ID   BRS3_SHEEP              Reviewed;         399 AA.
AC   O97967;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Bombesin receptor subtype-3;
DE            Short=BRS-3;
GN   Name=BRS3;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=10425452; DOI=10.1677/jme.0.0230107;
RA   Whitley J.C., Moore C., Giraud A.S., Shulkes A.;
RT   "Molecular cloning, genomic organization and selective expression of
RT   bombesin receptor subtype 3 in the sheep hypothalamus and pituitary.";
RL   J. Mol. Endocrinol. 23:107-116(1999).
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 (By
CC       similarity). {ECO:0000250}.
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; AF108210; AAD19642.1; -; mRNA.
DR   EMBL; AF108209; AAD19639.1; -; Genomic_DNA.
DR   EMBL; AF108207; AAD19639.1; JOINED; Genomic_DNA.
DR   EMBL; AF108208; AAD19639.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001009215.1; NM_001009215.1.
DR   AlphaFoldDB; O97967; -.
DR   SMR; O97967; -.
DR   STRING; 9940.ENSOARP00000012091; -.
DR   GeneID; 443044; -.
DR   KEGG; oas:443044; -.
DR   CTD; 680; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   OrthoDB; 1153238at2759; -.
DR   Proteomes; UP000002356; Unplaced.
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   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_0000069199"
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   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  44374 MW;  B48DD27197AED2EB CRC64;
     MSQRQPQSPN QTLISTTNDT ESSSSVVPND STNKRRTGDN SPGIEALCAI YITYAVIISV
     GILGNAILIK VFFKTKSMQT VPNIFITSLA FGDLLLLLTC VPVDVTHYLA EGWLFGRIGC
     KVLSFIRLTS VGVSVFTLTI LSADRYKAVV KPLERQPPNA ILKTCAKAGC IWIMSMIIAL
     PEAIFSNVYT FQDPDKNVTF KACASYPVSE RLLQEIHSLL CFLVFYIIPL SIISVYYSLI
     ARTLYKSTLN IPTEEQRHAR KQIESRKRIA KTVLVLVALF ALCWLPNHLL YLYRSFTSQT
     YMDSSTVHLF VTIISRILAF SNSCVNPFAL YWLSNTFQQH FKAQLFCCKA GRPDPTAANT
     PLDNLAVMGR VPGAASTQMS EISVSPFTGC SVKKEDDRV