NPBW1_RAT
ID NPBW1_RAT Reviewed; 329 AA.
AC Q56UD9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Neuropeptides B/W receptor type 1;
DE AltName: Full=G-protein coupled receptor 7;
GN Name=Npbwr1; Synonyms=Gpr7;
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 STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Nothacker H.-P., Wang Z., Civelli O.;
RT "Pharmacological characterization of rat GPR7.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Interacts specifically with a number of opioid ligands.
CC Receptor for neuropeptides B and W, which may be involved in
CC neuroendocrine system regulation, food intake and the organization of
CC other signals (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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; AY577901; AAT72915.1; -; mRNA.
DR RefSeq; NP_001014784.1; NM_001014784.1.
DR AlphaFoldDB; Q56UD9; -.
DR SMR; Q56UD9; -.
DR STRING; 10116.ENSRNOP00000010032; -.
DR GuidetoPHARMACOLOGY; 303; -.
DR GlyGen; Q56UD9; 3 sites.
DR PhosphoSitePlus; Q56UD9; -.
DR PaxDb; Q56UD9; -.
DR Ensembl; ENSRNOT00000010032; ENSRNOP00000010032; ENSRNOG00000007640.
DR GeneID; 297795; -.
DR KEGG; rno:297795; -.
DR UCSC; RGD:1305917; rat.
DR CTD; 2831; -.
DR RGD; 1305917; Npbwr1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000161936; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; Q56UD9; -.
DR OMA; PESVWWK; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; Q56UD9; -.
DR TreeFam; TF315737; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q56UD9; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IEA:InterPro.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0019222; P:regulation of metabolic process; ISO:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR009150; Neuropept_B/W_rcpt.
DR InterPro; IPR027348; NPBW1.
DR PANTHER; PTHR24229:SF47; PTHR24229:SF47; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01855; NRPEPTIDEWR.
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..329
FT /note="Neuropeptides B/W receptor type 1"
FT /id="PRO_0000069520"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..275
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..300
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 329 AA; 36306 MW; D93B017240F570D7 CRC64;
MHNLSLFEPG RGNVSCGGPF LGCPNESNPA PLPLPQPLAV AVPVVYGVIC AVGLAGNSAV
LYVLLRTPRM KTVTNVFILN LAIADELFTL VLPINIADFL LRRWPFGEVM CKLIVAVDQY
NTFSSLYFLA VMSADRYLVV LATAESRRVS GRTYGAARAV SLAVWALVTL VVLPFAVFAR
LDEEQGRRQC VLVFPQPEAF WWRASRLYTL VLGFAIPVST ICALYITLLC RLRAIQLDSH
AKALDRAKKR VTLLVVAILA VCLLCWTPYH LSTIVALTTD LPQTPLVIGI SYFITSLSYA
NSCLNPFLYA FLDDSFRRSL RQLVSCRTA
