NMBR_HUMAN
ID NMBR_HUMAN Reviewed; 390 AA.
AC P28336; E9KL38; Q5VUK8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Neuromedin-B receptor;
DE Short=NMB-R;
DE AltName: Full=Epididymis tissue protein Li 185a;
DE AltName: Full=Neuromedin-B-preferring bombesin receptor;
GN Name=NMBR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANT MET-390.
RX PubMed=1655761; DOI=10.1016/s0021-9258(18)55129-2;
RA Corjay M.H., Dobrzanski D.J., Way J.M., Viallet J., Shapira H., Worland P.,
RA Sausville E.A., Battey J.F.;
RT "Two distinct bombesin receptor subtypes are expressed and functional in
RT human lung carcinoma cells.";
RL J. Biol. Chem. 266:18771-18779(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Epididymis;
RX PubMed=20736409; DOI=10.1074/mcp.m110.001719;
RA Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C.,
RA Jin S., Liu J., Zhu P., Liu Y.;
RT "Systematic mapping and functional analysis of a family of human epididymal
RT secretory sperm-located proteins.";
RL Mol. Cell. Proteomics 9:2517-2528(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, 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).
CC -!- FUNCTION: Receptor for neuromedin-B (PubMed:1655761). 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 (By similarity). 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 (PubMed:31601264). 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:1655761,
CC ECO:0000269|PubMed:31601264}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in epididymis (at protein level).
CC {ECO:0000269|PubMed:20736409}.
CC -!- INDUCTION: Up-regulated in response to infection with influenza A
CC virus. {ECO:0000269|PubMed:31601264}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M73482; AAA59939.1; -; mRNA.
DR EMBL; GU727635; ADU87637.1; -; mRNA.
DR EMBL; AL589674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47886.1; -; Genomic_DNA.
DR CCDS; CCDS5196.1; -.
DR PIR; B41007; B41007.
DR RefSeq; NP_001311236.1; NM_001324307.1.
DR RefSeq; NP_001311237.1; NM_001324308.1.
DR RefSeq; NP_002502.2; NM_002511.3.
DR AlphaFoldDB; P28336; -.
DR SMR; P28336; -.
DR BioGRID; 110893; 2.
DR STRING; 9606.ENSP00000258042; -.
DR BindingDB; P28336; -.
DR ChEMBL; CHEMBL3636; -.
DR GuidetoPHARMACOLOGY; 38; -.
DR GlyGen; P28336; 3 sites.
DR iPTMnet; P28336; -.
DR PhosphoSitePlus; P28336; -.
DR BioMuta; NMBR; -.
DR DMDM; 212286370; -.
DR PaxDb; P28336; -.
DR PeptideAtlas; P28336; -.
DR PRIDE; P28336; -.
DR ProteomicsDB; 54477; -.
DR Antibodypedia; 19807; 284 antibodies from 29 providers.
DR DNASU; 4829; -.
DR Ensembl; ENST00000258042.2; ENSP00000258042.1; ENSG00000135577.5.
DR GeneID; 4829; -.
DR KEGG; hsa:4829; -.
DR MANE-Select; ENST00000258042.2; ENSP00000258042.1; NM_002511.4; NP_002502.2.
DR UCSC; uc003qiu.3; human.
DR CTD; 4829; -.
DR DisGeNET; 4829; -.
DR GeneCards; NMBR; -.
DR HGNC; HGNC:7843; NMBR.
DR HPA; ENSG00000135577; Tissue enhanced (brain, testis).
DR MIM; 162341; gene.
DR neXtProt; NX_P28336; -.
DR OpenTargets; ENSG00000135577; -.
DR PharmGKB; PA31655; -.
DR VEuPathDB; HostDB:ENSG00000135577; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_6_2_1; -.
DR InParanoid; P28336; -.
DR OMA; GHNLKQE; -.
DR OrthoDB; 1153238at2759; -.
DR PhylomeDB; P28336; -.
DR TreeFam; TF331292; -.
DR PathwayCommons; P28336; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P28336; -.
DR SIGNOR; P28336; -.
DR BioGRID-ORCS; 4829; 10 hits in 1068 CRISPR screens.
DR GeneWiki; Neuromedin_B_receptor; -.
DR GenomeRNAi; 4829; -.
DR Pharos; P28336; Tchem.
DR PRO; PR:P28336; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P28336; protein.
DR Bgee; ENSG00000135577; Expressed in left testis and 60 other tissues.
DR Genevisible; P28336; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004946; F:bombesin receptor activity; TAS:ProtInc.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IBA:GO_Central.
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:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IMP:UniProtKB.
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 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_0000069903"
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..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
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 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"
FT VARIANT 390
FT /note="L -> M (in dbSNP:rs7453944)"
FT /evidence="ECO:0000269|PubMed:1655761"
FT /id="VAR_044513"
SQ SEQUENCE 390 AA; 43435 MW; 8BA9AAD4F3B7309F CRC64;
MPSKSLSNLS VTTGANESGS VPEGWERDFL PASDGTTTEL VIRCVIPSLY LLIITVGLLG
NIMLVKIFIT NSAMRSVPNI FISNLAAGDL LLLLTCVPVD ASRYFFDEWM FGKVGCKLIP
VIQLTSVGVS VFTLTALSAD RYRAIVNPMD MQTSGALLRT CVKAMGIWVV SVLLAVPEAV
FSEVARISSL DNSSFTACIP YPQTDELHPK IHSVLIFLVY FLIPLAIISI YYYHIAKTLI
KSAHNLPGEY NEHTKKQMET RKRLAKIVLV FVGCFIFCWF PNHILYMYRS FNYNEIDPSL
GHMIVTLVAR VLSFGNSCVN PFALYLLSES FRRHFNSQLC CGRKSYQERG TSYLLSSSAV
RMTSLKSNAK NMVTNSVLLN GHSMKQEMAL
