BKRB2_PIG
ID BKRB2_PIG Reviewed; 367 AA.
AC Q9GLX8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=B2 bradykinin receptor;
DE Short=B2R;
DE Short=BK-2 receptor;
GN Name=BDKRB2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11673263; DOI=10.1095/biolreprod65.5.1462;
RA Kimura A., Kihara T., Ohkura R., Ogiwara K., Takahashi T.;
RT "Localization of bradykinin B(2) receptor in the follicles of porcine ovary
RT and increased expression of matrix metalloproteinase-3 and -20 in cultured
RT granulosa cells by bradykinin treatment.";
RL Biol. Reprod. 65:1462-1470(2001).
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; AB051422; BAB18462.1; -; mRNA.
DR RefSeq; NP_999311.1; NM_214146.1.
DR AlphaFoldDB; Q9GLX8; -.
DR SMR; Q9GLX8; -.
DR STRING; 9823.ENSSSCP00000025411; -.
DR PaxDb; Q9GLX8; -.
DR PRIDE; Q9GLX8; -.
DR GeneID; 110255240; -.
DR CTD; 624; -.
DR eggNOG; ENOG502QTX6; Eukaryota.
DR InParanoid; Q9GLX8; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004947; F:bradykinin receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IMP:AgBase.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IMP:AgBase.
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..367
FT /note="B2 bradykinin receptor"
FT /id="PRO_0000069192"
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; 41781 MW; 17F7C2A5936D409B CRC64;
MLNLTSQVPE PALNGTLPQS SSCFHSDWWN WLNTIQAPFL WVLFLLAALE NIFVLSVFCL
HKNSCTVAEI YLGNLAMADL ILALGLPFWA ITIANHFDWL FGEVLCRVVN TMIYMNLYSS
ICFLMLVSID RYLALVKTMS MGRMRGVRWA KLYSLVIWGC TLLLSSPMLA FRTMHEYAAE
GHNVTACIIK YPSRSWMVFT NILLNSVGFL LPLSIITYCT VQILQVLRNN EMQKFKEIQT
ERKATVLVLA VLLLFVVCWL PFQISTFLDT LLRLGVLSGC WDEHAVDVIT QISSYVAYSN
SGLNPLVYVI VGKRFRKKSR EVYRVLCQKG GCMGEPVQME NSMGTLRTSI SVERQIHKLQ
DWAGKKQ
