9JVH
Cryo-EM structure of the mmGPR4-Gs receptor in pH6.2
Functional Information from GO Data
Chain | GOid | namespace | contents |
R | 0004930 | molecular_function | G protein-coupled receptor activity |
R | 0005886 | cellular_component | plasma membrane |
R | 0007165 | biological_process | signal transduction |
R | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
R | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
R | 0007200 | biological_process | phospholipase C-activating G protein-coupled receptor signaling pathway |
R | 0010447 | biological_process | response to acidic pH |
R | 0016020 | cellular_component | membrane |
R | 0016525 | biological_process | negative regulation of angiogenesis |
R | 0030155 | biological_process | regulation of cell adhesion |
R | 0035025 | biological_process | positive regulation of Rho protein signal transduction |
R | 0043114 | biological_process | regulation of vascular permeability |
R | 0050729 | biological_process | positive regulation of inflammatory response |
R | 0060055 | biological_process | angiogenesis involved in wound healing |
R | 0071468 | biological_process | cellular response to acidic pH |
R | 0072144 | biological_process | glomerular mesangial cell development |
Functional Information from PROSITE/UniProt
site_id | PS00237 |
Number of Residues | 17 |
Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ISIaFLCCISVDRYLaV |
Chain | Residue | Details |
R | ILE105-VAL121 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 87 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
R | MET1-SER24 | |
R | ASP77-LEU94 | |
R | HIS157-TRP179 | |
R | SER248-SER273 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
R | LEU25-TYR45 |
site_id | SWS_FT_FI3 |
Number of Residues | 126 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
R | ARG46-GLY55 | |
R | ASP116-THR135 | |
R | LEU201-ARG226 | |
R | ASN292-GLN365 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
R | VAL56-VAL76 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
R | PHE95-VAL115 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
R | ALA136-PHE156 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
R | VAL180-LEU200 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
R | LEU227-LEU247 |
site_id | SWS_FT_FI9 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
R | LEU274-VAL291 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
R | ASN3 | |
R | ASN166 |