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BKRB1_RABIT
ID   BKRB1_RABIT             Reviewed;         352 AA.
AC   P48748;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=B1 bradykinin receptor;
DE            Short=B1R;
DE            Short=BK-1 receptor;
GN   Name=BDKRB1;
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 [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Aorta;
RX   PubMed=7495867; DOI=10.1016/0167-4781(95)00152-7;
RA   Macneil T., Bierilo K.K., Menke J.G., Hess J.F.;
RT   "Cloning and pharmacological characterization of a rabbit bradykinin B1
RT   receptor.";
RL   Biochim. Biophys. Acta 1264:223-228(1995).
CC   -!- FUNCTION: This is a receptor for bradykinin. Could be a factor in
CC       chronic pain and inflammation. {ECO:0000269|PubMed:7495867}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P46663};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- INDUCTION: In response to tissue injury.
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; U20507; AAC48482.1; -; mRNA.
DR   PIR; S60024; S60024.
DR   RefSeq; NP_001075816.1; NM_001082347.1.
DR   AlphaFoldDB; P48748; -.
DR   SMR; P48748; -.
DR   STRING; 9986.ENSOCUP00000022849; -.
DR   BindingDB; P48748; -.
DR   ChEMBL; CHEMBL4087; -.
DR   GeneID; 100009198; -.
DR   KEGG; ocu:100009198; -.
DR   CTD; 623; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; P48748; -.
DR   OrthoDB; 826485at2759; -.
DR   PRO; PR:P48748; -.
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:0006954; P:inflammatory response; IEA:InterPro.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:InterPro.
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   2: Evidence at transcript level;
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..352
FT                   /note="B1 bradykinin receptor"
FT                   /id="PRO_0000069186"
FT   TOPO_DOM        1..39
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..63
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..97
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..132
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..177
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..225
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..246
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..271
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..290
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..314
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        315..352
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           329
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        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        109..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   352 AA;  39503 MW;  492AD177258853CD CRC64;
     MASQGPLELQ PSNQSQLAPP NATSCSGAPD AWDLLHRLLP TFIIAIFTLG LLGNSFVLSV
     FLLARRRLSV AEIYLANLAA SDLVFVLGLP FWAENVRNQF DWPFGAALCR IVNGVIKANL
     FISIFLVVAI SQDRYSVLVH PMASRRGRRR RQAQATCALI WLAGGLLSTP TFVLRSVRAV
     PELNVSACIL LLPHEAWHWL RMVELNLLGF LLPLAAILFF NCHILASLRR RGERVPSRCG
     GPRDSKSTAL ILTLVASFLV CWAPYHFFAF LECLWQVHAI GGCFWEEFTD LGLQLSNFSA
     FVNSCLNPVI YVFVGRLFRT KVWELCQQCS PRSLAPVSSS RRKEMLWGFW RN
 
 
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