BKRB1_CANLF
ID BKRB1_CANLF Reviewed; 350 AA.
AC Q9BDQ5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=B1 bradykinin receptor;
DE Short=B1R;
DE Short=BK-1 receptor;
GN Name=BDKRB1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11258662; DOI=10.1515/bc.2001.018;
RA Hess F., Hey P.J., Chen T.-B., O'Brien J., Omalley S.S., Pettibone D.J.,
RA Chang R.S.L.;
RT "Molecular cloning and pharmacological characterization of the canine B1
RT and B2 bradykinin receptors.";
RL Biol. Chem. 382:123-129(2001).
CC -!- FUNCTION: This is a receptor for bradykinin. Could be a factor in
CC chronic pain and inflammation. {ECO:0000269|PubMed:11258662}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P46663};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Bradykinin receptor subfamily. BDKRB1 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF334947; AAK21216.1; -; Genomic_DNA.
DR RefSeq; NP_001014306.1; NM_001014284.1.
DR AlphaFoldDB; Q9BDQ5; -.
DR SMR; Q9BDQ5; -.
DR STRING; 9612.ENSCAFP00000039552; -.
DR BindingDB; Q9BDQ5; -.
DR ChEMBL; CHEMBL4724; -.
DR PaxDb; Q9BDQ5; -.
DR Ensembl; ENSCAFT00030016449; ENSCAFP00030014368; ENSCAFG00030008931.
DR Ensembl; ENSCAFT00040000241; ENSCAFP00040000184; ENSCAFG00040000168.
DR Ensembl; ENSCAFT00845006349; ENSCAFP00845005045; ENSCAFG00845003563.
DR GeneID; 490847; -.
DR KEGG; cfa:490847; -.
DR CTD; 623; -.
DR VEuPathDB; HostDB:ENSCAFG00845003563; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234534; -.
DR InParanoid; Q9BDQ5; -.
DR PRO; PR:Q9BDQ5; -.
DR Proteomes; UP000002254; Chromosome 8.
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:0004947; F:bradykinin receptor activity; IEA:Ensembl.
DR GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:InterPro.
DR InterPro; IPR001186; Brdyknn_1_rcpt.
DR InterPro; IPR000496; Brdyknn_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00425; BRADYKININR.
DR PRINTS; PR00993; BRADYKINNB1R.
DR PRINTS; PR00237; GPCRRHODOPSN.
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..350
FT /note="B1 bradykinin receptor"
FT /id="PRO_0000069179"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 327
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 350 AA; 39509 MW; 28272A819FF955E0 CRC64;
MASRAPLELL PLNRSQLSPP NATTCDDAPE AWDLLHRVLP SVIIIICVCG LLGNLLVLAV
LLRPRRRLNV AEMYLANLAA SDLVFVLGLP FWAANISNQF RWPFGGLLCR LVNGVIKANL
FISIFLVVAI SRDRYRALVH PMATRRRRQA RATCVLIWVA GSLLSVPTFL FRSIEAVPEL
NNDSACVLLH PPGAWHVARM VELNVLGFLL PLAAIVFFNC HILASLRGRP EVRGARCGGP
PDGRTTALIL TFVAAFLVCW TPYHFFAFLE FLTQVQVVRG CFWENFKDLG LQYASFFAFI
NSCLNPVIYV FVGRLFRTRV WDLFKQCAPR RPPAVSWSHR KRVLQLFWQN
