BKRB2_MOUSE
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 03-AUG-2022, entry version 175.
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}.
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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 GlyGen; P32299; 3 sites.
DR iPTMnet; P32299; -.
DR PhosphoSitePlus; P32299; -.
DR SwissPalm; P32299; -.
DR PaxDb; P32299; -.
DR PRIDE; P32299; -.
DR ProteomicsDB; 273496; -. [P32299-1]
DR ProteomicsDB; 273497; -. [P32299-2]
DR Antibodypedia; 14184; 265 antibodies from 35 providers.
DR DNASU; 12062; -.
DR Ensembl; ENSMUST00000001652; ENSMUSP00000001652; ENSMUSG00000021070. [P32299-1]
DR GeneID; 12062; -.
DR KEGG; mmu:12062; -.
DR UCSC; uc007oym.1; mouse. [P32299-1]
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; HKSRCTV; -.
DR OrthoDB; 826485at2759; -.
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; 0 hits in 73 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 38 other tissues.
DR Genevisible; P32299; MM.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
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 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 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
