BKRB2_CAVPO
ID BKRB2_CAVPO Reviewed; 372 AA.
AC O70526;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=B2 bradykinin receptor;
DE Short=B2R;
DE Short=BK-2 receptor;
GN Name=BDKRB2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Lung;
RX PubMed=9652372; DOI=10.1016/s0014-2999(98)00024-7;
RA Farmer S.G., Powell S.J., Wilkins D.E., Graham A.;
RT "Cloning, sequencing and functional expression of a guinea pig lung
RT bradykinin B2 receptor.";
RL Eur. J. Pharmacol. 346:291-298(1998).
CC -!- FUNCTION: Receptor for bradykinin. It is associated with G proteins
CC that activate a phosphatidylinositol-calcium second messenger system
CC (By similarity). {ECO:0000250|UniProtKB:P30411}.
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}.
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DR EMBL; AJ003243; CAA06025.1; -; mRNA.
DR RefSeq; NP_001166391.1; NM_001172920.1.
DR AlphaFoldDB; O70526; -.
DR SMR; O70526; -.
DR STRING; 10141.ENSCPOP00000020477; -.
DR BindingDB; O70526; -.
DR ChEMBL; CHEMBL4111; -.
DR DrugCentral; O70526; -.
DR GeneID; 100135486; -.
DR KEGG; cpoc:100135486; -.
DR CTD; 624; -.
DR eggNOG; ENOG502QTX6; Eukaryota.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; O70526; -.
DR OMA; HKSRCTV; -.
DR TreeFam; TF330024; -.
DR PRO; PR:O70526; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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 2: Evidence at transcript level;
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..372
FT /note="B2 bradykinin receptor"
FT /id="PRO_0000069189"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 130
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 320
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25023"
FT MOD_RES 346
FT /note="Phosphoserine; by GRK6"
FT /evidence="ECO:0000250|UniProtKB:P30411"
FT MOD_RES 348
FT /note="Phosphoserine; by GRK6"
FT /evidence="ECO:0000250|UniProtKB:P30411"
FT LIPID 324
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 372 AA; 42210 MW; 8B736B50887DAE67 CRC64;
MFNITSQVSA LNATLAQGNS CLDAEWWSWL NTIQAPFLWV LFVLAVLENI FVLSVFFLHK
SSCTVAEIYL GNLAVADLIL AFGLPFWAIT IANNFDWLFG EVLCRMVNTM IQMNMYSSIC
FLMLVSIDRY LALVKTMSMG RMRGVRWAKL YSLVIWGCAL LLSSPMLVFR TMKDYRDEGH
NVTACLIIYP SLTWQVFTNV LLNLVGFLLP LSIITFCTVQ IMQVLRNNEM QKFKEIQTER
RATVLVLAVL LLFVVCWLPF QIGTFLDTLR LLGFLPGCWE HVIDLITQIS SYLAYSNSCL
NPLVYVIVGK RFRKKSREVY HGLCRSGGCV SEPAQSENSM GTLRTSISVD RQIHKLQDWA
RSSSEGTPPG LL
