ID   BRS4_BOMOR              Reviewed;         392 AA.
AC   P47751;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=[Phe13]-bombesin receptor;
DE   AltName: Full=Bombesin receptor subtype-4;
DE            Short=BRS-4;
GN   Name=BB4;
OS   Bombina orientalis (Oriental fire-bellied toad).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Bombinatoridae; Bombina.
OX   NCBI_TaxID=8346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7597102; DOI=10.1073/pnas.92.13.6205;
RA   Nagalla S.R., Barry B.J., Creswick K.C., Eden P., Taylor J.T.,
RA   Spindel E.R.;
RT   "Cloning of a receptor for amphibian [Phe13]bombesin distinct from the
RT   receptor for gastrin-releasing peptide: identification of a fourth bombesin
RT   receptor subtype (BB4).";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:6205-6209(1995).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Spindel E.R.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The relative rank potency of bombesin-like peptides for this
CC       receptor is [Phe13]bombesin > [Leu13]bombesin > GRP > neuromedin-B.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed only in brain, primarily in cortex and
CC       forebrain and at low levels in the midbrain.
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; L39358; AAA91102.1; -; mRNA.
DR   AlphaFoldDB; P47751; -.
DR   SMR; P47751; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IEA:InterPro.
DR   InterPro; IPR001556; Bombsn_rcpt-like.
DR   InterPro; IPR000401; BRS4.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00638; BOMBESIN4R.
DR   PRINTS; PR00358; BOMBESINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..392
FT                   /note="[Phe13]-bombesin receptor"
FT                   /id="PRO_0000069200"
FT   TOPO_DOM        1..40
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..62
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..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..142
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..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..219
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..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..312
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..332
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..392
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           346
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        9
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        119..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   392 AA;  43462 MW;  497C620209F1DBEB CRC64;
     MPEGFQSLNQ TLPSAISSIA HLESLNDSFI LGAKQSEDVS PGLEILALIS VTYAVIISVG
     ILGNTILIKV FFKIKSMQTV PNIFITSLAF GDLLLLLTCV PVDASRYIVD TWMFGRAGCK
     IISFIQLTSV GVSVFTLTVL SADRYRAIVK PLQLQTSDAV LKTCGKAVCV WIISMLLAAP
     EAVFSDLYEF GSSEKNTTFE ACAPYPVSEK ILQETHSLIC FLVFYIVPLS IISAYYFLIA
     KTLYKSTFNM PAEEHTHARK QIESRKRVAK TVLVLVALFA VCWLPNHMLY LYRSFTYHSA
     VNSSAFHLSA TIFARVLAFS NSCVNPFALY WLSRSFRQHF KKQVYCCKTE PPASQQSPTH
     SSTITGITAV KGNIQMSEIS ITLLSAYDVK KE