BKRB1_RAT
ID BKRB1_RAT Reviewed; 337 AA.
AC P97583; O35782; Q9R250;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=B1 bradykinin receptor;
DE Short=B1R;
DE Short=BK-1 receptor;
DE AltName: Full=Kinin B1 receptor;
DE Short=KB1;
GN Name=Bdkrb1; Synonyms=B1bkr, Bkr;
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], AND INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=9804950; DOI=10.1016/s0167-4781(98)00163-8;
RA Ni A., Chai K.X., Chao L., Chao J.;
RT "Molecular cloning and expression of rat bradykinin B1 receptor.";
RL Biochim. Biophys. Acta 1442:177-185(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Urinary bladder;
RX PubMed=10422787; DOI=10.1016/s0014-2999(99)00315-5;
RA Jones C., Phillips E., Davis C., Arbuckle J., Yaqoob M., Burgess G.M.,
RA Docherty R.J., Webb M., Bevan S.J., McIntyre P.;
RT "Molecular characterisation of cloned bradykinin B1 receptors from rat and
RT human.";
RL Eur. J. Pharmacol. 374:423-433(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sprague-Dawley;
RA Oliveira S.M., Araujo R.C., Pesquero J.L., Bader M., Pesquero J.B.;
RT "Molecular cloning of a rat kinin B1 receptor gene.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-15.
RC STRAIN=Sprague-Dawley;
RA Schanstra J.P., Girolami J.P., Bascands J.L.;
RT "Rat bradykinin B1 gene, promoter region, exon 1, intron 1, and exon 2.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This is a receptor for bradykinin. Could be a factor in
CC chronic pain and inflammation. {ECO:0000250|UniProtKB:P46663}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P46663};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in bladder, lung, duodenum, kidney,
CC uterus, thymus, salivary gland, testis, prostate, macrophages, aorta,
CC spleen and heart.
CC -!- INDUCTION: By lipopolysaccharide (LPS), four hours after treatment
CC levels show an increase in many tissues. After 12 hours maximum levels
CC are observed in the heart. {ECO:0000269|PubMed:10422787,
CC ECO:0000269|PubMed:9804950}.
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; U66107; AAC78505.2; -; mRNA.
DR EMBL; AJ132230; CAA10610.1; -; mRNA.
DR EMBL; AF009899; AAB63592.1; -; Genomic_DNA.
DR EMBL; AF114406; AAD29286.1; -; Genomic_DNA.
DR RefSeq; NP_110478.1; NM_030851.1.
DR RefSeq; XP_008763083.1; XM_008764861.2.
DR AlphaFoldDB; P97583; -.
DR SMR; P97583; -.
DR STRING; 10116.ENSRNOP00000005953; -.
DR BindingDB; P97583; -.
DR ChEMBL; CHEMBL4613; -.
DR DrugCentral; P97583; -.
DR GuidetoPHARMACOLOGY; 41; -.
DR GlyGen; P97583; 3 sites.
DR PhosphoSitePlus; P97583; -.
DR PaxDb; P97583; -.
DR Ensembl; ENSRNOT00000005953; ENSRNOP00000005953; ENSRNOG00000004488.
DR GeneID; 81509; -.
DR KEGG; rno:81509; -.
DR UCSC; RGD:620401; rat.
DR CTD; 623; -.
DR RGD; 620401; Bdkrb1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234534; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P97583; -.
DR OMA; QGCFWEE; -.
DR OrthoDB; 951204at2759; -.
DR PhylomeDB; P97583; -.
DR TreeFam; TF330024; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P97583; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004488; Expressed in stomach and 4 other tissues.
DR Genevisible; P97583; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0004947; F:bradykinin receptor activity; IDA:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IPI:RGD.
DR GO; GO:0016477; P:cell migration; IMP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IMP:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:RGD.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:RGD.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:InterPro.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
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 Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..337
FT /note="B1 bradykinin receptor"
FT /id="PRO_0000069187"
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..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..337
FT /note="Cytoplasmic"
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 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 337 AA; 38378 MW; 226828DF0F26BA8E CRC64;
MASEVLLELQ PSNRSLQAPA NITSCESALE DWDLLYRVLP GFVITICFFG LLGNLLVLSF
FLLPWRQWWW QQRQRQQRLT IAEIYLANLA ASDLVFVLGL PFWAENIGNR FNWPFGTDLC
RVVSGVIKAN LFVSIFLVVA ISQDRYRLLV YPMTSWGYRR RRQAQATCLL IWVAGGLLSI
PTFLLRSVKV VPDLNVSACI LLFPHEAWHF ARMVELNVLG FLLPVTAIIF FNYHILASLR
GQKEASRTRC GGPKGSKTTG LILTLVASFL VCWCPYHFFA FLDFLVQVRV IQDCSWKEIT
DLGLQLANFF AFVNSCLNPL IYVFAGRLLK TRVLGTL
