QRFPR_RAT
ID QRFPR_RAT Reviewed; 433 AA.
AC P83858;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Pyroglutamylated RF-amide peptide receptor;
DE AltName: Full=AQ27;
DE AltName: Full=G-protein coupled receptor 103;
DE AltName: Full=Orexigenic neuropeptide QRFP receptor;
DE AltName: Full=SP9155;
GN Name=Qrfpr; Synonyms=Gpr103;
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 {ECO:0000312|EMBL:BAC98939.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12714592; DOI=10.1074/jbc.m302945200;
RA Jiang Y., Luo L., Gustafson E.L., Yadav D., Laverty M., Murgolo N.,
RA Vassileva G., Zeng M., Laz T.M., Behan J., Qiu P., Wang L., Wang S.,
RA Bayne M., Greene J., Monsma F.J. Jr., Zhang F.L.;
RT "Identification and characterization of a novel RF-amide peptide ligand for
RT orphan G-protein-coupled receptor SP9155.";
RL J. Biol. Chem. 278:27652-27657(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:12960173};
RX PubMed=12960173; DOI=10.1074/jbc.m305270200;
RA Fukusumi S., Yoshida H., Fujii R., Maruyama M., Komatsu H., Habata Y.,
RA Shintani Y., Hinuma S., Fujino M.;
RT "A new peptidic ligand and its receptor regulating adrenal function in
RT rats.";
RL J. Biol. Chem. 278:46387-46395(2003).
RN [3]
RP FUNCTION.
RX PubMed=16648250; DOI=10.1073/pnas.0602371103;
RA Takayasu S., Sakurai T., Iwasaki S., Teranishi H., Yamanaka A.,
RA Williams S.C., Iguchi H., Kawasawa Y.I., Ikeda Y., Sakakibara I., Ohno K.,
RA Ioka R.X., Murakami S., Dohmae N., Xie J., Suda T., Motoike T., Ohuchi T.,
RA Yanagisawa M., Sakai J.;
RT "A neuropeptide ligand of the G protein-coupled receptor GPR103 regulates
RT feeding, behavioral arousal, and blood pressure in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7438-7443(2006).
CC -!- FUNCTION: Receptor for the orexigenic neuropeptide QRFP. The activity
CC of this receptor is mediated by G proteins that modulate adenylate
CC cyclase activity and intracellular calcium levels.
CC {ECO:0000269|PubMed:16648250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in the adrenal gland and at
CC moderate levels in the eye and testis. Expressed widely in the brain
CC with high levels in the hypothalamus and moderate levels in the
CC amygdala, basal forebrain, cortex, medulla oblongata, midbrain and
CC thalamus. {ECO:0000269|PubMed:12960173}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB109630; BAC98939.1; -; mRNA.
DR RefSeq; NP_937842.1; NM_198199.1.
DR AlphaFoldDB; P83858; -.
DR SMR; P83858; -.
DR STRING; 10116.ENSRNOP00000035152; -.
DR ChEMBL; CHEMBL1949484; -.
DR GuidetoPHARMACOLOGY; 333; -.
DR GlyGen; P83858; 2 sites.
DR PhosphoSitePlus; P83858; -.
DR PaxDb; P83858; -.
DR PRIDE; P83858; -.
DR Ensembl; ENSRNOT00000039615; ENSRNOP00000035152; ENSRNOG00000014414.
DR GeneID; 310327; -.
DR KEGG; rno:310327; -.
DR UCSC; RGD:728380; rat.
DR CTD; 84109; -.
DR RGD; 728380; Qrfpr.
DR eggNOG; ENOG502QW2F; Eukaryota.
DR GeneTree; ENSGT01050000244933; -.
DR HOGENOM; CLU_009579_6_0_1; -.
DR InParanoid; P83858; -.
DR OMA; KRAIVMM; -.
DR OrthoDB; 1485786at2759; -.
DR PhylomeDB; P83858; -.
DR TreeFam; TF315303; -.
DR Reactome; R-RNO-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P83858; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000014414; Expressed in frontal cortex and 6 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
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; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..433
FT /note="Pyroglutamylated RF-amide peptide receptor"
FT /id="PRO_0000070099"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 356..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 433 AA; 49311 MW; 284A1589D38F93AD CRC64;
MQALNITAEQ FSRLLSAHNL TREQFIHRYG LRPLVYTPEL PARAKVAFAL AGALIFALAL
FGNSLVIYVV TRSKAMRTVT NIFICSLALS DLLIAFFCIP VTMLQNISDK WLGGAFICKM
VPFVQSTAVV TEILTMTCIA VERHQGLVHP FKMKWQYTTR RAFTILGVVW LAAIIVGSPM
WHVQRLEIKY DFLYEKEHIC CLEEWASPVH QRIYSTFILV ILFLLPLVVM LVLYSKIGYE
LWIKKRVGDS SALQTIHGKE MSKIARKKKR AVIMMVTVVA LFAACWAPFH VVHMMVEYSN
FEKEYDDVTI KMVFAVAQTI GFFNSICNPF VYAFMNENFK KNFLSAVCYC IVKESSSPAR
KPGNSGISMM QKRAKLSRPQ RPVEETKGDT FSDASIDVKL CEQPREKRQL KRQLAFFSSE
LSENSTFGSG HEL