ID   PKR1_BOVIN              Reviewed;         393 AA.
AC   Q8SPN2;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Prokineticin receptor 1;
DE            Short=PK-R1;
DE   AltName: Full=G-protein coupled receptor 73;
DE   AltName: Full=G-protein coupled receptor ZAQ;
GN   Name=PROKR1; Synonyms=GPR73, PKR1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12054613; DOI=10.1016/s0006-291x(02)00239-5;
RA   Masuda Y., Takatsu Y., Terao Y., Kumano S., Ishibashi Y., Suenaga M.,
RA   Abe M., Fukusumi S., Watanabe T., Shintani Y., Yamada T., Hinuma S.,
RA   Inatomi N., Ohtaki T., Onda H., Fujino M.;
RT   "Isolation and identification of EG-VEGF/prokineticins as cognate ligands
RT   for two orphan G-protein-coupled receptors.";
RL   Biochem. Biophys. Res. Commun. 293:396-402(2002).
CC   -!- FUNCTION: Receptor for prokineticin 1. Exclusively coupled to the G(q)
CC       subclass of heteromeric G proteins. Activation leads to mobilization of
CC       calcium, stimulation of phosphoinositide turnover and activation of
CC       p44/p42 mitogen-activated protein kinase. May play a role during early
CC       pregnancy (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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; AY089972; AAM11888.1; -; mRNA.
DR   RefSeq; NP_776755.1; NM_174330.1.
DR   AlphaFoldDB; Q8SPN2; -.
DR   SMR; Q8SPN2; -.
DR   STRING; 9913.ENSBTAP00000027549; -.
DR   PaxDb; Q8SPN2; -.
DR   GeneID; 281800; -.
DR   KEGG; bta:281800; -.
DR   CTD; 10887; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q8SPN2; -.
DR   OrthoDB; 664455at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000611; NPY_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01012; NRPEPTIDEYR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 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..393
FT                   /note="Prokineticin receptor 1"
FT                   /id="PRO_0000070078"
FT   TOPO_DOM        1..63
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..145
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..179
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..232
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..282
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..322
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        344..393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        137..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   393 AA;  44603 MW;  CF302DD364D8A2CC CRC64;
     MEITMGVMDE NATNTSTNYF PLLDPLGAQA ASFPFNFSYG DYDMPLDEDE DMTNSRTFFA
     AKIVIGMALV GIMLVCGIGN FIFIAALARY KKLRNLTNLL IANLAISDFL VAIVCCPFEM
     DYYVVRQLSW EHGHVLCASV NYLRTVSLYV STNALLAIAI DRYLAIVHPL RPRMKYQTAT
     GLIALVWVVS ILVAIPSAYF TTETVLVIVK SQEKIFCGQI WPVDQQIYYK SYFLFIFGIE
     FVGPVVTMTL CYARISRELW FKAVPGFQTE QIRKRLRCRR KTVLVLMCIL TAYVLCWAPF
     YGFAIVRDFF PTVFVKEKHY LTAFYVVECI AMSNSMINTV CFVTVKNNTI KYFKKIMLLH
     WKASYNGSKS SGDLDLKTTG VPATEEVDCI GLK