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0RGS7_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameRGS7
DescriptionRegulator of g-protein signaling 7 (rgs7).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016299 regulator of G-protein signaling activity (NAS)
0008277 regulation of G-protein coupled receptor pr... (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
RGS (Regulator of G Protein Signalling) proteins are multi-functional.TPase-accelerating proteins that promote GTP hydrolysis by the alpha subunit of heterotrimeric G proteins.hereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways . Upon activation by GPCRs.eterotrimeric G proteins exchange GDP for GTP.re released from the receptor.nd dissociate into free.ctive GTP-bound alpha subunit and beta-gamma dimer.oth of which activate downstream effectors. The response is terminated upon GTP hydrolysis by the alpha subunit ().hich can then bind the beta-gamma dimer (. and the receptor. RGS proteins markedly reduce the lifespan of GTP-bound alpha subunits by stabilising the G protein transition state.All RGS proteins contain an RGS-box (or RGS domain).hich is required for activity. Some small RGS proteins such as RGS1 and RGS4 are comprised of little more than an RGS domain.hile others also contain additional domains that confer further functionality . RGS domains can be found in conjunction with a variety of domains.ncluding: DEP for membrane targeting ().DZ for binding to GPCRs ().TB for phosphotyrosine-binding ().BD for Ras-binding ().oLoco for guanine nucleotide inhibitor activity ().X for phosphatidylinositol-binding ().XA that is associated with PX ().H for stimulating guanine nucleotide exchange ().nd GGL (G protein gamma subunit-like) for binding G protein beta subunits () . Those RGS proteins that contain GGL domains can interact with G protein beta subunits to form novel dimers that prevent G protein gamma subunit binding and G protein alpha subunit association.hereby preventing heterotrimer formation.
  IPR000342:Regulator of G protein signalling
This is a domain of unknown function present in signaling proteins including dishevelled.gl-10.nd pleckstrinproteins. Segment polarity dishevelled protein is required to establish coherent arrays of polarized cells andsegments in embryos.nd plays a role in wingless signaling. Egl-10 regulates G-protein signaling in the centralnervous system. Mammalian regulators of G-protein signaling also contain these domains.nd regulate signaltransduction by increasing the GTPase activity of G-protein alpha subunits.hereby driving them into theirinactive GDP-bound form.
  IPR000591:Pleckstrin/ G-protein, interacting region
Guanine nucleotide binding proteins (G proteins) are membrane-associated.eterotrimeric proteins composed of three subunits: alpha ().eta () and gamma () . G proteins and their receptors (GPCRs) form one of the most prevalent signalling systems in mammalian cells.egulating systems as diverse as sensory perception.ell growth and hormonal regulation . At the cell surface.he binding of ligands such as hormones and neurotransmitters to a GPCR activates the receptor by causing a conformational change.hich in turn activates the bound G protein on the intracellular-side of the membrane. The activated receptor promotes the exchange of bound GDP for GTP on the G protein alpha subunit. GTP binding changes the conformation of switch regions within the alpha subunit.hich allows the bound trimeric G protein (inactive) to be released from the receptor.nd to dissociate into active alpha subunit (GTP-bound) and beta/gamma dimer. The alpha subunit and the beta/gamma dimer go on to activate distinct downstream effectors.uch as adenylyl cyclase.hosphodiesterases.hospholipase C.nd ion channels. These effectors in turn regulate the intracellular concentrations of secondary messengers.uch as cAMP.iacylglycerol.odium or calcium cations.hich ultimately lead to a physiological response.sually via the downstream regulation of gene transcription. The cycle is completed by the hydrolysis of alpha subunit-bound GTP to GDP.esulting in the re-association of the alpha and beta/gamma subunits and their binding to the receptor.hich terminates the signal . The length of the G protein signal is controlled by the duration of the GTP-bound alpha subunit.hich can be regulated by RGS (regulator of G protein signalling) proteins () or by covalent modifications .There are several isoforms of each subunit.any of which have splice variants.hich together can make up hundreds of combinations of G proteins. The specific combination of subunits in heterotrimeric G proteins affects not only which receptor it can bind to.ut also which downstream target is affected.roviding the means to target specific physiological processes in response to specific external stimuli . G proteins carry lipid modifications on one or more of their subunits to target them to the plasma membrane and to contribute to protein interactions.This entry represents the G protein gamma subunit and the GGL (G protein gamma-like) domain.hich are related in sequence and are comprised of an extended alpha-helical polypeptide. The G protein gamma subunit forms a stable dimer with the beta subunit.ut it does not make any contact with the alpha subunit.hich contacts the opposite face of the beta subunit. The GGL domain is found in several RGS proteins. GGL domains can interact with beta subunits to form novel dimers that prevent gamma subunit binding.nd may prevent heterotrimer formation by inhibiting alpha subunit binding. The interaction between G protein beta-5 neuro-specific isoforms and RGS GGL domains may represent a general mode of binding between beta-propeller proteins and their partners .
  IPR001770:G-protein, gamma subunit
Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding motif.here the "wings".r loops.re small beta-sheets. The winged helix motif consists of two wings (W1.2).hree alpha helices (H1.2.3) and three beta-sheets (S1.2.3) arranged in the order H1-S1-H2-H3-S2-W1-S3-W2 . The DNA-recognition helix makes sequence-specific DNA contacts with the major groove of DNA.hile the wings make different DNA contacts.ften with the minor groove or the backbone of DNA. Several winged-helix proteins display an exposed patch of hydrophobic residues thought to mediate protein-protein interactions.Many different proteins with diverse biological functions contain a winged helix DNA-binding domain.ncluding transcriptional repressors such as biotin repressor.exA repressor and the arginine repressor ; transcription factors such as the hepatocyte nuclear factor-3 proteins involved in cell differentiation.eat-shock transcription factor.nd the general transcription factors TFIIE and TFIIF . helicases such as RuvB that promotes branch migration at the Holliday junction.nd CDC6 in the pre-replication complex . endonucleases such as FokI and TnsA ; histones; and Mu transposase.here the flexible wing of the enhancer-binding domain is essential for efficient transposition .
  IPR011991:Winged helix repressor DNA-binding
IPR000342:RGS 
Evalue:-55.9586067199707 
Location:333-448IPR000591:DEP 
Evalue:-32.4559326171875 
Location:37-116IPR001770:G-gamma 
Evalue:-26.2076091766357 
Location:255-308IPR001770:G_PROTEIN_GAMMA 
Evalue:0 
Location:0-0
SequencesProtein: RGS7_HUMAN (495 aa)
mRNA: AF493931 NM_002924
Local Annotation
Synapse Ontology
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 215 residues, 239005493-239006136Exon2: 20 residues, 239031377-239031431Exon3: 32 residues, 239032826-239032916Exon4: 64 residues, 239036062-239036249Exon5: 44 residues, 239041840-239041966Exon6: 39 residues, 239043540-239043651Exon7: 22 residues, 239044638-239044700Exon8: 35 residues, 239046239-239046338Exon9: 27 residues, 239057020-239057095Exon10: 29 residues, 239098509-239098591Exon11: 27 residues, 239098698-239098775Exon12: 23 residues, 239099977-239100042Exon13: 19 residues, 239160639-239160691Exon14: 37 residues, 239166522-239166629Exon15: 19 residues, 239213001-239213052Exon16: 34 residues, 239328588-239328685Exon17: 44 residues, 239585621-239585749Exon18: 95 residues, 239586821-239587101Exon19: 2 residues, -Jump to RGS7_HUMANExon1: 17 residues, 239006087-239006136Exon2: 29 residues, 239030563-239030644Exon3: 32 residues, 239032826-239032916Exon4: 64 residues, 239036062-239036249Exon5: 44 residues, 239041840-239041966Exon6: 39 residues, 239043540-239043651Exon7: 22 residues, 239044638-239044700Exon8: 35 residues, 239046239-239046338Exon9: 27 residues, 239057020-239057095Exon10: 29 residues, 239098509-239098591Exon11: 27 residues, 239098698-239098775Exon12: 23 residues, 239099977-239100042Exon13: 19 residues, 239160639-239160691Exon14: 37 residues, 239166522-239166629Exon15: 19 residues, 239213001-239213052Exon16: 34 residues, 239328588-239328685Exon17: 28 residues, 239585621-239585699Exon18: 2 residues, -Jump to RGS7_HUMAN