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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}.
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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
 
 
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