Detail Information for IndEnz0002012226
IED ID IndEnz0002012226
Enzyme Type ID protease012226
Protein Name Regulator of G-protein signaling 17
RGS17
Regulator of Gz-selective protein signaling 2
Gene Name Rgs17 Rgsz2
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MRKRQQSQNEGTQAVSQAPGNQRPNNTCCFCWCCCCSCSCLTVRNEERGDSSGRSPHTTKMESIQVLEECQNPTADEVLSWSQNFDKMMKTPAGRNLFREFLRTEYSEENLLFWLACEDLKKEQNKKAVEEKARMIYEDYISILSPKEVSLDSRVREVINRSLLDPSPHMYEDAQLQIYTLMHRDSFPRFLNSQIYKAFVESTTSCTSES
Enzyme Length 210
Uniprot Accession Number Q9QZB0
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Binds selectively to GNAZ and GNAI2 subunits, accelerates their GTPase activity and regulates their signaling activities. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins. {ECO:0000250|UniProtKB:Q9UGC6, ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (1); Domain (1); Modified residue (1); Region (1)
Keywords Cell junction;Cytoplasm;GTPase activation;Glycoprotein;Membrane;Nucleus;Phosphoprotein;Reference proteome;Signal transduction inhibitor;Synapse;Synaptosome;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. Cell junction, synapse, synaptosome {ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16900103}. Nucleus {ECO:0000269|PubMed:16900103}. Cytoplasm {ECO:0000269|PubMed:16900103}.
Modified Residue MOD_RES 137; /note=Phosphotyrosine; /evidence=ECO:0007744|PubMed:18034455
Post Translational Modification PTM: N- and O-glycosylated in synapsomal membranes. {ECO:0000269|PubMed:15827571}.; PTM: Serine phosphorylated in synapsomal membranes. {ECO:0000269|PubMed:16900103}.; PTM: Sumoylated with SUMO1 and SUM02 in synaptosomes. The sumoylated forms act as a scaffold for sequestering mu-opioid receptor-activated G(alpha) subunits (PubMed:16900103). Desumoylated by HINT1 (PubMed:31088288). {ECO:0000269|PubMed:16900103, ECO:0000269|PubMed:31088288}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 11342430; 11829488; 12466851; 15096504; 16602821; 18652891; 21267068; 21348811; 21677750; 22163035; 22967998; 30478225;
Motif
Gene Encoded By
Mass 24,345
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda