116-ENSRNOP00000005876; -.
DR   Ensembl; ENSRNOT00000005876.5; ENSRNOP00000005876.5; ENSRNOG00000004317.5.
DR   Ensembl; ENSRNOT00055008189; ENSRNOP00055006176; ENSRNOG00055005107.
DR   Ensembl; ENSRNOT00060024946; ENSRNOP00060019878; ENSRNOG00060014602.
DR   Ensembl; ENSRNOT00065011216; ENSRNOP00065008188; ENSRNOG00065007208.
DR   GeneID; 29555; -.
DR   KEGG; rno:29555; -.
DR   UCSC; RGD:3962; rat.
DR   AGR; RGD:3962; -.
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; ESALQFH; -.
DR   OrthoDB; 4226399at2759; -.
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 cell types or tissues.
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: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   CDD; cd15986; 7tmB1_VIP-R2; 1.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
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   InterPro; IPR047035; VIP-R2_7TM.
DR   PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR45620:SF22; VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 2; 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; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF111418; Hormone receptor domain; 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.
DR   Genevisible; P35000; RN.
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
//