NMBR_MOUSE
ID NMBR_MOUSE Reviewed; 390 AA.
AC O54799;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Neuromedin-B receptor;
DE Short=NMB-R;
DE AltName: Full=Neuromedin-B-preferring bombesin receptor;
GN Name=Nmbr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=9262170; DOI=10.1016/s0006-8993(97)00380-6;
RA Ohki-Hamazaki H., Wada E., Matsui K., Wada K.;
RT "Cloning and expression of the neuromedin B receptor and the third subtype
RT of bombesin receptor genes in the mouse.";
RL Brain Res. 762:165-172(1997).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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).
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=28780306; DOI=10.1016/j.yexcr.2017.08.003;
RA Yeo C.E., Kang W.Y., Seong S.J., Cho S., Lee H.W., Yoon Y.R., Kim H.J.;
RT "Neuromedin B and its receptor silencing suppresses osteoclast generation
RT by modulating precursor proliferation via M-CSF/c-Fms/D-type cyclins.";
RL Exp. Cell Res. 359:112-119(2017).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30734045; DOI=10.2340/00015555-3143;
RA Ehling S., Fukuyama T., Ko M.C., Olivry T., Baeumer W.;
RT "Neuromedin B Induces Acute Itch in Mice via the Activation of Peripheral
RT Sensory Neurons.";
RL Acta Derm. Venereol. 99:587-593(2019).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=31601264; DOI=10.1186/s13567-019-0695-2;
RA Yang G., Huang H., Tang M., Cai Z., Huang C., Qi B., Chen J.L.;
RT "Role of neuromedin B and its receptor in the innate immune responses
RT against influenza A virus infection in vitro and in vivo.";
RL Vet. Res. 50:80-80(2019).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=34133943; DOI=10.1016/j.cell.2021.05.017;
RA Li F., Jiang H., Shen X., Yang W., Guo C., Wang Z., Xiao M., Cui L.,
RA Luo W., Kim B.S., Chen Z., Huang A.J.W., Liu Q.;
RT "Sneezing reflex is mediated by a peptidergic pathway from nose to
RT brainstem.";
RL Cell 184:3762-3773(2021).
CC -!- FUNCTION: Receptor for neuromedin-B (By similarity). Contributes to the
CC maintenance of basal sigh rate through signaling in the pre-Botzinger
CC complex, a cluster of several thousand neurons in the ventrolateral
CC medulla responsible for inspiration during respiratory activity
CC (PubMed:26855425). Contributes to the induction of sneezing following
CC exposure to chemical irritants or allergens which causes release of NMB
CC by nasal sensory neurons and activation of NMBR-expressing neurons in
CC the sneeze-evoking region of the brainstem (PubMed:34133943). These in
CC turn activate neurons of the caudal ventral respiratory group, giving
CC rise to the sneezing response (PubMed:34133943). Contributes to
CC induction of acute itch, possibly through its activation on dorsal root
CC ganglion neurons by the NMB peptide (PubMed:30734045). Plays a role in
CC the innate immune response to influenza A virus infection by enhancing
CC interferon alpha expression and reducing expression of IL6
CC (PubMed:31601264). Plays a role in CSF1-induced proliferation of
CC osteoclast precursors by contributing to the positive regulation of the
CC expression of the CSF1 receptor CSF1R (PubMed:28780306).
CC {ECO:0000250|UniProtKB:P24053, ECO:0000269|PubMed:26855425,
CC ECO:0000269|PubMed:28780306, ECO:0000269|PubMed:30734045,
CC ECO:0000269|PubMed:31601264, ECO:0000269|PubMed:34133943}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in a subset of neurons of the pre-
CC Botzinger complex (PubMed:26855425). Within the pre-Botzinger complex,
CC there is some overlap with neurons expressing Grpr with some cells
CC expressing only Grpr or Nmbr while some cells express both
CC (PubMed:26855425). Expressed in dorsal root ganglion neurons and mast
CC cells (PubMed:30734045). Expressed in lung (PubMed:31601264).
CC {ECO:0000269|PubMed:26855425, ECO:0000269|PubMed:30734045,
CC ECO:0000269|PubMed:31601264}.
CC -!- DEVELOPMENTAL STAGE: During osteoclast development, expression is
CC abundant in early osteoclast precursor cells, decreases as the cells
CC differentiate and is almost absent in mature osteoclasts.
CC {ECO:0000269|PubMed:28780306}.
CC -!- INDUCTION: Up-regulated in lung tissue in response to infection with
CC influenza A virus. {ECO:0000269|PubMed:31601264}.
CC -!- DISRUPTION PHENOTYPE: Reduction in rate of basal sighing without
CC affecting the respiratory rate (PubMed:26855425). Significantly reduced
CC sneezing responses to chemical and allergen stimuli (PubMed:34133943).
CC {ECO:0000269|PubMed:26855425, ECO:0000269|PubMed:34133943}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB010281; BAA24405.1; -; Genomic_DNA.
DR CCDS; CCDS23707.1; -.
DR RefSeq; NP_032729.1; NM_008703.2.
DR AlphaFoldDB; O54799; -.
DR SMR; O54799; -.
DR STRING; 10090.ENSMUSP00000020015; -.
DR GlyGen; O54799; 3 sites.
DR iPTMnet; O54799; -.
DR PhosphoSitePlus; O54799; -.
DR jPOST; O54799; -.
DR PaxDb; O54799; -.
DR PRIDE; O54799; -.
DR ProteomicsDB; 252972; -.
DR Antibodypedia; 19807; 284 antibodies from 29 providers.
DR DNASU; 18101; -.
DR Ensembl; ENSMUST00000020015; ENSMUSP00000020015; ENSMUSG00000019865.
DR GeneID; 18101; -.
DR KEGG; mmu:18101; -.
DR UCSC; uc007elp.1; mouse.
DR CTD; 4829; -.
DR MGI; MGI:1100525; Nmbr.
DR VEuPathDB; HostDB:ENSMUSG00000019865; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_6_2_1; -.
DR InParanoid; O54799; -.
DR OMA; GHNLKQE; -.
DR OrthoDB; 1153238at2759; -.
DR PhylomeDB; O54799; -.
DR TreeFam; TF331292; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 18101; 1 hit in 71 CRISPR screens.
DR PRO; PR:O54799; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O54799; protein.
DR Bgee; ENSMUSG00000019865; Expressed in spermatocyte and 54 other tissues.
DR ExpressionAtlas; O54799; baseline and differential.
DR Genevisible; O54799; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0140374; P:antiviral innate immune response; IMP: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; IMP:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:MGI.
DR GO; GO:0090290; P:positive regulation of osteoclast proliferation; IMP:UniProtKB.
DR GO; GO:1903942; P:positive regulation of respiratory gaseous exchange; IMP:UniProtKB.
DR GO; GO:0160023; P:sneeze reflex; IMP: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 1: Evidence at protein 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_0000069904"
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 MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 16
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; 43623 MW; 2EA733B1DF108B42 CRC64;
MPPRSLSNLS FPTEANESEL VPEVWEKDFL PDSDGTTAEL VIRCVIPSLY LIIISVGLLG
NIMLVKIFLT NSAMRNVPNI FISNLAAGDL LLLLTCVPVD ASRYFFDEWV FGKLGCKLIP
AIQLTSVGVS VFTLTALSAD RYRAIVNPMD MQTSGVLLWT SLKAVGIWVV SVLLAVPEAV
FSEVARIGSL DNSSFTACIP YPQTDELHPK IHSVLIFLVY FLIPLVIISI YYYHIAKTLI
KSAHNLPGEY NEHTKKQMET RKRLAKIVLV FVGCFVFCWF PNHVLYLYRS FNYKEIDPSL
GHMIVTLVAR VLSFSNSCVN PFALYLLSES FRKHFNSQLC CGRKSYPERS TSYLLSSSAV
RMTSLKSNTK NVVTNSVLLN GHSTKQEIAL
