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BKRB1_PIG
ID   BKRB1_PIG               Reviewed;         353 AA.
AC   Q8HZN9;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=B1 bradykinin receptor;
DE            Short=B1R;
DE            Short=BK-1 receptor;
GN   Name=BDKRB1;
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 [GENOMIC DNA].
RA   Horlick R.A., Zhao J., Swanson R.N., Webb M.L., Strohl B., Baldwin J.J.,
RA   Auld D.S.;
RT   "Orthologs of human receptors and methods of use.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This is a receptor for bradykinin. Could be a factor in
CC       chronic pain and inflammation. {ECO:0000250|UniProtKB:P46663}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P46663};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Bradykinin receptor subfamily. BDKRB1 sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF540788; AAN16467.1; -; Genomic_DNA.
DR   RefSeq; NP_001106535.1; NM_001113064.1.
DR   AlphaFoldDB; Q8HZN9; -.
DR   SMR; Q8HZN9; -.
DR   STRING; 9823.ENSSSCP00000002708; -.
DR   PaxDb; Q8HZN9; -.
DR   GeneID; 100127469; -.
DR   KEGG; ssc:100127469; -.
DR   CTD; 623; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q8HZN9; -.
DR   OrthoDB; 951204at2759; -.
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:0019371; P:cyclooxygenase pathway; IMP:AgBase.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:InterPro.
DR   GO; GO:0060085; P:smooth muscle relaxation of the bladder outlet; IMP:AgBase.
DR   InterPro; IPR001186; Brdyknn_1_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; PR00993; BRADYKINNB1R.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..353
FT                   /note="B1 bradykinin receptor"
FT                   /id="PRO_0000069185"
FT   TOPO_DOM        1..41
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..251
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..295
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..353
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           330
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        109..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   353 AA;  40146 MW;  D496CC6C54EDD88F CRC64;
     MASQTLVVFQ ASNQSQLPPP NATLCDGAQE AWHLLHKVLP TCVVAICSGG LLGNLFVLSV
     FLVPRRRLNA AEIYLAHLAA SDLVFALGLP FWAETIRNGF HWPFGAPLCR VVNGVIKANL
     FISIFLVVAI SRDRYRALVH PVASWRRRRR RHWAQATCVL IWTAGGLLSI PTFLLRSVQV
     VPELNVSACV LPFPHEAWAF VRTVELNVLG FLLPLAAILF FNYHILAALR GREQLSRTRC
     GGPRDGKTTA LILTLVAVFL LCWTPYHVCA FLEFLLHVRA IRGCFWEDFT DLGLQYTNFF
     AFINSCLNPV IYVFWGQLFR TKIWELYHRC LPRKLTAVSS SRRKEIFQIF WRN
 
 
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