ID QRFPR_MOUSE Reviewed; 433 AA.
AC P83861;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 27-MAR-2024, entry version 146.
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 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 {ECO:0000312|EMBL:BAC98940.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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].
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 TISSUE SPECIFICITY.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q96P65}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed widely in the brain with high levels in
CC the cortex and hypothalamus, and moderate levels in the brain stem,
CC caudate nucleus, midbrain hippocampus, thalamus, trigeminal ganglia and
CC spinal cord. Particularly strong expression detected in the mitral cell
CC layer of the olfactory bulb, accessory olfactory bulb, island of
CC Calleja and nucleus of the solitary tract. In peripheral tissues,
CC expressed at moderate levels in the eye, liver, kidney, pituitary
CC gland, testis and thymus. {ECO:0000269|PubMed:12714592,
CC ECO:0000269|PubMed:16648250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB109631; BAC98940.1; -; mRNA.
DR CCDS; CCDS17311.1; -.
DR RefSeq; NP_937835.1; NM_198192.2.
DR AlphaFoldDB; P83861; -.
DR SMR; P83861; -.
DR STRING; 10090.ENSMUSP00000088768; -.
DR GuidetoPHARMACOLOGY; 333; -.
DR GlyCosmos; P83861; 2 sites, No reported glycans.
DR GlyGen; P83861; 2 sites.
DR PhosphoSitePlus; P83861; -.
DR PaxDb; 10090-ENSMUSP00000088768; -.
DR Antibodypedia; 2965; 306 antibodies from 31 providers.
DR Ensembl; ENSMUST00000091227.9; ENSMUSP00000088768.6; ENSMUSG00000058400.14.
DR GeneID; 229214; -.
DR KEGG; mmu:229214; -.
DR UCSC; uc008ozh.1; mouse.
DR AGR; MGI:2677633; -.
DR CTD; 84109; -.
DR MGI; MGI:2677633; Qrfpr.
DR VEuPathDB; HostDB:ENSMUSG00000058400; -.
DR eggNOG; ENOG502QW2F; Eukaryota.
DR GeneTree; ENSGT01070000253744; -.
DR InParanoid; P83861; -.
DR OMA; IHMMIEY; -.
DR OrthoDB; 2877170at2759; -.
DR PhylomeDB; P83861; -.
DR TreeFam; TF315303; -.
DR Reactome; R-MMU-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 229214; 0 hits in 78 CRISPR screens.
DR PRO; PR:P83861; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P83861; Protein.
DR Bgee; ENSMUSG00000058400; Expressed in ventromedial nucleus of hypothalamus and 34 other cell types or tissues.
DR ExpressionAtlas; P83861; baseline and differential.
DR Genevisible; P83861; MM.
DR GO; GO:0097730; C:non-motile cilium; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR CDD; cd15205; 7tmA_QRFPR; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000611; NPY_rcpt.
DR PANTHER; PTHR24241; NEUROPEPTIDE RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24241:SF155; PYROGLUTAMYLATED RF-AMIDE PEPTIDE RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01012; NRPEPTIDEYR.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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; 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_0000070098"
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 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; 49245 MW; 014D5AA21BD73055 CRC64;
MQALNITAEQ FSRLLSAHNL TREQFIHRYG LRPLVYTPEL PARAKLAFAL AGALIFALAL
FGNSLVIYVV TRSKAMRTVT NIFICSLALS DLLIAFFCIP VTMLQNISDK WLGGAFICKM
VPFVQSTAVV TEILTMTCIA VERHQGLIHP FKMKWQYTTR RAFTILGVVW LAAIIVGSPM
WHVQRLEIKY DFLYEKEHVC CLEEWASPMH QRIYTTFILV ILFLLPLVVM LVLYSKIGYE
LWIKKRVGDS SALQTIHGKE MSKIARKKKR AVVMMVTVVA LFAACWAPFH VVHMMVEYSN
FEKEYDDVTI KMVFAVAQTI GFFNSICNPF VYAFMNENFK KNFLSAVCYC IVRETFSPGQ
KPGNSGISMM QKRAKLSRSQ RPVAEAKGDL FSDANVDVKL CEQPGEKRQL KRQLAFFSSE
LSENSTFGSG HEL
//
