BKRB2_HUMAN
ID BKRB2_HUMAN Reviewed; 391 AA.
AC P30411;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=B2 bradykinin receptor;
DE Short=B2R;
DE Short=BK-2 receptor;
GN Name=BDKRB2; Synonyms=BKR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=1314587; DOI=10.1016/0006-291x(92)91187-u;
RA Hess J.F.R., Borkowski J.A., Young G.S., Strader C.D., Ransom R.W.;
RT "Cloning and pharmacological characterization of a human bradykinin (BK-2)
RT receptor.";
RL Biochem. Biophys. Res. Commun. 184:260-268(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT).
RX PubMed=7916737; DOI=10.1006/geno.1993.1084;
RA Powell S.J., Slynn G., Thomas C., Hopkins B., Briggs I., Graham A.;
RT "Human bradykinin B2 receptor: nucleotide sequence analysis and assignment
RT to chromosome 14.";
RL Genomics 15:435-438(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=8394991;
RA McIntyre P., Phillips E., Skidmore E., Brown M., Webb M.;
RT "Cloned murine bradykinin receptor exhibits a mixed B1 and B2
RT pharmacological selectivity.";
RL Mol. Pharmacol. 44:346-355(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT), AND FUNCTION.
RX PubMed=1329734; DOI=10.1016/0006-291x(92)90445-q;
RA Eggerickx D., Raspe E., Bertrand D., Vassart G., Parmentier M.;
RT "Molecular cloning, functional expression and pharmacological
RT characterization of a human bradykinin B2 receptor gene.";
RL Biochem. Biophys. Res. Commun. 187:1306-1313(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), AND TISSUE SPECIFICITY.
RX PubMed=7835885; DOI=10.1006/geno.1994.1512;
RA Ma J.-X., Wang D.-Z., Ward D.C., Chen L., Dessai T., Chao J., Chao L.;
RT "Structure and chromosomal localization of the gene (BDKRB2) encoding human
RT bradykinin B2 receptor.";
RL Genomics 23:362-369(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT CYS-14.
RX PubMed=7779090; DOI=10.1006/bbrc.1995.1801;
RA Braun A., Kammerer S., Boehme E., Mueller B., Roscher A.A.;
RT "Identification of polymorphic sites of the human bradykinin B2 receptor
RT gene.";
RL Biochem. Biophys. Res. Commun. 211:234-240(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Lung;
RA Warren C.N., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-14 AND GLU-354.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 1-9 AND 17-30.
RC TISSUE=Foreskin;
RX PubMed=8652530; DOI=10.1021/bi9601060;
RA Abdalla S., Godovac-Zimmermann J., Braun A., Roscher A.A.,
RA Mueller-Esterl W., Quitterer U.;
RT "Structure of the bradykinin B2 receptors' amino terminus.";
RL Biochemistry 35:7514-7519(1996).
RN [11]
RP INTERACTION WITH PECAM1.
RX PubMed=18672896; DOI=10.1021/bi8003846;
RA Yeh J.C., Otte L.A., Frangos J.A.;
RT "Regulation of G protein-coupled receptor activities by the platelet-
RT endothelial cell adhesion molecule, PECAM-1.";
RL Biochemistry 47:9029-9039(2008).
RN [12]
RP PHOSPHORYLATION AT SER-373 AND SER-375.
RX PubMed=11517230; DOI=10.1074/jbc.m107024200;
RA Blaukat A., Pizard A., Breit A., Wernstedt C., Alhenc-Gelas F.,
RA Muller-Esterl W., Dikic I.;
RT "Determination of bradykinin B2 receptor in vivo phosphorylation sites and
RT their role in receptor function.";
RL J. Biol. Chem. 276:40431-40440(2001).
CC -!- FUNCTION: Receptor for bradykinin. It is associated with G proteins
CC that activate a phosphatidylinositol-calcium second messenger system.
CC {ECO:0000269|PubMed:1314587, ECO:0000269|PubMed:1329734}.
CC -!- SUBUNIT: Forms a complex with PECAM1 and GNAQ. Interacts with PECAM1.
CC {ECO:0000269|PubMed:18672896}.
CC -!- INTERACTION:
CC P30411; PRO_0000006688 [P01042]: KNG1; NbExp=2; IntAct=EBI-6623386, EBI-6623273;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:1314587};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P30411-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P30411-2; Sequence=VSP_001865;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Widespread in normal smooth muscle
CC tissue and neurons. {ECO:0000269|PubMed:7835885}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Bradykinin receptor subfamily. BDKRB2 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Bradykinin receptor entry;
CC URL="https://en.wikipedia.org/wiki/Bradykinin_receptor";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/bdkrb2/";
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DR EMBL; M88714; AAB02793.1; -; mRNA.
DR EMBL; S56772; AAB25765.1; -; Genomic_DNA.
DR EMBL; X69680; CAA49360.1; -; mRNA.
DR EMBL; S45489; AAB23467.1; -; Genomic_DNA.
DR EMBL; L27594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X86165; CAA60109.1; -; mRNA.
DR EMBL; X86164; CAA60108.1; -; mRNA.
DR EMBL; AY275465; AAP32297.1; -; mRNA.
DR EMBL; AF378542; AAK56376.1; -; Genomic_DNA.
DR EMBL; BC074894; AAH74894.1; -; mRNA.
DR EMBL; BC074895; AAH74895.1; -; mRNA.
DR CCDS; CCDS9942.1; -. [P30411-1]
DR PIR; JH0712; JQ1488.
DR RefSeq; NP_000614.1; NM_000623.3. [P30411-1]
DR PDB; 7F2O; EM; 2.90 A; R=40-370.
DR PDBsum; 7F2O; -.
DR AlphaFoldDB; P30411; -.
DR SMR; P30411; -.
DR BioGRID; 107093; 28.
DR IntAct; P30411; 33.
DR MINT; P30411; -.
DR STRING; 9606.ENSP00000450482; -.
DR BindingDB; P30411; -.
DR ChEMBL; CHEMBL3157; -.
DR DrugBank; DB05038; Anatibant.
DR DrugBank; DB06196; Icatibant.
DR DrugBank; DB06549; Labradimil.
DR DrugCentral; P30411; -.
DR GuidetoPHARMACOLOGY; 42; -.
DR TCDB; 9.A.14.13.27; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P30411; 3 sites.
DR iPTMnet; P30411; -.
DR PhosphoSitePlus; P30411; -.
DR SwissPalm; P30411; -.
DR BioMuta; BDKRB2; -.
DR DMDM; 2506481; -.
DR MassIVE; P30411; -.
DR MaxQB; P30411; -.
DR PaxDb; P30411; -.
DR PeptideAtlas; P30411; -.
DR PRIDE; P30411; -.
DR ProteomicsDB; 54664; -. [P30411-1]
DR ProteomicsDB; 54665; -. [P30411-2]
DR Antibodypedia; 14184; 265 antibodies from 35 providers.
DR DNASU; 624; -.
DR Ensembl; ENST00000539359.1; ENSP00000438376.1; ENSG00000168398.7. [P30411-2]
DR Ensembl; ENST00000542454.2; ENSP00000439459.2; ENSG00000168398.7. [P30411-2]
DR Ensembl; ENST00000554311.2; ENSP00000450482.1; ENSG00000168398.7. [P30411-1]
DR GeneID; 624; -.
DR KEGG; hsa:624; -.
DR MANE-Select; ENST00000554311.2; ENSP00000450482.1; NM_001379692.1; NP_001366621.1.
DR UCSC; uc001yfg.3; human. [P30411-1]
DR CTD; 624; -.
DR DisGeNET; 624; -.
DR GeneCards; BDKRB2; -.
DR HGNC; HGNC:1030; BDKRB2.
DR HPA; ENSG00000168398; Tissue enhanced (urinary).
DR MIM; 113503; gene.
DR neXtProt; NX_P30411; -.
DR OpenTargets; ENSG00000168398; -.
DR PharmGKB; PA80; -.
DR VEuPathDB; HostDB:ENSG00000168398; -.
DR eggNOG; ENOG502QTX6; Eukaryota.
DR GeneTree; ENSGT01030000234534; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P30411; -.
DR OMA; HKSRCTV; -.
DR OrthoDB; 826485at2759; -.
DR PhylomeDB; P30411; -.
DR TreeFam; TF330024; -.
DR PathwayCommons; P30411; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P30411; -.
DR SIGNOR; P30411; -.
DR BioGRID-ORCS; 624; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; BDKRB2; human.
DR GeneWiki; Bradykinin_receptor_B2; -.
DR GenomeRNAi; 624; -.
DR Pharos; P30411; Tclin.
DR PRO; PR:P30411; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P30411; protein.
DR Bgee; ENSG00000168398; Expressed in stromal cell of endometrium and 144 other tissues.
DR Genevisible; P30411; HS.
DR GO; GO:0005768; C:endosome; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0004947; F:bradykinin receptor activity; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; TAS:ProtInc.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; IPI:BHF-UCL.
DR GO; GO:0050482; P:arachidonic acid secretion; IDA:BHF-UCL.
DR GO; GO:0008015; P:blood circulation; NAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IC:BHF-UCL.
DR GO; GO:1990127; P:intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator; IEA:Ensembl.
DR GO; GO:1902239; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator; IEA:Ensembl.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; TAS:ProtInc.
DR GO; GO:0043114; P:regulation of vascular permeability; IC:BHF-UCL.
DR GO; GO:0019229; P:regulation of vasoconstriction; IC:BHF-UCL.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0006939; P:smooth muscle contraction; IC:BHF-UCL.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
DR InterPro; IPR001504; Brdyknn_2_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; PR00994; BRADYKINNB2R.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..391
FT /note="B2 bradykinin receptor"
FT /id="PRO_0000069190"
FT TOPO_DOM 1..60
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..118
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..198
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..221
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..248
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..292
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..335
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 156
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 347
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 369
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 373
FT /note="Phosphoserine; by GRK6"
FT /evidence="ECO:0000269|PubMed:11517230"
FT MOD_RES 375
FT /note="Phosphoserine; by GRK6"
FT /evidence="ECO:0000269|PubMed:11517230"
FT LIPID 351
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 130..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:1314587,
FT ECO:0000303|PubMed:8394991"
FT /id="VSP_001865"
FT VARIANT 14
FT /note="R -> C (in dbSNP:rs1046248)"
FT /evidence="ECO:0000269|PubMed:7779090, ECO:0000269|Ref.8"
FT /id="VAR_003457"
FT VARIANT 354
FT /note="G -> E (in dbSNP:rs2227279)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_012284"
FT HELIX 56..84
FT /evidence="ECO:0007829|PDB:7F2O"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7F2O"
FT HELIX 91..118
FT /evidence="ECO:0007829|PDB:7F2O"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:7F2O"
FT HELIX 126..159
FT /evidence="ECO:0007829|PDB:7F2O"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:7F2O"
FT HELIX 171..195
FT /evidence="ECO:0007829|PDB:7F2O"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:7F2O"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:7F2O"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:7F2O"
FT HELIX 234..256
FT /evidence="ECO:0007829|PDB:7F2O"
FT HELIX 264..298
FT /evidence="ECO:0007829|PDB:7F2O"
FT HELIX 304..321
FT /evidence="ECO:0007829|PDB:7F2O"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:7F2O"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:7F2O"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:7F2O"
SQ SEQUENCE 391 AA; 44461 MW; 066940ED3D18BB66 CRC64;
MFSPWKISMF LSVREDSVPT TASFSADMLN VTLQGPTLNG TFAQSKCPQV EWLGWLNTIQ
PPFLWVLFVL ATLENIFVLS VFCLHKSSCT VAEIYLGNLA AADLILACGL PFWAITISNN
FDWLFGETLC RVVNAIISMN LYSSICFLML VSIDRYLALV KTMSMGRMRG VRWAKLYSLV
IWGCTLLLSS PMLVFRTMKE YSDEGHNVTA CVISYPSLIW EVFTNMLLNV VGFLLPLSVI
TFCTMQIMQV LRNNEMQKFK EIQTERRATV LVLVVLLLFI ICWLPFQIST FLDTLHRLGI
LSSCQDERII DVITQIASFM AYSNSCLNPL VYVIVGKRFR KKSWEVYQGV CQKGGCRSEP
IQMENSMGTL RTSISVERQI HKLQDWAGSR Q
