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   13-SEP-2023, entry version 176.
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   GlyCosmos; P28336; 3 sites, No reported glycans.
DR   GlyGen; P28336; 3 sites.
DR   iPTMnet; P28336; -.
DR   PhosphoSitePlus; P28336; -.
DR   BioMuta; NMBR; -.
DR   DMDM; 212286370; -.
DR   PaxDb; P28336; -.
DR   PeptideAtlas; P28336; -.
DR   ProteomicsDB; 54477; -.
DR   Antibodypedia; 19807; 302 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   AGR; HGNC:7843; -.
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; ENSGT01090000260032; -.
DR   HOGENOM; CLU_009579_6_2_1; -.
DR   InParanoid; P28336; -.
DR   OMA; GHNLKQE; -.
DR   OrthoDB; 2905228at2759; -.
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 1146 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:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0004946; F:bombesin receptor activity; TAS:ProtInc.
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   CDD; cd15125; 7tmA_NMBR; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001556; Bombsn_rcpt-like.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001642; NeuroB_rcpt.
DR   PANTHER; PTHR45695; LEUCOKININ RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR45695:SF8; NEUROMEDIN-B RECEPTOR; 1.
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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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
//