NMBR_PIG
ID NMBR_PIG Reviewed; 390 AA.
AC B2ZI34; A0A287BJR5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Neuromedin-B receptor {ECO:0000312|EMBL:ACD50931.1};
DE Short=NMB-R {ECO:0000305};
DE AltName: Full=Neuromedin-B-preferring bombesin receptor {ECO:0000305};
GN Name=NMBR {ECO:0000312|VGNC:VGNC:90789};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|EMBL:ACD50931.1};
RN [1] {ECO:0000312|EMBL:AIR07401.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=27010315; DOI=10.1371/journal.pone.0151871;
RA Ma Z., Su J., Guo T., Jin M., Li X., Lei Z., Hou Y., Li X., Jia C.,
RA Zhang Z., Ahmed E.;
RT "Neuromedin B and Its Receptor: Gene Cloning, Tissue Distribution and
RT Expression Levels of the Reproductive Axis in Pigs.";
RL PLoS ONE 11:e0151871-e0151871(2016).
RN [2] {ECO:0000312|EMBL:ACD50931.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang J., Yang G.-Y., Li H.-J., Wang Y.-L., Zhao W.-D., Wang W.-J.;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000312|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=29632025; DOI=10.1530/jme-17-0242;
RA Ma Z., Zhang Y., Su J., Yang S., Qiao W., Li X., Lei Z., Cheng L., An N.,
RA Wang W., Feng Y., Zhang J.;
RT "Effects of neuromedin B on steroidogenesis, cell proliferation and
RT apoptosis in porcine Leydig cells.";
RL J. Mol. Endocrinol. 61:13-23(2018).
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 (By
CC similarity). 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 (By similarity). These in
CC turn activate neurons of the caudal ventral respiratory group, giving
CC rise to the sneezing response (By similarity). Contributes to induction
CC of acute itch, possibly through its activation on dorsal root ganglion
CC neurons by the NMB peptide (By similarity). Plays a role in the innate
CC immune response to influenza A virus infection by enhancing interferon
CC alpha expression and reducing expression of IL6 (By similarity). Plays
CC a role in CSF1-induced proliferation of osteoclast precursors by
CC contributing to the positive regulation of the expression of the CSF1
CC receptor CSF1R (By similarity). {ECO:0000250|UniProtKB:O54799,
CC ECO:0000250|UniProtKB:P28336}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in peripheral tissues where it is
CC detected in the respiratory system, circulatory system, digestive
CC system, urogenital system, lymphatic organs and endocrine system (at
CC protein level) (PubMed:27010315). In the testis, expressed mainly in
CC Leydig cells (at protein level) (PubMed:29632025).
CC {ECO:0000269|PubMed:27010315, ECO:0000269|PubMed:29632025}.
CC -!- DEVELOPMENTAL STAGE: During the sow estrus cycle, highest levels are
CC found in the hypothalamus at proestrus and estrus with a significant
CC drop at metestrus and an increase at diestrus. In the pituitary gland,
CC expression increases from proestrus to estrus, drops at metestrus and
CC increases at diestrus. In the ovary, expression increases from
CC proestrus to estrus, drops at metestrus and remains at a similar level
CC at diestrus. During boar postnatal development, expression peaks in the
CC hypothalamus at day 30 and decreases thereafter. In the pituitary
CC gland, expression peaks at day 60, drops slightly at day 90 and
CC increases again at day 120. In the testis, expression drops from day 3
CC to day 30 with peak levels at day 90 and a decrease at day 120.
CC {ECO:0000269|PubMed:27010315}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|RuleBase:RU000688}.
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DR EMBL; KM058699; AIR07401.1; -; mRNA.
DR EMBL; EU670045; ACD50931.1; -; mRNA.
DR EMBL; AEMK02000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001121961.1; NM_001128489.1.
DR SMR; B2ZI34; -.
DR STRING; 9823.ENSSSCP00000004473; -.
DR PaxDb; B2ZI34; -.
DR Ensembl; ENSSSCT00000042834; ENSSSCP00000056848; ENSSSCG00000036250.
DR Ensembl; ENSSSCT00005006839; ENSSSCP00005003967; ENSSSCG00005004584.
DR Ensembl; ENSSSCT00015072556; ENSSSCP00015029109; ENSSSCG00015054424.
DR Ensembl; ENSSSCT00025015717; ENSSSCP00025006226; ENSSSCG00025011882.
DR Ensembl; ENSSSCT00035096923; ENSSSCP00035040861; ENSSSCG00035071663.
DR Ensembl; ENSSSCT00040016579; ENSSSCP00040006663; ENSSSCG00040012537.
DR Ensembl; ENSSSCT00045031812; ENSSSCP00045022034; ENSSSCG00045018702.
DR Ensembl; ENSSSCT00055058408; ENSSSCP00055046743; ENSSSCG00055029411.
DR Ensembl; ENSSSCT00060046354; ENSSSCP00060019851; ENSSSCG00060034182.
DR Ensembl; ENSSSCT00065091742; ENSSSCP00065040157; ENSSSCG00065066840.
DR GeneID; 100169653; -.
DR KEGG; ssc:100169653; -.
DR CTD; 4829; -.
DR VGNC; VGNC:90789; NMBR.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_6_2_1; -.
DR InParanoid; B2ZI34; -.
DR OrthoDB; 1153238at2759; -.
DR TreeFam; TF331292; -.
DR Reactome; R-SSC-416476; G alpha (q) signalling events.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000036250; Expressed in medulla oblongata and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0004946; F:bombesin receptor activity; IEA:InterPro.
DR GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IEA:Ensembl.
DR GO; GO:0090290; P:positive regulation of osteoclast proliferation; ISS:UniProtKB.
DR GO; GO:1903942; P:positive regulation of respiratory gaseous exchange; IEA:Ensembl.
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_0000455614"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 77..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..117
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..210
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 211..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 267..287
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..305
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..328
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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"
SQ SEQUENCE 390 AA; 43328 MW; F4C172DF906ED21A CRC64;
MPPKSLSNLS QTAGVNQSGF FPGASERDFL PATDRTTAEF VIRCVIPSLY LLIITVGLLG
NIVLVKIFLT NSAMRSVPNI FISNLAAGDV LLLLTCVPVD ASRYFLDEWM FGKVGCKLIP
VIQLTSVGVS VFTLTALSAD RYRAIVNPMD IQTSGAVLWT CVKAGGIWVV SVLLAVPEAV
FSEVARIDGL DNGSFTACIP YPQTDELHPK IHSVLIFLVY FLIPLGIISV YYYHIAKTLI
KSAHNLPGEY NEHTKKQMET RKRLAKIVLV FVGCFVFCWF PNHILYMYRS FNYNEIDPSL
GHMIVTLVAR VLSFCNSCVN PFALYLLSES FRKHFNNQLC CGRKSYRERS PSYLLSSSAV
RMTSLKSNAK NIVTNSVVPN GHSVKQEMAL
