BRS3_HUMAN
ID BRS3_HUMAN Reviewed; 399 AA.
AC P32247;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Bombesin receptor subtype-3;
DE Short=BRS-3;
GN Name=BRS3;
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].
RX PubMed=8383682; DOI=10.1016/s0021-9258(18)53415-3;
RA Fathi Z., Corjay M.H., Shapira H., Wada E., Benya R., Jensen R.,
RA Viallet J., Sausville E.A., Battey J.F.;
RT "BRS-3: a novel bombesin receptor subtype selectively expressed in testis
RT and lung carcinoma cells.";
RL J. Biol. Chem. 268:5979-5984(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Uterus;
RX PubMed=8131855; DOI=10.1016/0014-5793(94)80150-9;
RA Gorbulev V., Akhundova A., Grzeschik K.H., Fahrenholz F.;
RT "Organization and chromosomal localization of the gene for the human
RT bombesin receptor subtype expressed in pregnant uterus.";
RL FEBS Lett. 340:260-264(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP INTERACTION WITH C6ORF89.
RX PubMed=21857995; DOI=10.1371/journal.pone.0023072;
RA Liu H.J., Tan Y.R., Li M.L., Liu C., Xiang Y., Qin X.Q.;
RT "Cloning of a novel protein interacting with BRS-3 and its effects in wound
RT repair of bronchial epithelial cells.";
RL PLoS ONE 6:E23072-E23072(2011).
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:0000269|PubMed:21857995}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: In germ cells in testis. Lung carcinoma cells.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L08893; AAA35604.1; -; mRNA.
DR EMBL; X76498; CAA54031.1; -; Genomic_DNA.
DR EMBL; AY585193; AAT79496.1; -; mRNA.
DR EMBL; Z97632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14656.1; -.
DR PIR; A46632; A46632.
DR RefSeq; NP_001718.1; NM_001727.1.
DR AlphaFoldDB; P32247; -.
DR SMR; P32247; -.
DR STRING; 9606.ENSP00000359682; -.
DR BindingDB; P32247; -.
DR ChEMBL; CHEMBL4080; -.
DR GuidetoPHARMACOLOGY; 40; -.
DR GlyGen; P32247; 2 sites.
DR iPTMnet; P32247; -.
DR PhosphoSitePlus; P32247; -.
DR BioMuta; BRS3; -.
DR DMDM; 416726; -.
DR MassIVE; P32247; -.
DR PaxDb; P32247; -.
DR PeptideAtlas; P32247; -.
DR PRIDE; P32247; -.
DR Antibodypedia; 580; 484 antibodies from 31 providers.
DR DNASU; 680; -.
DR Ensembl; ENST00000370648.4; ENSP00000359682.3; ENSG00000102239.5.
DR GeneID; 680; -.
DR KEGG; hsa:680; -.
DR MANE-Select; ENST00000370648.4; ENSP00000359682.3; NM_001727.2; NP_001718.1.
DR UCSC; uc004ezv.2; human.
DR CTD; 680; -.
DR DisGeNET; 680; -.
DR GeneCards; BRS3; -.
DR HGNC; HGNC:1113; BRS3.
DR HPA; ENSG00000102239; Tissue enriched (epididymis).
DR MIM; 300107; gene.
DR neXtProt; NX_P32247; -.
DR OpenTargets; ENSG00000102239; -.
DR PharmGKB; PA25427; -.
DR VEuPathDB; HostDB:ENSG00000102239; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_6_2_1; -.
DR InParanoid; P32247; -.
DR OMA; HFIVTIF; -.
DR OrthoDB; 1153238at2759; -.
DR PhylomeDB; P32247; -.
DR TreeFam; TF331292; -.
DR PathwayCommons; P32247; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P32247; -.
DR BioGRID-ORCS; 680; 11 hits in 692 CRISPR screens.
DR GeneWiki; Bombesin-like_receptor_3; -.
DR GenomeRNAi; 680; -.
DR Pharos; P32247; Tchem.
DR PRO; PR:P32247; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P32247; protein.
DR Bgee; ENSG00000102239; Expressed in buccal mucosa cell and 36 other tissues.
DR Genevisible; P32247; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
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:0008343; P:adult feeding behavior; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; TAS:ProtInc.
DR GO; GO:0008217; P:regulation of blood pressure; TAS:ProtInc.
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 1: Evidence at protein 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_0000069196"
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 DISULFID 120..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 53
FT /note="T -> P (in dbSNP:rs5232)"
FT /id="VAR_011844"
FT VARIANT 162
FT /note="L -> Q (in dbSNP:rs5234)"
FT /id="VAR_011845"
SQ SEQUENCE 399 AA; 44411 MW; 979C93E962A3A28A CRC64;
MAQRQPHSPN QTLISITNDT ESSSSVVSND NTNKGWSGDN SPGIEALCAI YITYAVIISV
GILGNAILIK VFFKTKSMQT VPNIFITSLA FGDLLLLLTC VPVDATHYLA EGWLFGRIGC
KVLSFIRLTS VGVSVFTLTI LSADRYKAVV KPLERQPSNA ILKTCVKAGC VWIVSMIFAL
PEAIFSNVYT FRDPNKNMTF ESCTSYPVSK KLLQEIHSLL CFLVFYIIPL SIISVYYSLI
ARTLYKSTLN IPTEEQSHAR KQIESRKRIA RTVLVLVALF ALCWLPNHLL YLYHSFTSQT
YVDPSAMHFI FTIFSRVLAF SNSCVNPFAL YWLSKSFQKH FKAQLFCCKA ERPEPPVADT
SLTTLAVMGT VPGTGSIQMS EISVTSFTGC SVKQAEDRF
