BKRB2_RABIT
ID BKRB2_RABIT Reviewed; 367 AA.
AC Q28642;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=B2 bradykinin receptor;
DE Short=B2R;
DE Short=BK-2 receptor;
GN Name=BDKRB2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=8531137;
RA Bachvarov D.R., Saint-Jacques E., Larrivee J.F., Levesque L., Rioux F.,
RA Drapeau G., Marceau F.;
RT "Cloning and pharmacological characterization of the rabbit bradykinin B2
RT receptor.";
RL J. Pharmacol. Exp. Ther. 275:1623-1630(1995).
CC -!- FUNCTION: Receptor for bradykinin. It is associated with G proteins
CC that activate a phosphatidylinositol-calcium second messenger system.
CC {ECO:0000269|PubMed:8531137}.
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 -!- 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; U33334; AAA96149.1; -; Genomic_DNA.
DR AlphaFoldDB; Q28642; -.
DR SMR; Q28642; -.
DR STRING; 9986.ENSOCUP00000012746; -.
DR BindingDB; Q28642; -.
DR ChEMBL; CHEMBL3453; -.
DR eggNOG; ENOG502QTX6; Eukaryota.
DR InParanoid; Q28642; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004947; F:bradykinin receptor activity; IEA:InterPro.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..367
FT /note="B2 bradykinin receptor"
FT /id="PRO_0000069193"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..311
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 323
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 349
FT /note="Phosphoserine; by GRK6"
FT /evidence="ECO:0000250|UniProtKB:P30411"
FT MOD_RES 351
FT /note="Phosphoserine; by GRK6"
FT /evidence="ECO:0000250|UniProtKB:P30411"
FT LIPID 327
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 367 AA; 41480 MW; EF12A2A3A6FD9FC8 CRC64;
MLNITSQVLA PALNGSVSQS SGCPNTEWSG WLNVIQAPFL WVLFVLATLE NLFVLSVFCL
HKSSCTVAEV YLGNLAAADL ILACGLPFWA VTIANHFDWL FGEALCRVVN TMIYMNLYSS
ICFLMLVSID RYLALVKTMS IGRMRRVRWA KLYSLVIWGC TLLLSSPMLV FRTMKDYRDE
GYNVTACIID YPSRSWEVFT NVLLNLVGFL LPLSVITFCT VQILQVLRNN EMQKFKEIQT
ERRATVLVLA VLLLFVVCWL PFQVSTFLDT LLKLGVLSSC WDEHVIDVIT QVGSFMGYSN
SCLNPLVYVI VGKRFRKKSR EVYRAACPKA GCVLEPVQAE SSMGTLRTSI SVERQIHKLP
EWTRSSQ
