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BRS3_CAVPO
ID   BRS3_CAVPO              Reviewed;         399 AA.
AC   P35371;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Bombesin receptor subtype-3;
DE            Short=BRS-3;
GN   Name=BRS3;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Uterus;
RX   PubMed=1325907; DOI=10.1111/j.1432-1033.1992.tb17201.x;
RA   Gorbulev V., Akhundova A., Buechner H., Fahrenholz F.;
RT   "Molecular cloning of a new bombesin receptor subtype expressed in uterus
RT   during pregnancy.";
RL   Eur. J. Biochem. 208:405-410(1992).
CC   -!- FUNCTION: Role in sperm cell division, maturation, or function. The
CC       relative order of ligand affinity is GRP = neuromedin-C >> neuromedin-
CC       B. This receptor mediates its action by association with G proteins
CC       that activate a phosphatidylinositol-calcium second messenger system.
CC   -!- SUBUNIT: Interacts with C6orf89. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Mainly in uteri of pregnant animals.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X67126; CAA47605.1; -; mRNA.
DR   PIR; S29480; S29480.
DR   RefSeq; NP_001166392.1; NM_001172921.1.
DR   AlphaFoldDB; P35371; -.
DR   SMR; P35371; -.
DR   STRING; 10141.ENSCPOP00000012930; -.
DR   Ensembl; ENSCPOT00000014498; ENSCPOP00000012930; ENSCPOG00000014354.
DR   GeneID; 100135488; -.
DR   KEGG; cpoc:100135488; -.
DR   CTD; 680; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244862; -.
DR   HOGENOM; CLU_009579_6_2_1; -.
DR   InParanoid; P35371; -.
DR   OMA; HFIVTIF; -.
DR   OrthoDB; 1153238at2759; -.
DR   TreeFam; TF331292; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000014354; Expressed in heart and 2 other tissues.
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_0000069195"
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"
SQ   SEQUENCE   399 AA;  44342 MW;  19B75D027AB9A0DE CRC64;
     MSQKQPQSPN QTLISITNDT ESSSSVVSND TTNKGWTGDN SPGIEALCAI YITYAVIISV
     GILGNAILIK VFFKTKSMQT VPNIFITSLA LGDLLLLLTC VPVDATHYLA EGWLFGRIGC
     KVLSFIRLTS VGVSVFTLTI LSADRYKAVV KPLERQPSNA ILKTCAKAGC IWIMSMIFAL
     PEAIFSNVHT LRDPNKNMTS EWCAFYPVSE KLLQEIHALL SFLVFYIIPL SIISVYYSLI
     ARTLYKSTLN IPTEEQSHAR KQVESRKRIA KTVLVLVALF ALCWLPNHLL NLYHSFTHKA
     YEDSSAIHFI VTIFSRVLAF SNSCVNPFAL YWLSKTFQKQ FKAQLFCCKG ELPEPPLAAT
     PLNSLAVMGR VSGTENTHIS EIGVASFIGR PMKKEENRV
 
 
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