7EWP
Cryo-EM structure of human GPR158 in complex with RGS7-Gbeta5 in a 2:1:1 ratio
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0006091 | biological_process | generation of precursor metabolites and energy |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0008218 | biological_process | bioluminescence |
A | 0016020 | cellular_component | membrane |
B | 0004930 | molecular_function | G protein-coupled receptor activity |
B | 0006091 | biological_process | generation of precursor metabolites and energy |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0008218 | biological_process | bioluminescence |
B | 0016020 | cellular_component | membrane |
C | 0001965 | molecular_function | G-protein alpha-subunit binding |
C | 0003924 | molecular_function | GTPase activity |
C | 0005096 | molecular_function | GTPase activator activity |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
C | 0008277 | biological_process | regulation of G protein-coupled receptor signaling pathway |
C | 0009968 | biological_process | negative regulation of signal transduction |
C | 0016020 | cellular_component | membrane |
C | 0030425 | cellular_component | dendrite |
C | 0031681 | molecular_function | G-protein beta-subunit binding |
C | 0035556 | biological_process | intracellular signal transduction |
C | 0042734 | cellular_component | presynaptic membrane |
C | 0043005 | cellular_component | neuron projection |
C | 0043547 | biological_process | positive regulation of GTPase activity |
C | 0044292 | cellular_component | dendrite terminus |
C | 0045211 | cellular_component | postsynaptic membrane |
C | 0045744 | biological_process | negative regulation of G protein-coupled receptor signaling pathway |
C | 0051286 | cellular_component | cell tip |
C | 0060078 | biological_process | regulation of postsynaptic membrane potential |
C | 0098793 | cellular_component | presynapse |
C | 0098978 | cellular_component | glutamatergic synapse |
D | 0003924 | molecular_function | GTPase activity |
D | 0005096 | molecular_function | GTPase activator activity |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0005834 | cellular_component | heterotrimeric G-protein complex |
D | 0005886 | cellular_component | plasma membrane |
D | 0007165 | biological_process | signal transduction |
D | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
D | 0007212 | biological_process | G protein-coupled dopamine receptor signaling pathway |
D | 0016020 | cellular_component | membrane |
D | 0030159 | molecular_function | signaling receptor complex adaptor activity |
D | 0030425 | cellular_component | dendrite |
D | 0031682 | molecular_function | G-protein gamma-subunit binding |
D | 0036367 | biological_process | light adaption |
D | 0042734 | cellular_component | presynaptic membrane |
D | 0043547 | biological_process | positive regulation of GTPase activity |
D | 0045202 | cellular_component | synapse |
D | 0045211 | cellular_component | postsynaptic membrane |
D | 0051087 | molecular_function | protein-folding chaperone binding |
D | 0051286 | cellular_component | cell tip |
D | 0098688 | cellular_component | parallel fiber to Purkinje cell synapse |
D | 0098793 | cellular_component | presynapse |
D | 1901386 | biological_process | negative regulation of voltage-gated calcium channel activity |
D | 1902773 | cellular_component | GTPase activator complex |
D | 1990603 | biological_process | dark adaptation |
Functional Information from PROSITE/UniProt
site_id | PS00678 |
Number of Residues | 15 |
Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. IVSSsqDgKVIVWDS |
Chain | Residue | Details |
D | ILE78-SER92 | |
D | ILE168-VAL182 | |
D | LEU298-VAL312 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49803 |
Chain | Residue | Details |
C | SER229 | |
A | VAL548-ASP576 | |
A | LEU634-TRP642 | |
B | ALA24-ARG417 | |
B | VAL548-ASP576 | |
B | LEU634-TRP642 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O54829 |
Chain | Residue | Details |
C | SER241 | |
B | LEU418-TYR439 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O54829 |
Chain | Residue | Details |
C | THR243 | |
A | LYS502-ARG525 | |
A | TYR598-ARG611 | |
B | HIS440-GLY451 | |
B | LYS502-ARG525 | |
B | TYR598-ARG611 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:10862767 |
Chain | Residue | Details |
C | SER434 | |
B | LEU452-PHE474 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0000305, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF |
Chain | Residue | Details |
A | GLU475-THR478 | |
B | GLU475-THR478 |
site_id | SWS_FT_FI6 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF |
Chain | Residue | Details |
A | PHE479-LEU501 | |
B | PHE479-LEU501 |
site_id | SWS_FT_FI7 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF |
Chain | Residue | Details |
A | VAL526-SER547 | |
B | VAL526-SER547 |
site_id | SWS_FT_FI8 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF |
Chain | Residue | Details |
A | ARG577-CYS597 | |
B | ARG577-CYS597 |
site_id | SWS_FT_FI9 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF |
Chain | Residue | Details |
A | TYR612-VAL633 | |
B | TYR612-VAL633 |
site_id | SWS_FT_FI10 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:34793198, ECO:0000269|PubMed:34815401, ECO:0007744|PDB:7EWL, ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR, ECO:0007744|PDB:7SHE, ECO:0007744|PDB:7SHF |
Chain | Residue | Details |
A | MET643-ILE664 | |
B | MET643-ILE664 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:36996198 |
Chain | Residue | Details |
A | SER172 | |
A | ARG173 | |
A | GLU271 | |
A | ASP307 | |
B | SER172 | |
B | ARG173 | |
B | GLU271 | |
B | ASP307 |
site_id | SWS_FT_FI12 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8C419 |
Chain | Residue | Details |
A | SER694 | |
A | SER705 | |
A | SER708 | |
B | SER694 | |
B | SER705 | |
B | SER708 |
site_id | SWS_FT_FI13 |
Number of Residues | 10 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN98 | |
B | ASN333 | |
A | ASN143 | |
A | ASN215 | |
A | ASN274 | |
A | ASN333 | |
B | ASN98 | |
B | ASN143 | |
B | ASN215 | |
B | ASN274 |
site_id | SWS_FT_FI14 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18655026 |
Chain | Residue | Details |
A | LYS774 | |
B | LYS774 |