PKR1_HUMAN
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 03-AUG-2022, entry version 157.
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 -!- 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_138964.3.
DR AlphaFoldDB; Q8TCW9; -.
DR SMR; Q8TCW9; -.
DR BioGRID; 116094; 24.
DR STRING; 9606.ENSP00000303775; -.
DR BindingDB; Q8TCW9; -.
DR ChEMBL; CHEMBL5649; -.
DR GuidetoPHARMACOLOGY; 335; -.
DR GlyGen; Q8TCW9; 3 sites.
DR iPTMnet; Q8TCW9; -.
DR PhosphoSitePlus; Q8TCW9; -.
DR BioMuta; PROKR1; -.
DR DMDM; 33112428; -.
DR MassIVE; Q8TCW9; -.
DR PaxDb; Q8TCW9; -.
DR PeptideAtlas; Q8TCW9; -.
DR PRIDE; Q8TCW9; -.
DR ProteomicsDB; 74182; -.
DR Antibodypedia; 30945; 106 antibodies from 20 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 CTD; 10887; -.
DR DisGeNET; 10887; -.
DR GeneCards; PROKR1; -.
DR HGNC; HGNC:4524; PROKR1.
DR HPA; ENSG00000169618; Tissue enhanced (adipose tissue, epididymis).
DR MIM; 607122; gene.
DR neXtProt; NX_Q8TCW9; -.
DR OpenTargets; ENSG00000169618; -.
DR OpenTargets; ENSG00000169621; -.
DR PharmGKB; PA28916; -.
DR VEuPathDB; HostDB:ENSG00000169618; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00390000010591; -.
DR GeneTree; ENSGT00940000154544; -.
DR HOGENOM; CLU_009579_6_0_1; -.
DR InParanoid; Q8TCW9; -.
DR OMA; IVMAMCY; -.
DR OrthoDB; 664455at2759; -.
DR PhylomeDB; Q8TCW9; -.
DR TreeFam; TF315303; -.
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 BioGRID-ORCS; 10887; 15 hits in 1060 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 ganglionic eminence and 33 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 1: Evidence at protein 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_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
