ID   PKR1_HUMAN              Reviewed;         393 AA.
AC   Q8TCW9; A5JUU2; Q53QT9; Q8NFJ7;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   02-SEP-2026, entry version 175.
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;
DE   AltName: Full=GPR73a;
GN   Name=PROKR1; Synonyms=GPR73, PKR1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12427552; DOI=10.1016/s0167-4781(02)00546-8;
RA   Soga T., Matsumoto S., Oda T., Saito T., Hiyama H., Takasaki J.,
RA   Kamohara M., Ohishi T., Matsushime H., Furuichi K.;
RT   "Molecular cloning and characterization of prokineticin receptors.";
RL   Biochim. Biophys. Acta 1579:173-179(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11886876; DOI=10.1074/jbc.m202139200;
RA   Lin D.C.-H., Bullock C.M., Ehlert F.J., Chen J.-L., Tian H., Zhou Q.-Y.;
RT   "Identification and molecular characterization of two closely related G
RT   protein-coupled receptors activated by prokineticins/endocrine gland
RT   vascular endothelial growth factor.";
RL   J. Biol. Chem. 277:19276-19280(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Martin A.L., Kaighin V.A., Aronstam R.S.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=18339712; DOI=10.1210/en.2007-1633;
RA   Evans J., Catalano R.D., Morgan K., Critchley H.O.D., Millar R.P.,
RA   Jabbour H.N.;
RT   "Prokineticin 1 signaling and gene regulation in early human pregnancy.";
RL   Endocrinology 149:2877-2887(2008).
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. {ECO:0000269|PubMed:18339712}.
CC   -!- INTERACTION:
CC       Q8TCW9; O60894: RAMP1; NbExp=2; IntAct=EBI-40234563, EBI-962893;
CC       Q8TCW9; O60895: RAMP2; NbExp=2; IntAct=EBI-40234563, EBI-9009040;
CC       Q8TCW9; O60896: RAMP3; NbExp=2; IntAct=EBI-40234563, EBI-720447;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Localizes to glandular epithelium, stroma and
CC       vascular endothelial cells of first trimester decidua (at protein
CC       level). Up-regulated in first trimester decidua when compared with non-
CC       pregnant endometrium. Expressed in the stomach, throughout the small
CC       intestine, colon, rectum, thyroid gland, pituitary gland, salivary
CC       gland, adrenal gland, testis, ovary, brain, spleen, prostate and
CC       pancreas. {ECO:0000269|PubMed:18339712}.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AY089976; AAM11892.1; -; mRNA.
DR   EMBL; AB084080; BAC24021.1; -; mRNA.
DR   EMBL; AF506287; AAM48127.1; -; mRNA.
DR   EMBL; AC105054; AAY24114.1; -; Genomic_DNA.
DR   EMBL; EF577399; ABQ52419.1; -; mRNA.
DR   EMBL; BC100960; AAI00961.1; -; mRNA.
DR   CCDS; CCDS1889.1; -.
DR   RefSeq; NP_620414.1; NM_138964.4.
DR   AlphaFoldDB; Q8TCW9; -.
DR   SMR; Q8TCW9; -.
DR   BioGRID; 116094; 25.
DR   FunCoup; Q8TCW9; 868.
DR   IntAct; Q8TCW9; 22.
DR   MINT; Q8TCW9; -.
DR   NDEx; IQUERY-CP-PROKR1; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000303775; -.
DR   BindingDB; Q8TCW9; -.
DR   ChEMBL; CHEMBL5649; -.
DR   GuidetoPHARMACOLOGY; 335; -.
DR   TCDB; 9.A.14.13.38; the g-protein-coupled receptor (gpcr) family.
DR   GlyCosmos; Q8TCW9; 3 sites, No reported glycans.
DR   GlyGen; Q8TCW9; 3 sites.
DR   iPTMnet; Q8TCW9; -.
DR   PhosphoSitePlus; Q8TCW9; -.
DR   BioMuta; PROKR1; -.
DR   DMDM; 33112428; -.
DR   MassIVE; Q8TCW9; -.
DR   PaxDb; 9606-ENSP00000303775; -.
DR   PeptideAtlas; Q8TCW9; -.
DR   ProteomicsDB; 74182; -.
DR   Antibodypedia; 30945; 138 antibodies from 21 providers.
DR   DNASU; 10887; -.
DR   Ensembl; ENST00000303786.5; ENSP00000303775.4; ENSG00000169618.7.
DR   GeneID; 10887; -.
DR   KEGG; hsa:10887; -.
DR   MANE-Select; ENST00000303786.5; ENSP00000303775.4; NM_138964.4; NP_620414.1.
DR   UCSC; uc010yqj.3; human.
DR   AGR; HGNC:4524; -.
DR   ClinPGx; PA28916; -.
DR   CTD; 10887; -.
DR   DisGeNET; 10887; -.
DR   GeneCards; PROKR1; -.
DR   HGNC; HGNC:4524; PROKR1.
DR   HPA; ENSG00000169618; Tissue enhanced (adipose tissue, adrenal gland, epididymis).
DR   MalaCards; PROKR1; -.
DR   MIM; 607122; gene.
DR   OpenTargets; ENSG00000169618; -.
DR   VEuPathDB; HostDB:ENSG00000169618; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000154544; -.
DR   HOGENOM; CLU_009579_6_0_1; -.
DR   InParanoid; Q8TCW9; -.
DR   OMA; HGHVMCA; -.
DR   OrthoDB; 10053194at2759; -.
DR   PAN-GO; Q8TCW9; 5 GO annotations based on evolutionary models.
DR   PhylomeDB; Q8TCW9; -.
DR   PathwayCommons; Q8TCW9; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   SignaLink; Q8TCW9; -.
DR   SIGNOR; Q8TCW9; -.
DR   Agora; ENSG00000169618; -.
DR   BioGRID-ORCS; 10887; 15 hits in 1137 CRISPR screens.
DR   GeneWiki; Prokineticin_receptor_1; -.
DR   GenomeRNAi; 10887; -.
DR   Pharos; Q8TCW9; Tchem.
DR   PRO; PR:Q8TCW9; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q8TCW9; protein.
DR   Bgee; ENSG00000169618; Expressed in primordial germ cell in gonad and 34 other cell types or tissues.
DR   GO; GO:0005886; C: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:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR   GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   CDD; cd15204; 7tmA_prokineticin-R; 1.
DR   FunFam; 1.20.1070.10:FF:000069; Prokineticin receptor 2; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000611; NPY_rcpt.
DR   PANTHER; PTHR24238; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24238:SF74; PROKINETICIN RECEPTOR 2; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01012; NRPEPTIDEYR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G protein-coupled receptor; Glycoprotein;
KW   Membrane; Proteomics identification; Receptor; Reference proteome;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..393
FT                   /note="Prokineticin receptor 1"
FT                   /id="PRO_0000070079"
FT   TOPO_DOM        1..62
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..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..146
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..180
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..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"
FT   VARIANT         40
FT                   /note="S -> G (in dbSNP:rs7570797)"
FT                   /id="VAR_024261"
FT   CONFLICT        255..256
FT                   /note="IS -> MT (in Ref. 3; AAM48127)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  44770 MW;  0D36461CA99CAEC1 CRC64;
     METTMGFMDD NATNTSTSFL SVLNPHGAHA TSFPFNFSYS DYDMPLDEDE DVTNSRTFFA
     AKIVIGMALV GIMLVCGIGN FIFIAALVRY KKLRNLTNLL IANLAISDFL VAIVCCPFEM
     DYYVVRQLSW EHGHVLCTSV NYLRTVSLYV STNALLAIAI DRYLAIVHPL RPRMKCQTAT
     GLIALVWTVS ILIAIPSAYF TTETVLVIVK SQEKIFCGQI WPVDQQLYYK SYFLFIFGIE
     FVGPVVTMTL CYARISRELW FKAVPGFQTE QIRKRLRCRR KTVLVLMCIL TAYVLCWAPF
     YGFTIVRDFF PTVFVKEKHY LTAFYIVECI AMSNSMINTL CFVTVKNDTV KYFKKIMLLH
     WKASYNGGKS SADLDLKTIG MPATEEVDCI RLK
//