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DescriptionRecName: Full=Pyroglutamylated RFamide peptide receptor; AltName: Full=AQ27; AltName: Full=G-protein coupled receptor 103; AltName: Full=Orexigenic neuropeptide QRFP receptor; AltName: Full=SP9155;
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MyHits synonymsQRFPR_RAT , P83858 , 284A1589D38F93AD
match map segment
ipat:G_PROTEIN_RECEP_F1_1 ipfam:7tm_1 iprf:G_PROTEIN_RECEP_F1_2  
Legends: 1, N-linked (GlcNAc...) asparagine. {ECO:0000255}; 2, TOPO_DOM Extracellular. {ECO:0000255}; 3, TRANSMEM Helical; Name=1. {ECO:0000255}; 4, TOPO_DOM Cytoplasmic. {ECO:0000255}; 5, TRANSMEM Helical; Name=2. {ECO:0000255}; 6, TRANSMEM Helical; Name=3. {ECO:0000255}; 7, TRANSMEM Helical; Name=4. {ECO:0000255}; 8, TRANSMEM Helical; Name=5. {ECO:0000255}; 9, TRANSMEM Helical; Name=6. {ECO:0000255}; 10, TRANSMEM Helical; Name=7. {ECO:0000255}; 11, ipat:G_PROTEIN_RECEP_F1_1 [T].
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   10-MAY-2017, entry version 101.
DE   RecName: Full=Pyroglutamylated RFamide 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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   ligand for 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.,
RA   Ohno K., Ioka R.X., Murakami S., Dohmae N., Xie J., Suda T.,
RA   Motoike T., Ohuchi T., Yanagisawa M., Sakai J.;
RT   "A neuropeptide ligand of the G protein-coupled receptor GPR103
RT   regulates 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
CC       activity of this receptor is mediated by G proteins that modulate
CC       adenylate 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
CC       brain with high levels in the hypothalamus and moderate levels in
CC       the amygdala, basal forebrain, cortex, medulla oblongata, midbrain
CC       and 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   UniGene; Rn.162584; -.
DR   ProteinModelPortal; P83858; -.
DR   STRING; 10116.ENSRNOP00000035152; -.
DR   ChEMBL; CHEMBL1949484; -.
DR   GuidetoPHARMACOLOGY; 333; -.
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; KOG3656; Eukaryota.
DR   eggNOG; ENOG410XRW9; LUCA.
DR   GeneTree; ENSGT00760000118781; -.
DR   HOGENOM; HOG000136537; -.
DR   HOVERGEN; HBG067831; -.
DR   InParanoid; P83858; -.
DR   KO; K08378; -.
DR   OMA; HAIMNIT; -.
DR   OrthoDB; EOG091G0976; -.
DR   PhylomeDB; P83858; -.
DR   TreeFam; TF315303; -.
DR   PRO; PR:P83858; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0097730; C:non-motile cilium; IEA:Ensembl.
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   GO; GO:1901652; P:response to peptide; IBA:GO_Central.
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; Complete proteome; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    433       Pyroglutamylated RFamide peptide
FT                                receptor.
FT                                /FTId=PRO_0000070099.
FT   TOPO_DOM      1     46       Extracellular. {ECO:0000255}.
FT   TRANSMEM     47     67       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM     68     81       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     82    102       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    103    120       Extracellular. {ECO:0000255}.
FT   TRANSMEM    121    141       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    142    162       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    163    183       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    184    212       Extracellular. {ECO:0000255}.
FT   TRANSMEM    213    233       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    234    271       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    272    292       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    293    313       Extracellular. {ECO:0000255}.
FT   TRANSMEM    314    334       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    335    433       Cytoplasmic. {ECO:0000255}.
FT   CARBOHYD      5      5       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     19     19       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       131    147       ipat:G_PROTEIN_RECEP_F1_1 [T]
FT   MYHIT        62    332       ipfam:7tm_1 [T]
FT   MYHIT        62    332       iprf:G_PROTEIN_RECEP_F1_2 [T]
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
//