VIPR_MELGA
ID VIPR_MELGA Reviewed; 457 AA.
AC Q91085;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Vasoactive intestinal polypeptide receptor;
DE Short=VIP receptor;
DE Short=VIP-R;
DE Flags: Precursor;
GN Name=VIPR1;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC TISSUE=Pituitary, and Small intestine;
RX PubMed=11703071; DOI=10.1006/gcen.2001.7685;
RA You S., Hsu C.-C., Kim H., Kho Y., Choi Y.J., el Halawani M.E., Farris J.,
RA Foster D.N.;
RT "Molecular cloning and expression analysis of the turkey vasoactive
RT intestinal peptide receptor.";
RL Gen. Comp. Endocrinol. 124:53-65(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 198-457.
RC TISSUE=Small intestine;
RX PubMed=8618952; DOI=10.3181/00379727-212-43991;
RA Xu M., Proudman J.A., Pitts G.R., Wong E.A., Foster D.N., el Halawani M.E.;
RT "Vasoactive intestinal peptide stimulates prolactin mRNA expression in
RT turkey pituitary cells: effects of dopaminergic drugs.";
RL Proc. Soc. Exp. Biol. Med. 212:52-62(1996).
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 -!- TISSUE SPECIFICITY: Expressed in pituitary, hypothalamus, small
CC intestine and ovarian follicles. {ECO:0000269|PubMed:11703071}.
CC -!- DEVELOPMENTAL STAGE: Pituitary levels are highest in non-
CC photostimulated and incubating birds and lower in photostimulated,
CC laying and photorefractory birds. {ECO:0000269|PubMed:11703071}.
CC -!- INDUCTION: Pituitary levels decrease on VIP immunization.
CC {ECO:0000269|PubMed:11703071}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; U31991; AAA99740.2; -; mRNA.
DR RefSeq; NP_001290107.1; NM_001303178.1.
DR AlphaFoldDB; Q91085; -.
DR SMR; Q91085; -.
DR GeneID; 100303683; -.
DR KEGG; mgp:100303683; -.
DR InParanoid; Q91085; -.
DR OrthoDB; 651627at2759; -.
DR Proteomes; UP000001645; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..457
FT /note="Vasoactive intestinal polypeptide receptor"
FT /id="PRO_0000012859"
FT TOPO_DOM 20..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..166
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..193
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..239
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..275
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..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 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
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 DISULFID 51..73
FT /evidence="ECO:0000250"
FT DISULFID 64..105
FT /evidence="ECO:0000250"
FT DISULFID 87..122
FT /evidence="ECO:0000250"
FT DISULFID 214..284
FT /evidence="ECO:0000250"
SQ SEQUENCE 457 AA; 52770 MW; D862F1F2BE4ECBBC CRC64;
MGLVEVVWWW RWRFGGGGGG LVVEVEVWWW RWRFGGGGCI MLEIEEERSQ CPAEITEDNQ
TSGCRRQWDN ITCWPEAQVG AVVVKPCPKY FRLLTTFLGN VSRNCTSQGW TDVYPAPYAV
ACGYDSTAHQ GKEQTAFYGT VKTGYTIGHT LSLIALTAAM IILCLFRKLH CTRNYIHMHL
FMSFIMRAIA VFIKDVTLFE SGEPEHCFVS SVGCKAMMVF FQYCVMANFF WLLVEGLYLH
TLLVISFFSE RKYFWWYILI GWGAPSVFIT AWTVVRIYFF NVGCWEEIIE SPIWWIIKTP
ILVSILVNFI LFICIIRILV QKLHSPDVGH NETSQYSRLA KSTLLLIPLF GIHYIMFAFF
PDNFKAQVKL VFELVVGSFQ GFVVAVLYCF LNGEVQAELK RKWRRWHLER FLGSDMKYHH
PSLGSNGTNF STQISMLTKC SPKTRRCSSF QAEFSLV
