ID   PKR1_MOUSE              Reviewed;         393 AA.
AC   Q9JKL1; Q3U0M4; Q6PD11;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Prokineticin receptor 1;
DE            Short=PK-R1;
DE   AltName: Full=G-protein coupled receptor 73;
GN   Name=Prokr1; Synonyms=Gpr73, Pkr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=10760605; DOI=10.1016/s0167-4781(00)00023-3;
RA   Parker R., Liu M., Eyre H.J., Copeland N.G., Gilbert D.J., Crawford J.,
RA   Sutherland G.R., Jenkins N.A., Herzog H.;
RT   "Y-receptor-like genes GPR72 and GPR73: molecular cloning, genomic
RT   organisation and assignment to human chromosome 11q21.1 and 2p14 and mouse
RT   chromosome 9 and 6.";
RL   Biochim. Biophys. Acta 1491:369-375(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=12024206; DOI=10.1038/417405a;
RA   Cheng M.Y., Bullock C.M., Li C., Lee A.G., Bermak J.C., Belluzzi J.,
RA   Weaver D.R., Leslie F.M., Zhou Q.-Y.;
RT   "Prokineticin 2 transmits the behavioural circadian rhythm of the
RT   suprachiasmatic nucleus.";
RL   Nature 417:405-410(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Forelimb, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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).
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   -!- TISSUE SPECIFICITY: Expressed at high levels in the heart, skeletal
CC       muscle and pancreas. Expressed at lower levels in the brain, lung,
CC       liver and kidney.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF236082; AAF43706.1; -; mRNA.
DR   EMBL; AF487278; AAM49570.1; -; mRNA.
DR   EMBL; AK134279; BAE22080.1; -; mRNA.
DR   EMBL; AK156734; BAE33828.1; -; mRNA.
DR   EMBL; CH466523; EDK99210.1; -; Genomic_DNA.
DR   EMBL; BC059003; AAH59003.1; -; mRNA.
DR   CCDS; CCDS20323.1; -.
DR   RefSeq; NP_067356.2; NM_021381.3.
DR   RefSeq; XP_006506494.1; XM_006506431.3.
DR   RefSeq; XP_006506495.1; XM_006506432.3.
DR   AlphaFoldDB; Q9JKL1; -.
DR   SMR; Q9JKL1; -.
DR   STRING; 10090.ENSMUSP00000144999; -.
DR   ChEMBL; CHEMBL1949486; -.
DR   GlyCosmos; Q9JKL1; 1 site, No reported glycans.
DR   GlyGen; Q9JKL1; 1 site.
DR   iPTMnet; Q9JKL1; -.
DR   PhosphoSitePlus; Q9JKL1; -.
DR   PaxDb; 10090-ENSMUSP00000059034; -.
DR   DNASU; 58182; -.
DR   Ensembl; ENSMUST00000050887.9; ENSMUSP00000059034.8; ENSMUSG00000049409.10.
DR   Ensembl; ENSMUST00000204682.3; ENSMUSP00000144999.2; ENSMUSG00000049409.10.
DR   GeneID; 58182; -.
DR   KEGG; mmu:58182; -.
DR   UCSC; uc009cto.1; mouse.
DR   AGR; MGI:1929676; -.
DR   CTD; 10887; -.
DR   MGI; MGI:1929676; Prokr1.
DR   VEuPathDB; HostDB:ENSMUSG00000049409; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000164891; -.
DR   HOGENOM; CLU_009579_6_0_1; -.
DR   InParanoid; Q9JKL1; -.
DR   OMA; QTAYWLI; -.
DR   OrthoDB; 4111530at2759; -.
DR   PhylomeDB; Q9JKL1; -.
DR   TreeFam; TF315303; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   BioGRID-ORCS; 58182; 5 hits in 77 CRISPR screens.
DR   PRO; PR:Q9JKL1; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9JKL1; Protein.
DR   Bgee; ENSMUSG00000049409; Expressed in lumbar dorsal root ganglion and 97 other cell types or tissues.
DR   ExpressionAtlas; Q9JKL1; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR   GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR   GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
DR   GO; GO:0060976; P:coronary vasculature development; TAS:DFLAT.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   CDD; cd15204; 7tmA_prokineticin-R; 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:SF71; 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.
DR   Genevisible; Q9JKL1; MM.
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_0000070080"
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..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   DISULFID        137..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        275..276
FT                   /note="RL -> TV (in Ref. 1; AAF43706 and 2; AAM49570)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  44597 MW;  D0F5E79606D74283 CRC64;
     METTVGALGE NTTDTFTDFF SALDGHEAQT GSLPFTFSYG DYDMPLDEEE DVTNSRTFFA
     AKIVIGMALV GIMLVCGIGN FIFITALARY KKLRNLTNLL IANLAISDFL VAIVCCPFEM
     DYYVVRQLSW EHGHVLCASV NYLRTVSLYV STNALLAIAI DRYLAIVHPL RPRMKCQTAA
     GLIFLVWSVS ILIAIPAAYF TTETVLVIVE RQEKIFCGQI WPVDQQFYYR SYFLLVFGLE
     FVGPVVAMTL CYARVSRELW FKAVPGFQTE QIRRRLRCRR RTVLGLVCVL SAYVLCWAPF
     YGFTIVRDFF PSVFVKEKHY LTAFYVVECI AMSNSMINTL CFVTVRNNTS KYLKRILRLQ
     WRASPSGSKA SADLDLRTTG IPATEEVDCI RLK
//