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 27-MAR-2024, entry version 212. 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7F6H; EM; 2.90 A; A=25-391. DR PDB; 7F6I; EM; 2.80 A; A=25-391. DR PDBsum; 7F2O; -. DR PDBsum; 7F6H; -. DR PDBsum; 7F6I; -. DR AlphaFoldDB; P30411; -. DR EMDB; EMD-31429; -. DR EMDB; EMD-31480; -. DR EMDB; EMD-31481; -. 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 GlyCosmos; P30411; 3 sites, No reported glycans. 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; 9606-ENSP00000450482; -. DR PeptideAtlas; P30411; -. DR ProteomicsDB; 54664; -. [P30411-1] DR ProteomicsDB; 54665; -. [P30411-2] DR Antibodypedia; 14184; 335 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 AGR; HGNC:1030; -. 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; LAFRTMK; -. DR OrthoDB; 4066805at2759; -. 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 1155 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 145 other cell types or tissues. DR GO; GO:0005768; C:endosome; IDA:BHF-UCL. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. 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: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; IDA:UniProt. DR CDD; cd15381; 7tmA_BK-2; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR001504; Brdyknn_2_rcpt. DR InterPro; IPR000496; Brdyknn_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR10489:SF948; B2 BRADYKININ RECEPTOR; 1. DR PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00425; BRADYKININR. DR PRINTS; PR00994; BRADYKINNB2R. DR PRINTS; PR00237; GPCRRHODOPSN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; P30411; HS. 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 51..84 FT /evidence="ECO:0007829|PDB:7F6I" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 91..107 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 110..118 FT /evidence="ECO:0007829|PDB:7F6I" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:7F2O" FT HELIX 126..159 FT /evidence="ECO:0007829|PDB:7F6I" FT TURN 162..165 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 171..188 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 190..194 FT /evidence="ECO:0007829|PDB:7F6I" FT STRAND 195..201 FT /evidence="ECO:0007829|PDB:7F6I" FT STRAND 208..213 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 218..229 FT /evidence="ECO:0007829|PDB:7F6I" FT TURN 230..233 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 234..251 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 265..297 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 304..320 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 323..332 FT /evidence="ECO:0007829|PDB:7F6I" FT TURN 333..335 FT /evidence="ECO:0007829|PDB:7F6I" FT HELIX 337..350 FT /evidence="ECO:0007829|PDB:7F6I" 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 //