BRS3_MOUSE
ID BRS3_MOUSE Reviewed; 399 AA.
AC O54798; O88790; Q544G9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Bombesin receptor subtype-3;
DE Short=BRS-3;
GN Name=Brs3;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9573346; DOI=10.1016/s0378-1119(98)00050-x;
RA Weber H.C., Hampton L.L., Jensen R.T., Battey J.F.;
RT "Structure and chromosomal localization of the mouse bombesin receptor
RT subtype 3 gene.";
RL Gene 211:125-131(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Role in sperm cell division, maturation, or function. This
CC receptor mediates its action by association with G proteins that
CC activate a phosphatidylinositol-calcium second messenger system.
CC -!- SUBUNIT: Interacts with C6orf89. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB010280; BAA24404.1; -; Genomic_DNA.
DR EMBL; U84901; AAC40133.1; -; Genomic_DNA.
DR EMBL; U84899; AAC40133.1; JOINED; Genomic_DNA.
DR EMBL; U84900; AAC40133.1; JOINED; Genomic_DNA.
DR EMBL; AK038616; BAC30064.1; -; mRNA.
DR EMBL; BC106961; AAI06962.1; -; mRNA.
DR EMBL; BC106962; AAI06963.1; -; mRNA.
DR CCDS; CCDS30150.1; -.
DR RefSeq; NP_033896.2; NM_009766.3.
DR AlphaFoldDB; O54798; -.
DR SMR; O54798; -.
DR STRING; 10090.ENSMUSP00000033464; -.
DR BindingDB; O54798; -.
DR ChEMBL; CHEMBL1075140; -.
DR GuidetoPHARMACOLOGY; 40; -.
DR GlyGen; O54798; 3 sites.
DR PhosphoSitePlus; O54798; -.
DR PaxDb; O54798; -.
DR PRIDE; O54798; -.
DR ProteomicsDB; 273845; -.
DR Antibodypedia; 580; 484 antibodies from 31 providers.
DR DNASU; 12209; -.
DR Ensembl; ENSMUST00000033464; ENSMUSP00000033464; ENSMUSG00000031130.
DR GeneID; 12209; -.
DR KEGG; mmu:12209; -.
DR UCSC; uc009tgu.1; mouse.
DR CTD; 680; -.
DR MGI; MGI:1100501; Brs3.
DR VEuPathDB; HostDB:ENSMUSG00000031130; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_6_2_1; -.
DR InParanoid; O54798; -.
DR OMA; HFIVTIF; -.
DR OrthoDB; 1153238at2759; -.
DR PhylomeDB; O54798; -.
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; 12209; 4 hits in 74 CRISPR screens.
DR PRO; PR:O54798; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O54798; protein.
DR Bgee; ENSMUSG00000031130; Expressed in gastrula and 13 other tissues.
DR Genevisible; O54798; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR001560; Bombesin_rcpt_3.
DR InterPro; IPR001556; Bombsn_rcpt-like.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00637; BOMBESIN3R.
DR PRINTS; PR00358; BOMBESINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..399
FT /note="Bombesin receptor subtype-3"
FT /id="PRO_0000069198"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..333
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 347
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 27..28
FT /note="VS -> AP (in Ref. 2; AAC40133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 44229 MW; 9E2DE5BD8E5567BF CRC64;
MSQRQSQSPN QTLISITNDT ETSSSVVSND TTHKGWTGDN SPGIEALCAI YITYAGIISV
GILGNAILIK VFFKTKSMQT VPNIFITSLA FGDLLLLLTC VPVDATHYLA EGWLFGKVGC
KVLSFIRLTS VGVSVFTLTI LSADRYKAVV KPLERQPPNA ILKTCAKAGG IWIVSMIFAL
PEAIFSNVYT FQDPNRNVTF ESCNSYPISE RLLQEIHSLL CFLVFYIIPL SIISVYYSLI
ARTLYKSTLN IPTEEQSHAR KQIESRKRIA KTVLVLVALF ALCWLPNHLL YLYHSFTYES
YANHSDVPFV IIIFSRVLAF SNSCVNPFAL YWLSKTFQQH FKAQLCCLKA EQPEPPLGDI
PLNNLTVMGR VPATGSAHVS EISVTLFSGS SAKKGEDKV
