BKRB2_RAT
ID BKRB2_RAT Reviewed; 396 AA.
AC P25023;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=B2 bradykinin receptor;
DE Short=B2R;
DE Short=BK-2 receptor;
GN Name=Bdkrb2;
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 FUNCTION.
RC TISSUE=Uterus;
RX PubMed=1715575; DOI=10.1073/pnas.88.17.7724;
RA McEachern A.E., Shelton E.R., Bhakta S., Obernolte R., Bach C., Zuppan P.,
RA Fujisaki J., Aldrich R.W., Jarnagin K.;
RT "Expression cloning of a rat B2 bradykinin receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7724-7728(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT).
RC STRAIN=Sprague-Dawley;
RX PubMed=7929432; DOI=10.1016/s0021-9258(18)47107-4;
RA Pesquero J.B., Lindsey C.J., Zeh K., Paiva A.C.M., Ganten D., Bader M.;
RT "Molecular structure and expression of rat bradykinin B2 receptor gene.
RT Evidence for alternative splicing.";
RL J. Biol. Chem. 269:26920-26925(1994).
RN [3]
RP SEQUENCE REVISION.
RA Bader M.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT).
RC STRAIN=Sprague-Dawley;
RX PubMed=8086459; DOI=10.1016/0167-4781(94)90264-x;
RA Wang D.Z., Ma J.X., Chao L., Chao J.;
RT "Molecular cloning and sequence analysis of rat bradykinin B2 receptor
RT gene.";
RL Biochim. Biophys. Acta 1219:171-174(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
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 [6]
RP PROTEIN SEQUENCE OF 1-18.
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 [7]
RP PALMITOYLATION AT CYS-356, PHOSPHORYLATION AT TYR-161; TYR-352; SER-365;
RP SER-371; THR-374; SER-378 AND SER-380, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=10085087; DOI=10.1074/jbc.274.13.8539;
RA Soskic V., Nyakatura E., Roos M., Mueller-Esterl W., Godovac-Zimmermann J.;
RT "Correlations in palmitoylation and multiple phosphorylation of rat
RT bradykinin B2 receptor in Chinese hamster ovary cells.";
RL J. Biol. Chem. 274:8539-8545(1999).
CC -!- FUNCTION: Receptor for bradykinin. It is associated with G proteins
CC that activate a phosphatidylinositol-calcium second messenger system.
CC {ECO:0000269|PubMed:1715575}.
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=P25023-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P25023-2; Sequence=VSP_001867;
CC -!- TISSUE SPECIFICITY: Uterus, vas deferens, kidney, ileum, heart, testis,
CC lung and brain.
CC -!- PTM: Diphosphorylation at Ser-365 and Ser-371, at Ser-378 and Ser-380,
CC and at Thr-374 and Ser-380 seem to be correlated pairwise.
CC -!- PTM: Palmitoylation at Cys-356 and phosphorylation at Tyr-352 seem to
CC be mutually exclusive. {ECO:0000269|PubMed:10085087}.
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; M59967; AAA16425.1; -; mRNA.
DR EMBL; M59967; AAA16426.1; -; mRNA.
DR EMBL; X80187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X80188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X80189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X80190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L26173; AAA62492.1; -; Genomic_DNA.
DR EMBL; X69681; CAA49361.1; -; mRNA.
DR PIR; A41283; OORTB2.
DR RefSeq; NP_775123.2; NM_173100.2.
DR AlphaFoldDB; P25023; -.
DR SMR; P25023; -.
DR STRING; 10116.ENSRNOP00000064990; -.
DR BindingDB; P25023; -.
DR ChEMBL; CHEMBL2501; -.
DR DrugCentral; P25023; -.
DR GuidetoPHARMACOLOGY; 42; -.
DR GlyGen; P25023; 3 sites.
DR iPTMnet; P25023; -.
DR PhosphoSitePlus; P25023; -.
DR SwissPalm; P25023; -.
DR PaxDb; P25023; -.
DR PRIDE; P25023; -.
DR GeneID; 25245; -.
DR KEGG; rno:25245; -.
DR UCSC; RGD:2201; rat. [P25023-1]
DR CTD; 624; -.
DR RGD; 2201; Bdkrb2.
DR eggNOG; ENOG502QTX6; Eukaryota.
DR InParanoid; P25023; -.
DR OrthoDB; 837077at2759; -.
DR PhylomeDB; P25023; -.
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:P25023; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P25023; RN.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI: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:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; ISO:RGD.
DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IMP:RGD.
DR GO; GO:0050482; P:arachidonic acid secretion; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; IDA:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; ISO:RGD.
DR GO; GO:1902239; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator; ISO:RGD.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0009651; P:response to salt stress; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0019233; P:sensory perception of pain; TAS:RGD.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR GO; GO:0042311; P:vasodilation; ISO:RGD.
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 Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..396
FT /note="B2 bradykinin receptor"
FT /id="PRO_0000069194"
FT TOPO_DOM 1..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..89
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..123
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..158
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..203
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..253
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..340
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 161
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10085087"
FT MOD_RES 352
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:10085087"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10085087"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10085087"
FT MOD_RES 374
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10085087"
FT MOD_RES 378
FT /note="Phosphoserine; by GRK6"
FT /evidence="ECO:0000269|PubMed:10085087"
FT MOD_RES 380
FT /note="Phosphoserine; by GRK6"
FT /evidence="ECO:0000269|PubMed:10085087"
FT LIPID 356
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10085087"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 135..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8394991"
FT /id="VSP_001867"
FT CONFLICT 106
FT /note="A -> G (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 44930 MW; 535676FCA74E92B3 CRC64;
MDTRSSLCPK TQAVVAVFWG PGCHLSTCIE MFNITTQALG SAHNGTFSEV NCPDTEWWSW
LNAIQAPFLW VLFLLAALEN IFVLSVFCLH KTNCTVAEIY LGNLAAADLI LACGLPFWAI
TIANNFDWLF GEVLCRVVNT MIYMNLYSSI CFLMLVSIDR YLALVKTMSM GRMRGVRWAK
LYSLVIWSCT LLLSSPMLVF RTMKDYREEG HNVTACVIVY PSRSWEVFTN MLLNLVGFLL
PLSIITFCTV RIMQVLRNNE MKKFKEVQTE KKATVLVLAV LGLFVLCWFP FQISTFLDTL
LRLGVLSGCW NERAVDIVTQ ISSYVAYSNS CLNPLVYVIV GKRFRKKSRE VYQAICRKGG
CMGESVQMEN SMGTLRTSIS VDRQIHKLQD WAGNKQ
