BRS3_RAT
ID BRS3_RAT Reviewed; 399 AA.
AC Q8K418;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Bombesin receptor subtype-3;
DE Short=BRS-3;
GN Name=Brs3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=12102638; DOI=10.1021/bi0202777;
RA Liu J., Lao Z.J., Zhang J., Schaeffer M.T., Jiang M.M., Guan X.M.,
RA van der Ploeg L.H.T., Fong T.M.;
RT "Molecular basis of the pharmacological difference between rat and human
RT bombesin receptor subtype-3 (BRS-3).";
RL Biochemistry 41:8954-8960(2002).
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; AF510984; AAM95932.1; -; mRNA.
DR RefSeq; NP_690058.1; NM_152845.1.
DR AlphaFoldDB; Q8K418; -.
DR SMR; Q8K418; -.
DR STRING; 10116.ENSRNOP00000001164; -.
DR BindingDB; Q8K418; -.
DR ChEMBL; CHEMBL1075111; -.
DR GuidetoPHARMACOLOGY; 40; -.
DR GlyGen; Q8K418; 3 sites.
DR iPTMnet; Q8K418; -.
DR PhosphoSitePlus; Q8K418; -.
DR PaxDb; Q8K418; -.
DR GeneID; 260319; -.
DR KEGG; rno:260319; -.
DR CTD; 680; -.
DR RGD; 628645; Brs3.
DR VEuPathDB; HostDB:ENSRNOG00000000873; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_6_2_1; -.
DR InParanoid; Q8K418; -.
DR OMA; HFIVTIF; -.
DR OrthoDB; 1153238at2759; -.
DR PhylomeDB; Q8K418; -.
DR TreeFam; TF331292; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:Q8K418; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000000873; Expressed in testis.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
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_0000263005"
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"
SQ SEQUENCE 399 AA; 44204 MW; 13034C6D44451338 CRC64;
MSQRQPQSPN QTLISITNDT ETSSSAVSND TTPKGWTGDN SPGIEALCAI YITYAVIISV
GILGNAILIK VFFKTKSMQT VPNIFITSLA FGDLLLLLTC VPVDATHYLA EGWLFGKVGC
KVLSFIRLTS VGVSVFTLTI LSADRYKAVV KPLERQPSNA ILKTCAKAGG IWIMAMIFAL
PEAIFSNVYT FQDPNRNVTF ESCNSYPISE RLLQEIHSLL CFLVFYIIPL SIISVYYSLI
ARTLYKSTLN IPTEEQSHAR KQIESRKRIA KTVLVLVALF ALCWLPNHLL YLYHSFTYES
YAEPSDVPFV VTIFSRVLAF SNSCVNPFAL YWLSKTFQKH FKAQLCCFKA EQPEPPLGDT
PLNNLTVMGR VPATGSAHVS EISVTLFSGS TAKKGEDKV
