BRS3_MACMU
ID BRS3_MACMU Reviewed; 398 AA.
AC Q6H2Y3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Bombesin receptor subtype-3;
DE Short=BRS-3;
GN Name=BRS3;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15203211; DOI=10.1016/j.ygeno.2004.01.008;
RA Sano H., Feighner S.D., Hreniuk D.L., Iwaasa H., Sailer A.W., Pan J.,
RA Reitman M.L., Kanatani A., Howard A.D., Tan C.P.;
RT "Characterization of the bombesin-like peptide receptor family in
RT primates.";
RL Genomics 84:139-146(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; AY350447; AAR07972.1; -; mRNA.
DR RefSeq; NP_001028074.1; NM_001032902.1.
DR AlphaFoldDB; Q6H2Y3; -.
DR SMR; Q6H2Y3; -.
DR STRING; 9544.ENSMMUP00000008499; -.
DR Ensembl; ENSMMUT00000093189; ENSMMUP00000077818; ENSMMUG00000052892.
DR GeneID; 574261; -.
DR KEGG; mcc:574261; -.
DR CTD; 680; -.
DR VEuPathDB; HostDB:ENSMMUG00000052892; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_6_2_1; -.
DR InParanoid; Q6H2Y3; -.
DR OMA; HFIVTIF; -.
DR OrthoDB; 1153238at2759; -.
DR TreeFam; TF331292; -.
DR Proteomes; UP000006718; Chromosome X.
DR ExpressionAtlas; Q6H2Y3; baseline.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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..398
FT /note="Bombesin receptor subtype-3"
FT /id="PRO_0000069197"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..142
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..332
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 346
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 119..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 398 AA; 44266 MW; B687A36AA9391B92 CRC64;
MAQRQPHSPN QTLISITNDT ESSSVVSNDN TNKGRSGDNS PGIEALCAIY ITYAVIISVG
ILGNAILIKV FFKTKSMQTV PNIFITSLAF GDLLLLLTCV PVDATHYLAE GWLFGRIGCK
VLSFIRLTSV GVSVFTLTIL SADRYKAVVK PLERQPSNAI LKTCIKAGCV WIVSMIFALP
EAIFSNVYSF RDPNKNVTFE SCTSYPVSKK LLQEIHSLLC FLVFYIIPLS IISVYYSLIA
RTLYKSTLNI PTEEQGHARK QIESRKRIAR TVLVLVALFA LCWLPNHLLY LYHSFTSQTY
VDPSAMHFIF TIFSRVLAFS NSCVNPFALY WLSKTFQKHF KAQLFCCKAE QPEPPVADTS
LTTLAVMGRV PGTGNMQMSE ISVTSFPGCS VKQAEDRV
