PKR1_MOUSE
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 03-AUG-2022, entry version 144.
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.ENSMUSP00000059034; -.
DR ChEMBL; CHEMBL1949486; -.
DR GlyGen; Q9JKL1; 1 site.
DR iPTMnet; Q9JKL1; -.
DR PhosphoSitePlus; Q9JKL1; -.
DR PaxDb; Q9JKL1; -.
DR PRIDE; Q9JKL1; -.
DR DNASU; 58182; -.
DR Ensembl; ENSMUST00000050887; ENSMUSP00000059034; ENSMUSG00000049409.
DR Ensembl; ENSMUST00000204682; ENSMUSP00000144999; ENSMUSG00000049409.
DR GeneID; 58182; -.
DR KEGG; mmu:58182; -.
DR UCSC; uc009cto.1; mouse.
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; AYMASEM; -.
DR OrthoDB; 664455at2759; -.
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; 4 hits in 72 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 96 other tissues.
DR ExpressionAtlas; Q9JKL1; baseline and differential.
DR Genevisible; Q9JKL1; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; TAS:MGI.
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 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_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
