位置:首页 > 蛋白库 > BKRB1_HUMAN
BKRB1_HUMAN
ID   BKRB1_HUMAN             Reviewed;         353 AA.
AC   P46663; A8K7F5; Q546S7; Q8N0Y8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 3.
DT   03-AUG-2022, entry version 190.
DE   RecName: Full=B1 bradykinin receptor;
DE            Short=B1R;
DE            Short=BK-1 receptor;
GN   Name=BDKRB1; Synonyms=BRADYB1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=8063797; DOI=10.1016/s0021-9258(17)31844-6;
RA   Menke J.G., Borkowski J.A., Bierilo K.K., Macneil T., Derrick A.W.,
RA   Schneck K.A., Ransom R.W., Strader C.D., Linemeyer D.L., Hess J.F.;
RT   "Expression cloning of a human B1 bradykinin receptor.";
RL   J. Biol. Chem. 269:21583-21586(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8651911; DOI=10.1006/bbrc.1996.0810;
RA   Yang X., Polgar P.;
RT   "Genomic structure of the human bradykinin B1 receptor gene and preliminary
RT   characterization of its regulatory regions.";
RL   Biochem. Biophys. Res. Commun. 222:718-725(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8660997; DOI=10.1006/geno.1996.0213;
RA   Bachvarov D.R., Hess J.F., Menke J.G., Larrivee J.F., Marceau F.;
RT   "Structure and genomic organization of the human B1 receptor gene for
RT   kinins (BDKRB1).";
RL   Genomics 33:374-381(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Lung;
RX   PubMed=10422787; DOI=10.1016/s0014-2999(99)00315-5;
RA   Jones C., Phillips E., Davis C., Arbuckle J., Yaqoob M., Burgess G.M.,
RA   Docherty R.J., Webb M., Bevan S.J., McIntyre P.;
RT   "Molecular characterisation of cloned bradykinin B1 receptors from rat and
RT   human.";
RL   Eur. J. Pharmacol. 374:423-433(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA   Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT   "Genome-wide discovery and analysis of human seven transmembrane helix
RT   receptor genes.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Warren C.N., Aronstam R.S., Sharma S.V.;
RT   "Isolation of complete coding sequence for bradykinin receptor B1
RT   (BDKRB1).";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: This is a receptor for bradykinin. Could be a factor in
CC       chronic pain and inflammation. {ECO:0000269|PubMed:8063797,
CC       ECO:0000269|PubMed:8660997}.
CC   -!- INTERACTION:
CC       P46663; PRO_0000006687 [P01042]: KNG1; NbExp=2; IntAct=EBI-6623218, EBI-6623250;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8063797};
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}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Bradykinin receptor entry;
CC       URL="https://en.wikipedia.org/wiki/Bradykinin_receptor";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U12512; AAA21346.1; -; mRNA.
DR   EMBL; U22346; AAC50594.1; -; Genomic_DNA.
DR   EMBL; U48231; AAB60693.1; -; Genomic_DNA.
DR   EMBL; AJ238044; CAB45650.1; -; mRNA.
DR   EMBL; AB065896; BAC06112.1; -; Genomic_DNA.
DR   EMBL; AY275464; AAP32296.1; -; Genomic_DNA.
DR   EMBL; AK291970; BAF84659.1; -; mRNA.
DR   EMBL; CH471061; EAW81632.1; -; Genomic_DNA.
DR   EMBL; BC034705; AAH34705.1; -; mRNA.
DR   CCDS; CCDS9943.1; -.
DR   PIR; A53858; A53858.
DR   RefSeq; NP_000701.2; NM_000710.3.
DR   PDB; 7EIB; EM; 3.00 A; A=2-350.
DR   PDBsum; 7EIB; -.
DR   AlphaFoldDB; P46663; -.
DR   SMR; P46663; -.
DR   BioGRID; 107092; 32.
DR   IntAct; P46663; 32.
DR   MINT; P46663; -.
DR   STRING; 9606.ENSP00000216629; -.
DR   BindingDB; P46663; -.
DR   ChEMBL; CHEMBL4308; -.
DR   DrugBank; DB01197; Captopril.
DR   DrugBank; DB09477; Enalaprilat.
DR   DrugBank; DB00178; Ramipril.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   DrugCentral; P46663; -.
DR   GuidetoPHARMACOLOGY; 41; -.
DR   GlyGen; P46663; 3 sites.
DR   iPTMnet; P46663; -.
DR   PhosphoSitePlus; P46663; -.
DR   BioMuta; BDKRB1; -.
DR   DMDM; 85681914; -.
DR   MassIVE; P46663; -.
DR   PaxDb; P46663; -.
DR   PeptideAtlas; P46663; -.
DR   PRIDE; P46663; -.
DR   ProteomicsDB; 55746; -.
DR   Antibodypedia; 153; 322 antibodies from 36 providers.
DR   DNASU; 623; -.
DR   Ensembl; ENST00000216629.11; ENSP00000216629.6; ENSG00000100739.11.
DR   Ensembl; ENST00000611804.1; ENSP00000479276.1; ENSG00000100739.11.
DR   GeneID; 623; -.
DR   KEGG; hsa:623; -.
DR   MANE-Select; ENST00000216629.11; ENSP00000216629.6; NM_000710.4; NP_000701.2.
DR   UCSC; uc001yfh.4; human.
DR   CTD; 623; -.
DR   DisGeNET; 623; -.
DR   GeneCards; BDKRB1; -.
DR   HGNC; HGNC:1029; BDKRB1.
DR   HPA; ENSG00000100739; Tissue enhanced (gallbladder, urinary bladder).
DR   MIM; 600337; gene.
DR   neXtProt; NX_P46663; -.
DR   OpenTargets; ENSG00000100739; -.
DR   PharmGKB; PA79; -.
DR   VEuPathDB; HostDB:ENSG00000100739; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234534; -.
DR   InParanoid; P46663; -.
DR   OMA; QGCFWEE; -.
DR   OrthoDB; 951204at2759; -.
DR   PhylomeDB; P46663; -.
DR   TreeFam; TF330024; -.
DR   PathwayCommons; P46663; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; P46663; -.
DR   SIGNOR; P46663; -.
DR   BioGRID-ORCS; 623; 11 hits in 1070 CRISPR screens.
DR   ChiTaRS; BDKRB1; human.
DR   GeneWiki; Bradykinin_receptor_B1; -.
DR   GenomeRNAi; 623; -.
DR   Pharos; P46663; Tchem.
DR   PRO; PR:P46663; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; P46663; protein.
DR   Bgee; ENSG00000100739; Expressed in gall bladder and 87 other tissues.
DR   ExpressionAtlas; P46663; baseline and differential.
DR   Genevisible; P46663; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004947; F:bradykinin receptor activity; IDA:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; TAS:ProtInc.
DR   GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:InterPro.
DR   GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
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   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..353
FT                   /note="B1 bradykinin receptor"
FT                   /id="PRO_0000069181"
FT   TOPO_DOM        1..40
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..64
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..98
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        99..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..133
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..178
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..199
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..226
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..247
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..272
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..291
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..314
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        315..353
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           330
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        22
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        110..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         250
FT                   /note="A -> V (in dbSNP:rs2229459)"
FT                   /id="VAR_014359"
FT   VARIANT         317
FT                   /note="R -> Q (in dbSNP:rs8004609)"
FT                   /id="VAR_049376"
FT   CONFLICT        146
FT                   /note="R -> G (in Ref. 1, 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240..243
FT                   /note="CGGR -> VRGP (in Ref. 1, 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246
FT                   /note="S -> R (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259
FT                   /note="F -> S (in Ref. 2; AAC50594)"
FT                   /evidence="ECO:0000305"
FT   HELIX           31..63
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           71..88
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           90..97
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   TURN            98..101
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           107..140
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           144..147
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           150..167
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           170..175
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   STRAND          176..180
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   TURN            182..184
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   STRAND          187..191
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           197..210
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           212..238
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           247..277
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           284..301
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           303..312
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   TURN            313..315
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   HELIX           317..324
FT                   /evidence="ECO:0007829|PDB:7EIB"
FT   TURN            325..329
FT                   /evidence="ECO:0007829|PDB:7EIB"
SQ   SEQUENCE   353 AA;  40495 MW;  B62B0690A7593077 CRC64;
     MASSWPPLEL QSSNQSQLFP QNATACDNAP EAWDLLHRVL PTFIISICFF GLLGNLFVLL
     VFLLPRRQLN VAEIYLANLA ASDLVFVLGL PFWAENIWNQ FNWPFGALLC RVINGVIKAN
     LFISIFLVVA ISQDRYRVLV HPMASRRQQR RRQARVTCVL IWVVGGLLSI PTFLLRSIQA
     VPDLNITACI LLLPHEAWHF ARIVELNILG FLLPLAAIVF FNYHILASLR TREEVSRTRC
     GGRKDSKTTA LILTLVVAFL VCWAPYHFFA FLEFLFQVQA VRGCFWEDFI DLGLQLANFF
     AFTNSSLNPV IYVFVGRLFR TKVWELYKQC TPKSLAPISS SHRKEIFQLF WRN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024