PRLHR_RAT
ID PRLHR_RAT Reviewed; 370 AA.
AC Q64121;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=UHR-1;
GN Name=Prlhr; Synonyms=Gpr10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=7733930; DOI=10.1006/bbrc.1995.1543;
RA Welch S.K., O'Hara B.F., Kilduff T.S., Heller H.C.;
RT "Sequence and tissue distribution of a candidate G-coupled receptor cloned
RT from rat hypothalamus.";
RL Biochem. Biophys. Res. Commun. 209:606-613(1995).
RN [2]
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).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in pituitary,
CC cerebellum, and hypothalamus. {ECO:0000269|PubMed:10498338}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; S77867; AAB34129.1; -; mRNA.
DR RefSeq; NP_631932.3; NM_139193.3.
DR AlphaFoldDB; Q64121; -.
DR SMR; Q64121; -.
DR STRING; 10116.ENSRNOP00000013170; -.
DR GlyGen; Q64121; 2 sites.
DR PhosphoSitePlus; Q64121; -.
DR PaxDb; Q64121; -.
DR GeneID; 246075; -.
DR KEGG; rno:246075; -.
DR CTD; 2834; -.
DR RGD; 71037; Prlhr.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q64121; -.
DR OrthoDB; 1072979at2759; -.
DR PhylomeDB; Q64121; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR PRO; PR:Q64121; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IMP:RGD.
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:0017046; F:peptide hormone binding; IMP:RGD.
DR GO; GO:0007631; P:feeding behavior; IMP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0042445; P:hormone metabolic process; ISO:RGD.
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 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..370
FT /note="Prolactin-releasing peptide receptor"
FT /id="PRO_0000069526"
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..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..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..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..370
FT /note="Required for interaction with GRIP1, GRIP2 and
FT PICK1"
FT /evidence="ECO:0000250"
FT COMPBIAS 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 370 AA; 41161 MW; 8EE5E689D127CB2C CRC64;
MTSLPPGTTG DPDLFSGPSP AGSTPANQSA EASESNVSAT VPRAAAVTPF QSLQLVHQLK
GLIVMLYSIV VVVGLVGNCL LVLVIARVRR LHNVTNFLIG NLALSDVLMC AACVPLTLAY
AFEPRGWVFG GGLCHLVFFL QPVTVYVSVF TLTTIAVDRY VVLVHPLRRR ISLKLSAYAV
LGIWALSAVL ALPAAVHTYH VELKPHDVRL CEEFWGSQER QRQIYAWGLL LGTYLLPLLA
ILLSYVRVSV KLRNRVVPGS VTQSQADWDR ARRRRTFCLL VVVVVVFALC WLPLHIFNLL
RDLDPRAIDP YAFGLVQLLC HWLAMSSACY NPFIYAWLHD SFREELRKML LSWPRKIVPH
GQNMTVSVVI
