NMBR_RAT
ID NMBR_RAT Reviewed; 390 AA.
AC P24053;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Neuromedin-B receptor;
DE Short=NMB-R;
DE AltName: Full=Neuromedin-B-preferring bombesin receptor;
GN Name=Nmbr;
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], AND FUNCTION.
RC TISSUE=Esophagus;
RX PubMed=1848080; DOI=10.1016/0896-6273(91)90250-4;
RA Wada E., Way J., Shapira H., Kusano K., Lebacq-Verheyden A.-M., Coy D.,
RA Jensen R., Battey J.F.;
RT "cDNA cloning, characterization, and brain region-specific expression of a
RT neuromedin-B-preferring bombesin receptor.";
RL Neuron 6:421-430(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8391296; DOI=10.1007/bf02736689;
RA Giladi E., Nagalla S.R., Spindel E.R.;
RT "Molecular cloning and characterization of receptors for the mammalian
RT bombesin-like peptides.";
RL J. Mol. Neurosci. 4:41-54(1993).
RN [3]
RP FUNCTION.
RX PubMed=26855425; DOI=10.1038/nature16964;
RA Li P., Janczewski W.A., Yackle K., Kam K., Pagliardini S., Krasnow M.A.,
RA Feldman J.L.;
RT "The peptidergic control circuit for sighing.";
RL Nature 530:293-297(2016).
CC -!- FUNCTION: Receptor for neuromedin-B (PubMed:1848080). Contributes to
CC the maintenance of basal sigh rate through signaling in the pre-
CC Botzinger complex, a cluster of several thousand neurons in the
CC ventrolateral medulla responsible for inspiration during respiratory
CC activity (PubMed:26855425). Contributes to the induction of sneezing
CC following exposure to chemical irritants or allergens which causes
CC release of NMB by nasal sensory neurons and activation of NMBR-
CC expressing neurons in the sneeze-evoking region of the brainstem (By
CC similarity). These in turn activate neurons of the caudal ventral
CC respiratory group, giving rise to the sneezing response (By
CC similarity). Contributes to induction of acute itch, possibly through
CC its activation on dorsal root ganglion neurons by the NMB peptide (By
CC similarity). Plays a role in the innate immune response to influenza A
CC virus infection by enhancing interferon alpha expression and reducing
CC expression of IL6 (By similarity). Plays a role in CSF1-induced
CC proliferation of osteoclast precursors by contributing to the positive
CC regulation of the expression of the CSF1 receptor CSF1R (By
CC similarity). {ECO:0000250|UniProtKB:O54799, ECO:0000269|PubMed:1848080,
CC ECO:0000269|PubMed:26855425}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Brain (olfactory bulb and central thalamic
CC regions), and esophagus.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U37058; AAA79881.1; -; mRNA.
DR PIR; JH0374; JH0374.
DR RefSeq; NP_036931.1; NM_012799.1.
DR RefSeq; XP_017444304.1; XM_017588815.1.
DR AlphaFoldDB; P24053; -.
DR SMR; P24053; -.
DR BindingDB; P24053; -.
DR ChEMBL; CHEMBL4440; -.
DR GuidetoPHARMACOLOGY; 38; -.
DR GlyGen; P24053; 2 sites.
DR PhosphoSitePlus; P24053; -.
DR PRIDE; P24053; -.
DR Ensembl; ENSRNOT00000016215; ENSRNOP00000016215; ENSRNOG00000012103.
DR GeneID; 25264; -.
DR KEGG; rno:25264; -.
DR CTD; 4829; -.
DR RGD; 3181; Nmbr.
DR GeneTree; ENSGT01050000244862; -.
DR InParanoid; P24053; -.
DR OrthoDB; 1153238at2759; -.
DR PhylomeDB; P24053; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P24053; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004946; F:bombesin receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IPI:RGD.
DR GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:RGD.
DR GO; GO:0090290; P:positive regulation of osteoclast proliferation; ISS:UniProtKB.
DR GO; GO:1903942; P:positive regulation of respiratory gaseous exchange; ISS:UniProtKB.
DR GO; GO:0160023; P:sneeze reflex; ISS:UniProtKB.
DR InterPro; IPR001556; Bombsn_rcpt-like.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001642; NeuroB_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00358; BOMBESINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00639; NEUROMEDINBR.
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; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..390
FT /note="Neuromedin-B receptor"
FT /id="PRO_0000069905"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..327
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54799"
FT LIPID 341
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 390 AA; 43535 MW; EEAEC625014614B4 CRC64;
MPPRSLPNLS LPTEASESEL EPEVWENDFL PDSDGTTAEL VIRCVIPSLY LIIISVGLLG
NIMLVKIFLT NSTMRSVPNI FISNLAAGDL LLLLTCVPVD ASRYFFDEWV FGKLGCKLIP
AIQLTSVGVS VFTLTALSAD RYRAIVNPMD MQTSGVVLWT SLKAVGIWVV SVLLAVPEAV
FSEVARIGSS DNSSFTACIP YPQTDELHPK IHSVLIFLVY FLIPLVIISI YYYHIAKTLI
RSAHNLPGEY NEHTKKQMET RKRLAKIVLV FVGCFVFCWF PNHILYLYRS FNYKEIDPSL
GHMIVTLVAR VLSFSNSCVN PFALYLLSES FRKHFNSQLC CGQKSYPERS TSYLLSSSAV
RMTSLKSNAK NVVTNSVLLN GHSTKQEIAL
