Detail Information for IndEnz0002002846
IED ID IndEnz0002002846
Enzyme Type ID protease002846
Protein Name B2 bradykinin receptor
B2R
BK-2 receptor
Gene Name Bdkrb2
Organism Rattus norvegicus (Rat)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MDTRSSLCPKTQAVVAVFWGPGCHLSTCIEMFNITTQALGSAHNGTFSEVNCPDTEWWSWLNAIQAPFLWVLFLLAALENIFVLSVFCLHKTNCTVAEIYLGNLAAADLILACGLPFWAITIANNFDWLFGEVLCRVVNTMIYMNLYSSICFLMLVSIDRYLALVKTMSMGRMRGVRWAKLYSLVIWSCTLLLSSPMLVFRTMKDYREEGHNVTACVIVYPSRSWEVFTNMLLNLVGFLLPLSIITFCTVRIMQVLRNNEMKKFKEVQTEKKATVLVLAVLGLFVLCWFPFQISTFLDTLLRLGVLSGCWNERAVDIVTQISSYVAYSNSCLNPLVYVIVGKRFRKKSREVYQAICRKGGCMGESVQMENSMGTLRTSISVDRQIHKLQDWAGNKQ
Enzyme Length 396
Uniprot Accession Number P25023
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Modified residue (7); Sequence conflict (2); Topological domain (8); Transmembrane (7)
Keywords Alternative splicing;Cell membrane;Direct protein sequencing;Disulfide bond;G-protein coupled receptor;Glycoprotein;Lipoprotein;Membrane;Palmitate;Phosphoprotein;Receptor;Reference proteome;Transducer;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Modified Residue MOD_RES 161; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:10085087; MOD_RES 352; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:10085087; MOD_RES 365; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:10085087; MOD_RES 371; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:10085087; MOD_RES 374; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:10085087; MOD_RES 378; /note=Phosphoserine; by GRK6; /evidence=ECO:0000269|PubMed:10085087; MOD_RES 380; /note=Phosphoserine; by GRK6; /evidence=ECO:0000269|PubMed:10085087
Post Translational Modification PTM: Diphosphorylation at Ser-365 and Ser-371, at Ser-378 and Ser-380, and at Thr-374 and Ser-380 seem to be correlated pairwise.; PTM: Palmitoylation at Cys-356 and phosphorylation at Tyr-352 seem to be mutually exclusive. {ECO:0000269|PubMed:10085087}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10188975; 10702448; 11686492; 11934804; 12025958; 12025970; 12177051; 12435802; 12444060; 12489796; 12558524; 12558526; 12623134; 12639805; 12694402; 12746865; 12791684; 12923406; 14727005; 14753436; 14766673; 14766794; 15001555; 15576455; 15607753; 15708952; 15878794; 16138314; 16507603; 16513137; 16754789; 18182225; 18190998; 18264983; 18302192; 18632797; 19017652; 19027830; 19300402; 19544046; 19565561; 19889854; 19950773; 19954757; 20080302; 20150590; 20198577; 20345876; 20531238; 20637711; 20883789; 21232147; 21986469; 22739815; 22862305; 22877648; 23306173; 23417862; 23735753; 23982204; 24025224; 24724708; 25713410; 25955317; 26256678; 26565562; 27628189; 30580020; 31086419; 33687297; 7791078; 9208140;
Motif
Gene Encoded By
Mass 44,930
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda