ID BKRB2_MOUSE Reviewed; 392 AA. AC P32299; B9EHE3; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 4. DT 27-MAR-2024, entry version 184. DE RecName: Full=B2 bradykinin receptor; DE Short=B2R; DE Short=BK-2 receptor; GN Name=Bdkrb2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM SHORT), AND FUNCTION. RC STRAIN=C57BL/6J; 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 [2] RP NUCLEOTIDE SEQUENCE (ISOFORM SHORT), AND FUNCTION. RC STRAIN=129/J; RX PubMed=8302267; RA Hess J.F.R., Borkowski J.A., Macneil T., Stonesifer G.Y., Fraher J., RA Strader C.D., Ransom R.W.; RT "Differential pharmacology of cloned human and mouse B2 bradykinin RT receptors."; RL Mol. Pharmacol. 45:1-8(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). RC STRAIN=A/J; RX PubMed=8166739; DOI=10.1006/bbrc.1994.1495; RA Yokoyama S., Kimura Y., Taketo M., Black J.A., Ransom B.R., Higashida H.; RT "B2 bradykinin receptors in NG108-15 cells: cDNA cloning and functional RT expression."; RL Biochem. Biophys. Res. Commun. 200:634-641(1994). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7959003; DOI=10.1016/0378-1119(94)90162-7; RA Ma J.X., Wang D.Z., Chao L., Chao J.; RT "Cloning, sequence analysis and expression of the gene encoding the mouse RT bradykinin B2 receptor."; RL Gene 149:283-288(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RC TISSUE=Testis; 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 [6] RP IDENTIFICATION OF LONG FORM. 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). CC -!- FUNCTION: Receptor for bradykinin. It is associated with G proteins CC that activate a phosphatidylinositol-calcium second messenger system. CC {ECO:0000269|PubMed:8302267, ECO:0000269|PubMed:8394991}. CC -!- SUBUNIT: Forms a complex with PECAM1 and GNAQ. Interacts with PECAM1 CC (By similarity). {ECO:0000250|UniProtKB:P30411}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30411}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P32299-1; Sequence=Displayed; CC Name=Short; CC IsoId=P32299-2; Sequence=VSP_001866; 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 --------------------------------------------------------------------------- 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; X69676; CAA49357.1; -; Genomic_DNA. DR EMBL; X69682; CAA49362.1; -; mRNA. DR EMBL; L26047; AAA19797.1; -; Unassigned_DNA. DR EMBL; X78438; CAA55202.1; -; mRNA. DR EMBL; L27595; AAA62616.1; -; Genomic_DNA. DR EMBL; BC137755; AAI37756.1; -; mRNA. DR CCDS; CCDS49160.1; -. [P32299-1] DR PIR; I49519; I49519. DR RefSeq; NP_033877.3; NM_009747.2. [P32299-1] DR RefSeq; XP_006515505.1; XM_006515442.3. [P32299-1] DR AlphaFoldDB; P32299; -. DR SMR; P32299; -. DR STRING; 10090.ENSMUSP00000001652; -. DR DrugCentral; P32299; -. DR GuidetoPHARMACOLOGY; 42; -. DR GlyCosmos; P32299; 3 sites, No reported glycans. DR GlyGen; P32299; 3 sites. DR iPTMnet; P32299; -. DR PhosphoSitePlus; P32299; -. DR SwissPalm; P32299; -. DR PaxDb; 10090-ENSMUSP00000001652; -. DR ProteomicsDB; 273496; -. [P32299-1] DR ProteomicsDB; 273497; -. [P32299-2] DR Antibodypedia; 14184; 335 antibodies from 35 providers. DR DNASU; 12062; -. DR Ensembl; ENSMUST00000001652.7; ENSMUSP00000001652.6; ENSMUSG00000021070.7. [P32299-1] DR GeneID; 12062; -. DR KEGG; mmu:12062; -. DR UCSC; uc007oym.1; mouse. [P32299-1] DR AGR; MGI:102845; -. DR CTD; 624; -. DR MGI; MGI:102845; Bdkrb2. DR VEuPathDB; HostDB:ENSMUSG00000021070; -. DR eggNOG; ENOG502QTX6; Eukaryota. DR GeneTree; ENSGT01030000234534; -. DR HOGENOM; CLU_009579_8_3_1; -. DR InParanoid; P32299; -. DR OMA; LAFRTMK; -. DR OrthoDB; 4066805at2759; -. DR PhylomeDB; P32299; -. DR TreeFam; TF330024; -. DR Reactome; R-MMU-375276; Peptide ligand-binding receptors. DR Reactome; R-MMU-416476; G alpha (q) signalling events. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR BioGRID-ORCS; 12062; 1 hit in 78 CRISPR screens. DR ChiTaRS; Bdkrb2; mouse. DR PRO; PR:P32299; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; P32299; Protein. DR Bgee; ENSMUSG00000021070; Expressed in esophagus and 40 other cell types or tissues. DR GO; GO:0005768; C:endosome; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI. DR GO; GO:0004947; F:bradykinin receptor activity; ISO:MGI. DR GO; GO:0002020; F:protease binding; ISO:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0031702; F:type 1 angiotensin receptor binding; ISO:MGI. DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; ISO:MGI. DR GO; GO:0050482; P:arachidonic acid secretion; ISO:MGI. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:1990127; P:intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator; IGI:MGI. DR GO; GO:0035633; P:maintenance of blood-brain barrier; ISO:MGI. DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI. DR GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IMP:MGI. DR GO; GO:1902239; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator; IGI:MGI. DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:MGI. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI. DR GO; GO:0009651; P:response to salt stress; IGI:MGI. DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro. DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro. DR GO; GO:0042311; P:vasodilation; IMP:MGI. 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; P32299; MM. PE 2: Evidence at transcript level; KW Alternative splicing; Cell membrane; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate; KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1..392 FT /note="B2 bradykinin receptor" FT /id="PRO_0000069191" FT TOPO_DOM 1..61 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 62..85 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 86..94 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 95..119 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 120..132 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 133..154 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 155..176 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 177..199 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 200..222 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 223..249 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 250..268 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 269..293 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 294..312 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 313..336 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 337..392 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOD_RES 157 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P25023" FT MOD_RES 348 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P25023" FT MOD_RES 367 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25023" FT MOD_RES 370 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P25023" FT MOD_RES 374 FT /note="Phosphoserine; by GRK6" FT /evidence="ECO:0000250|UniProtKB:P30411" FT MOD_RES 376 FT /note="Phosphoserine; by GRK6" FT /evidence="ECO:0000250|UniProtKB:P30411" FT LIPID 352 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000255" FT CARBOHYD 29 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 40 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 208 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 131..212 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VAR_SEQ 1..26 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000303|PubMed:8166739, FT ECO:0000303|PubMed:8394991" FT /id="VSP_001866" FT CONFLICT 298 FT /note="R -> A (in Ref. 1 and 4)" FT /evidence="ECO:0000305" SQ SEQUENCE 392 AA; 44389 MW; FB1AA59BCBFFF5F9 CRC64; MPCSWKLLGF LSVHEPMPTA ASFGIEMFNV TTQVLGSALN GTLSKDNCPD TEWWSWLNAI QAPFLWVLFL LAALENLFVL SVFFLHKNSC TVAEIYLGNL AAADLILACG LPFWAITIAN NFDWVFGEVL CRVVNTMIYM NLYSSICFLM LVSIDRYLAL VKTMSMGRMR GVRWAKLYSL VIWGCTLLLS SPMLVFRTMR EYSEEGHNVT ACVIVYPSRS WEVFTNVLLN LVGFLLPLSV ITFCTVRILQ VLRNNEMKKF KEVQTERKAT VLVLAVLGLF VLCWVPFQIS TFLDTLLRLG VLSGCWDEHA VDVITQISSY VAYSNSGLNP LVYVIVGKRF RKKSREVYRV LCQKGGCMGE PVQMENSMGT LRTSISVERQ IHKLQDWAGK KQ //