VIPR_CARAU
ID VIPR_CARAU Reviewed; 447 AA.
AC Q90308;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Vasoactive intestinal polypeptide receptor;
DE Short=VIP receptor;
DE Short=VIP-R;
GN Name=vipr1;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9038250; DOI=10.1006/gcen.1996.6818;
RA Chow B.K.C., Yuen T.T.H., Chan K.W.;
RT "Molecular evolution of vertebrate VIP receptors and functional
RT characterization of a VIP receptor from goldfish Carassius auratus.";
RL Gen. Comp. Endocrinol. 105:176-185(1997).
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 -!- 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; U56391; AAB05459.1; -; mRNA.
DR AlphaFoldDB; Q90308; -.
DR SMR; Q90308; -.
DR Proteomes; UP000515129; Genome assembly.
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; IPR001771; GPCR_2_VIP_rcpt_1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
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; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..447
FT /note="Vasoactive intestinal polypeptide receptor"
FT /id="PRO_0000070331"
FT TOPO_DOM 1..103
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..128
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..155
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..202
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..238
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..280
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..325
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..357
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 15..36
FT /evidence="ECO:0000250"
FT DISULFID 27..69
FT /evidence="ECO:0000250"
FT DISULFID 50..86
FT /evidence="ECO:0000250"
FT DISULFID 177..247
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 50959 MW; 66839E243702554C CRC64;
MCDVVNEIEL ARARCENKTA GNVTSGCKGM WDIIACWPSA KVGEHVVIPC PNYFRHFSDH
HEGNLSKTCT ADGWTEMDPM EIAVYCGYNL NGTVDDDSFF RSVKIGYTIG HSVSLISLTT
AIVILCMSRK LHCTRNYIHM HLFVSFILKA IAVFVKDAVL YDVIQESDNC STASVGCKAV
IVFFQYCIMA SFFWLLVEGL YLHALLAVSF FSERKYFWWY ILIGWGGPTI FIMAWSFAKA
YFNDVGCWDI IENSDLFWWI IKTPILASIL MNFILFICII RILRQKINCP DIGRNESNQY
SRLAKSTLLL IPLFGINFII FAFIPENIKT ELRLVFDLIL GSFQGFVVAV LYCFLNGEVQ
AEIKRKWRRW HLERFLGPDT KYQHPSMGSN GNNFSTQISM LTRCSPKTRR ASTCQDETSI
TVLGSTTMGY GHQNETVKGH EDVREVS
