VIPR1_PIG
ID VIPR1_PIG Reviewed; 458 AA.
AC Q28992;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 106.
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 Flags: Precursor;
GN Name=VIPR1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hsiung H.M., Smith D.P., Hyslop P.A., Heiman M.L., Hassan H.A., Zhang X.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This is a receptor for VIP. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase (By similarity).
CC {ECO:0000250}.
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; U49434; AAA93390.1; -; mRNA.
DR RefSeq; NP_999201.1; NM_214036.1.
DR AlphaFoldDB; Q28992; -.
DR SMR; Q28992; -.
DR STRING; 9823.ENSSSCP00000012026; -.
DR PaxDb; Q28992; -.
DR GeneID; 100155402; -.
DR KEGG; ssc:100155402; -.
DR CTD; 7433; -.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; Q28992; -.
DR OrthoDB; 651627at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..458
FT /note="Vasoactive intestinal polypeptide receptor 1"
FT /id="PRO_0000012857"
FT TOPO_DOM 32..143
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..168
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..195
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..241
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..277
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..317
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..362
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..394
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..458
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 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..73
FT /evidence="ECO:0000250"
FT DISULFID 64..106
FT /evidence="ECO:0000250"
FT DISULFID 87..123
FT /evidence="ECO:0000250"
FT DISULFID 216..286
FT /evidence="ECO:0000250"
SQ SEQUENCE 458 AA; 51479 MW; E166E4D6B3BE1189 CRC64;
MRPLSPPPAG WFCVLAGVLA CVLGPVGSWA VGLQQEECDY LQMIKVQHKQ CLEEAQLENE
TSGCSKMWDN LTCWPATPRG QVVVLACPLI FKLFSPTQGL NVSRNCTDEG WTPLEPGPYP
IACGMDDKAS GLDEQQTVFY NSVKTGYTIG YSLSLAALLV ATAILSLFRK LHCTRNYIHM
HLFISFILRA TAVFIKDLAL FDSEESDHCS KGSVGCKAAV VLFQYCVMAN FFWLLVEGLY
LHTLLAVSFF SERKYFWGYI FVGWGVPSTF IMVWTVVRIH FEDYGCWDTI HSSLWWIIKA
PILASILVNF ILFIRIIGIL VQKLRPPDVG KSDNSPYSRL AKSTLLLIPL FGVHYIMFAF
FPDNFKAEVK MVFELIVGSF QGCVVAILYC FLNGEVQAEL RRKWRRWHQQ GVLGWDSKYQ
HPSGGSNGDT CSTQVSMLTR VSPSARRSSS FQAEVSLV
