ID   NPBW1_BOVIN             Reviewed;         331 AA.
AC   Q8MJV3;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Neuropeptides B/W receptor type 1;
DE   AltName: Full=G-protein coupled receptor 7;
GN   Name=NPBWR1; Synonyms=GPR7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12118011; DOI=10.1074/jbc.m205883200;
RA   Fujii R., Yoshida H., Fukusumi S., Habata Y., Hosoya M., Kawamata Y.,
RA   Yano T., Hinuma S., Kitada C., Asami T., Mori M., Fujisawa Y., Fujino M.;
RT   "Identification of a neuropeptide modified with bromine as an endogenous
RT   ligand for GPR7.";
RL   J. Biol. Chem. 277:34010-34016(2002).
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}.
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DR   EMBL; AB085946; BAC07179.1; -; mRNA.
DR   AlphaFoldDB; Q8MJV3; -.
DR   SMR; Q8MJV3; -.
DR   STRING; 9913.ENSBTAP00000021510; -.
DR   PaxDb; Q8MJV3; -.
DR   PRIDE; Q8MJV3; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q8MJV3; -.
DR   Proteomes; UP000009136; Unplaced.
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:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
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..331
FT                   /note="Neuropeptides B/W receptor type 1"
FT                   /id="PRO_0000069517"
FT   TOPO_DOM        1..43
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..66
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..75
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..100
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..115
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..135
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..160
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..180
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..227
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        228..251
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..276
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        277..286
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..301
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..331
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        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        112..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   331 AA;  36268 MW;  A474CA041EDF3B57 CRC64;
     MHNASYWGPE RANTSCPAPA PTLGCPNASG PAPPLPPPLA VAVPVVYAVI CAVGLAGNSA
     VLFVLLRAPR RKTVTNLFIL NLAVADELFT LVPPVNIADF LLRRWPFGEL LCKLVVAVDQ
     YNTFSSLYFL TVMSADRYLV VLATAESRRV AGRTYGAARA VSLAVWGVAT LVVLPFAVFA
     RLDEEQGRRQ CVLVFPQPEA LWWRASRLYT LVLGFAIPVS TICVLYTSLL CRLRAIRLDS
     HAKALDRAKK RVTVLVVAIL AVCLLVWTPY HLSTVVALTT DLPQTPLVIA VSYFITSLSY
     ANSCLNPFLY AFLDDSFRRS LRQLLACRTT S