PRLHR_HUMAN
ID PRLHR_HUMAN Reviewed; 370 AA.
AC P49683; O75194; Q502U8; Q5VXR9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Prolactin-releasing peptide receptor;
DE Short=PrRP receptor;
DE Short=PrRPR;
DE AltName: Full=G-protein coupled receptor 10;
DE AltName: Full=hGR3;
GN Name=PRLHR; Synonyms=GPR10, GR3;
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 [GENOMIC DNA], AND VARIANT VAL-283.
RX PubMed=8666380; DOI=10.1006/geno.1995.9996;
RA Marchese A., Heiber M., Nguyen T., Heng H.H.Q., Saldivia V.R., Cheng R.,
RA Murphy P.M., Tsui L.-C., Shi X., Gregor P., George S.R., O'Dowd B.F.,
RA Docherty J.M.;
RT "Cloning and chromosomal mapping of three novel genes, GPR9, GPR10, and
RT GPR14, encoding receptors related to interleukin 8, neuropeptide Y, and
RT somatostatin receptors.";
RL Genomics 29:335-344(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-283.
RX PubMed=9607765; DOI=10.1038/30515;
RA Hinuma S., Habata Y., Fujii R., Kawamata Y., Hosoya M., Fukusumi S.,
RA Kitada C., Masuo Y., Asano T., Matsumoto H., Sekiguchi M., Kurokawa T.,
RA Nishimura O., Onda H., Fujino M.;
RT "A prolactin-releasing peptide in the brain.";
RL Nature 393:272-276(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION, AND
RP VARIANT VAL-283.
RX PubMed=11923475; DOI=10.1210/mend.16.4.0819;
RA Ozawa A., Yamada M., Satoh T., Monden T., Hashimoto K., Kohga H.,
RA Hashiba Y., Sasaki T., Mori M.;
RT "Transcriptional regulation of the human PRL-releasing peptide (PrRP)
RT receptor gene by a dopamine 2 receptor agonist: cloning and
RT characterization of the human PrRP receptor gene and its promoter region.";
RL Mol. Endocrinol. 16:785-798(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-283.
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=10498338; DOI=10.1016/s0167-0115(99)00028-2;
RA Fujii R., Fukusumi S., Hosoya M., Kawamata Y., Habata Y., Hinuma S.,
RA Sekiguchi M., Kitada C., Kurokawa T., Nishimura O., Onda H., Sumino Y.,
RA Fujino M.;
RT "Tissue distribution of prolactin-releasing peptide (PrRP) and its
RT receptor.";
RL Regul. Pept. 83:1-10(1999).
RN [7]
RP INTERACTION WITH GRIP1; GRIP2 AND PICK1, AND MUTAGENESIS OF THR-365;
RP VAL-366; SER-367; VAL-368; VAL-369 AND ILE-370.
RX PubMed=11641419; DOI=10.1124/mol.60.5.916;
RA Lin S.H.S., Arai A.C., Wang Z., Nothacker H.-P., Civelli O.;
RT "The carboxyl terminus of the prolactin-releasing peptide receptor
RT interacts with PDZ domain proteins involved in alpha-amino-3-hydroxy-5-
RT methylisoxazole-4-propionic acid receptor clustering.";
RL Mol. Pharmacol. 60:916-923(2001).
CC -!- FUNCTION: Receptor for prolactin-releasing peptide (PrRP). Implicated
CC in lactation, regulation of food intake and pain-signal processing.
CC -!- SUBUNIT: Interacts through its C-terminal region with the PDZ domain-
CC containing proteins GRIP1, GRIP2 and PICK1. Interacts with PDZ domains
CC 4 and 5 of GRIP1 and with the PDZ domain of PICK1.
CC {ECO:0000269|PubMed:11641419}.
CC -!- INTERACTION:
CC P49683; Q9Y3R0: GRIP1; NbExp=2; IntAct=EBI-8009236, EBI-5349621;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Only detected in the pituitary gland and in all
CC cell types of pituitary adenomas. {ECO:0000269|PubMed:10498338,
CC ECO:0000269|PubMed:11923475}.
CC -!- INDUCTION: Repressed by bromocriptine, a dopamine agonist.
CC {ECO:0000269|PubMed:11923475}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50504.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U32672; AAC50504.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AB015745; BAA31159.1; -; mRNA.
DR EMBL; AB048946; BAB83030.1; -; Genomic_DNA.
DR EMBL; AL356865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC095539; AAH95539.1; -; mRNA.
DR EMBL; BC101490; AAI01491.1; -; mRNA.
DR EMBL; BC101492; AAI01493.1; -; mRNA.
DR CCDS; CCDS7606.1; -.
DR RefSeq; NP_004239.1; NM_004248.2.
DR AlphaFoldDB; P49683; -.
DR SMR; P49683; -.
DR BioGRID; 109095; 3.
DR IntAct; P49683; 3.
DR MINT; P49683; -.
DR STRING; 9606.ENSP00000239032; -.
DR BindingDB; P49683; -.
DR ChEMBL; CHEMBL1681611; -.
DR GuidetoPHARMACOLOGY; 337; -.
DR GlyGen; P49683; 2 sites.
DR iPTMnet; P49683; -.
DR PhosphoSitePlus; P49683; -.
DR BioMuta; PRLHR; -.
DR DMDM; 311033415; -.
DR PaxDb; P49683; -.
DR PeptideAtlas; P49683; -.
DR PRIDE; P49683; -.
DR Antibodypedia; 18777; 304 antibodies from 29 providers.
DR DNASU; 2834; -.
DR Ensembl; ENST00000239032.4; ENSP00000239032.2; ENSG00000119973.6.
DR Ensembl; ENST00000636925.1; ENSP00000490073.1; ENSG00000119973.6.
DR GeneID; 2834; -.
DR KEGG; hsa:2834; -.
DR MANE-Select; ENST00000239032.4; ENSP00000239032.2; NM_004248.3; NP_004239.2.
DR UCSC; uc001ldp.2; human.
DR CTD; 2834; -.
DR DisGeNET; 2834; -.
DR GeneCards; PRLHR; -.
DR HGNC; HGNC:4464; PRLHR.
DR HPA; ENSG00000119973; Tissue enhanced (adrenal gland, brain, pituitary gland).
DR MIM; 600895; gene.
DR neXtProt; NX_P49683; -.
DR OpenTargets; ENSG00000119973; -.
DR PharmGKB; PA28847; -.
DR VEuPathDB; HostDB:ENSG00000119973; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000162008; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; P49683; -.
DR OMA; LAWPRKI; -.
DR OrthoDB; 1072979at2759; -.
DR PhylomeDB; P49683; -.
DR TreeFam; TF315303; -.
DR PathwayCommons; P49683; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR SignaLink; P49683; -.
DR SIGNOR; P49683; -.
DR BioGRID-ORCS; 2834; 10 hits in 1057 CRISPR screens.
DR GeneWiki; Prolactin-releasing_peptide_receptor; -.
DR GenomeRNAi; 2834; -.
DR Pharos; P49683; Tchem.
DR PRO; PR:P49683; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P49683; protein.
DR Bgee; ENSG00000119973; Expressed in pituitary gland and 42 other tissues.
DR Genevisible; P49683; HS.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IBA:GO_Central.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0007631; P:feeding behavior; IEA:Ensembl.
DR GO; GO:0007565; P:female pregnancy; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001402; Prolrel_pep_rcpt.
DR PANTHER; PTHR24235:SF11; PTHR24235:SF11; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01018; PRPRECEPTOR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 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; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..370
FT /note="Prolactin-releasing peptide receptor"
FT /id="PRO_0000069524"
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..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 365..370
FT /note="Required for interaction with GRIP1, GRIP2 and
FT PICK1"
FT /evidence="ECO:0000269|PubMed:11641419"
FT CARBOHYD 27
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 134..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 283
FT /note="I -> V (in dbSNP:rs1613448)"
FT /evidence="ECO:0000269|PubMed:11923475,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8666380,
FT ECO:0000269|PubMed:9607765"
FT /id="VAR_023948"
FT VARIANT 302
FT /note="D -> G (in dbSNP:rs8192523)"
FT /id="VAR_029746"
FT MUTAGEN 365..370
FT /note="Missing: Abolishes binding to GRIP1 and PICK1."
FT MUTAGEN 365
FT /note="T->A: No effect on binding to GRIP1."
FT /evidence="ECO:0000269|PubMed:11641419"
FT MUTAGEN 366
FT /note="V->A: No effect on binding to GRIP1."
FT /evidence="ECO:0000269|PubMed:11641419"
FT MUTAGEN 367
FT /note="S->A: Abolishes binding to GRIP1."
FT /evidence="ECO:0000269|PubMed:11641419"
FT MUTAGEN 368
FT /note="V->A: Abolishes binding to GRIP1."
FT /evidence="ECO:0000269|PubMed:11641419"
FT MUTAGEN 369
FT /note="V->A: No effect on binding to GRIP1."
FT /evidence="ECO:0000269|PubMed:11641419"
FT MUTAGEN 370
FT /note="I->A: Abolishes binding to GRIP1."
FT /evidence="ECO:0000269|PubMed:11641419"
FT CONFLICT 89
FT /note="R -> P (in Ref. 1; AAC50504)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="A -> P (in Ref. 1; AAC50504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 41121 MW; 47F71490A080C81F CRC64;
MASSTTRGPR VSDLFSGLPP AVTTPANQSA EASAGNGSVA GADAPAVTPF QSLQLVHQLK
GLIVLLYSVV VVVGLVGNCL LVLVIARVRR LHNVTNFLIG NLALSDVLMC TACVPLTLAY
AFEPRGWVFG GGLCHLVFFL QPVTVYVSVF TLTTIAVDRY VVLVHPLRRR ISLRLSAYAV
LAIWALSAVL ALPAAVHTYH VELKPHDVRL CEEFWGSQER QRQLYAWGLL LVTYLLPLLV
ILLSYVRVSV KLRNRVVPGC VTQSQADWDR ARRRRTFCLL VVIVVVFAVC WLPLHVFNLL
RDLDPHAIDP YAFGLVQLLC HWLAMSSACY NPFIYAWLHD SFREELRKLL VAWPRKIAPH
GQNMTVSVVI
