ID A0A0D9RDX3_CHLSB Unreviewed; 391 AA.
AC A0A0D9RDX3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=B2 bradykinin receptor {ECO:0000256|ARBA:ARBA00013512};
GN Name=BDKRB2 {ECO:0000313|Ensembl:ENSCSAP00000006812.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000006812.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000006812.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000006812.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for bradykinin. It is associated with G proteins
CC that activate a phosphatidylinositol-calcium second messenger system.
CC {ECO:0000256|ARBA:ARBA00025423}.
CC -!- SUBUNIT: Forms a complex with PECAM1 and GNAQ. Interacts with PECAM1.
CC {ECO:0000256|ARBA:ARBA00025954}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
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DR EMBL; AQIB01046263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007985950.1; XM_007987759.1.
DR RefSeq; XP_007985951.1; XM_007987760.1.
DR RefSeq; XP_007985952.1; XM_007987761.1.
DR AlphaFoldDB; A0A0D9RDX3; -.
DR STRING; 60711.ENSCSAP00000006812; -.
DR Ensembl; ENSCSAT00000008665.1; ENSCSAP00000006812.1; ENSCSAG00000010582.1.
DR GeneID; 103229642; -.
DR KEGG; csab:103229642; -.
DR CTD; 624; -.
DR eggNOG; ENOG502QTX6; Eukaryota.
DR GeneTree; ENSGT01030000234534; -.
DR OMA; LAFRTMK; -.
DR OrthoDB; 4066805at2759; -.
DR BioGRID-ORCS; 103229642; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 24.
DR Bgee; ENSCSAG00000010582; Expressed in fibroblast and 2 other cell types or tissues.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004947; F:bradykinin receptor activity; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; IEA:Ensembl.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl.
DR GO; GO:1990127; P:intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator; IEA:Ensembl.
DR GO; GO:1902239; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator; IEA:Ensembl.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..332
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 391 AA; 44478 MW; 99696501D298AAAD CRC64;
MFSPWKSPMF LSVREDSVPT TASFSADMLN VTLQLPALNG TFAQSKCPQV EWLGWLNTIQ
APFLWVLFVL ATLENIFVLS VFCLHRSSCT VAEIYLGNLA AADLILACGL PFWAITISNN
FDWLFGETLC RVVNAITSMN LYSSICFLML VSIDRYLALV KTMSMGRMRG VRWAKLYSLV
IWACTLLLSS PMLVFRTMEE YSDEGHNVTA CVISYPSFIW EVFTNMLLNI VGFLLPLSVI
TFCTMQIMQV LRNNEMQKFK EIQTERRATV LVLVVLLLFV ICWLPFQVST FLDTLHRLGI
LASCRDEHII DVITQIASFM AYSNSCLNPL VYVIVGKRFR KKSWEVYQGV CQKGGCRSES
IQMENSMGTL RTSISVERQI HKLQDWAGSR Q
//