1FQJ,1FQI,1FQJ,2PBI,2PBI


Conserved Protein Domain Family
RGS_RGS9

?
cd08739: RGS_RGS9 
Click on image for an interactive view with Cn3D
Regulator of G protein signaling (RGS) domain found in the RGS9 protein
The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS9 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS7, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. RGS9 forms constitutive complexes with G-beta-5 subunit and controls such fundamental functions as vision and behavior. RGS9 exists in two splice isoforms: RGS9-1 which regulates phototransduction in rods and cones and RGS9-2 which regulates dopamine and opioid signaling in the basal ganglia. In addition, RGS9 was found to bind many other proteins outside of G protein signaling pathways including: mu-opioid receptor, beta-arrestin, alpha-actinin-2, NMDAR, polycystin, spinophilin, and guanylyl cyclase, among others.
Statistics
?
PSSM-Id: 188693
Aligned: 8 rows
Threshold Bit Score: 251.87
Created: 22-Jul-2009
Updated: 2-Oct-2020
Structure
?
Program:
Drawing:
Aligned Rows:
 
heterotrimericG-beta-5
Conserved site includes 36 residues -Click on image for an interactive view with Cn3D
Feature 1:heterotrimeric complex
Evidence:
  • Structure:1FQJ_B: Homo sapiens RGS9 RGS binds GtI1 chimera alpha subunit, the gamma subunit of Phosphodiesterase (PDE); contacts at 4 A
  • Comment:RGS domain of the RGS9 interacts with both switch II region of G alpha and PDE through a unique complementation of electrostatic ( R360) and hydrophobic (W362) interactions.The interaction is RGS9 specific - in other RGS proteins R360 and W362 replaced.

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1     #  #  #   #  # #  ##  #   # ### ##    #   #                       ####### ###   
1FQJ_B     17 RVERWAFNFSELIRDPKGRQSFQHFLRKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMD 96  cattle
1FQI_A     17 RVERWAFNFSELIRDPKGRQSFQHFLRKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTXD 96  cattle
1FQJ_E     17 RVERWAFNFSELIRDPKGRQSFQHFLRKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMD 96  cattle
2PBI_A    294 RVERWAFNFSELIRDPKGRQSFQYFLKKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMD 373 house mouse
2PBI_C    294 RVERWAFNFSELIRDPKGRQSFQYFLKKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMD 373 house mouse
AAZ79484  294 RVERWALNFSELMRDPKGRQNFQLFLKKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKTFLAPGARRWINIDGTTMG 373 Uta stansburiana
XP_415685 297 RVERWAFNFSELIRDPKGRQNFQLFLKKEFSGENLSFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGTTMG 376 chicken
CAP09555  295 RVERWTFSFGELLTDQRGRADFRLFLKKEFSGENLAFWEACEDLKWGAAETMKEKAQQIYKTFLARGAPRWINIDGKTME 374 zebrafish
Feature 1                        #  ## ####  #  #      
1FQJ_B     97 ITVKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKE 137 cattle
1FQI_A     97 ITVKGLKHPHRYVLDAAQTHIYXLXKKDSYARYLKSPIYKE 137 cattle
1FQJ_E     97 ITVKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKE 137 cattle
2PBI_A    374 ITVKGLRHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKE 414 house mouse
2PBI_C    374 ITVKGLRHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKE 414 house mouse
AAZ79484  374 ITVRGLKHPHRYVLDAAQTHIYMLMKKDSYGRYLKSPVYKE 414 Uta stansburiana
XP_415685 377 ITVKGLKHPHRYVLDAAQTHIYMLMKKDSYGRYLKSPVYKE 417 chicken
CAP09555  375 ITVKGLGHPHRYVLDAAQTHIYMLMKKDSYGRYLKSPVFKE 415 zebrafish

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap