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Information on EC 3.6.5.1 - heterotrimeric G-protein GTPase and Organism(s) Rattus norvegicus

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IUBMB Comments
This group comprises GTP-hydrolysing systems, where GTP and GDP alternate in binding. This group includes stimulatory and inhibitory G-proteins such as Gs, Gi, Go and Golf, targetting adenylate cyclase and/or K+ and Ca2+ channels; Gq stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. Golf is instrumental in odour perception, transducin in vision and gustducin in taste recognition. At least 16 different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and 12 gamma subunits (6-9 kDa) are known.
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Rattus norvegicus
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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GTP
+
H2O
=
GDP
+
phosphate
+
=
+
Synonyms
gtpase, transducin, gs alpha, heterotrimeric g protein, galphaq, guanosine triphosphatase, elongation factor 2, heterotrimeric g-protein, rab1a, g alpha q, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Gs alpha
-
-
GTP phosphohydrolase
GTPase
-
-
-
-
guanosine 5'-triphosphatase
-
-
-
-
guanosine triphosphatase
-
-
-
-
heterotrimeric G-protein
-
-
heterotrimeric G-protein GTPase
-
-
phosphatase, guanosine tri-
-
-
-
-
ribosomal GTPase
-
-
-
-
transducin GTPase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + H2O = GDP + phosphate
show the reaction diagram
mechanism of membrane translocation
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
-
-
phosphorous acid anhydride hydrolysis
SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (signalling)
This group comprises GTP-hydrolysing systems, where GTP and GDP alternate in binding. This group includes stimulatory and inhibitory G-proteins such as Gs, Gi, Go and Golf, targetting adenylate cyclase and/or K+ and Ca2+ channels; Gq stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. Golf is instrumental in odour perception, transducin in vision and gustducin in taste recognition. At least 16 different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and 12 gamma subunits (6-9 kDa) are known.
CAS REGISTRY NUMBER
COMMENTARY hide
9059-32-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
additional information
?
-
-
membrane translocation of RGS8, a regulator of G-protein signaling, depends on interaction of RGS8 with enzyme
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pertussis toxin
-
pertussis toxin-catalysed ADP-ribosylation prevents functional contacts between G-protein-coupled receptors and the Gi-like G-proteins
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
amyloid beta-peptide fragment (1-42)
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stimulates GTPase activity
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amyloid beta-peptide fragment (25-35)
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stimulates GTPase activity
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CIVIAKLKANLM amide
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peptide derived from glucagon-like peptide, residues 329-340, 0.001 mM, 186% of basal GTPase activity
CIVIAKLKANLMCKTDIKCRLAK amide
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peptide derived from glucagon-like peptide, residues 329-351, 0.001 mM, 595% of basal GTPase activity
CKTDIKCRLAK amide
-
peptide derived from glucagon-like peptide, residues 341-351, 0.001 mM, 216% of basal GTPase activity
additional information
-
tubulin binds to Gs alpha
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
Go-alpha subunit
Manually annotated by BRENDA team
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Go-alpha subunit
Manually annotated by BRENDA team
-
Go-alpha subunit
Manually annotated by BRENDA team
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cerebellar granule neuron
Manually annotated by BRENDA team
-
Go-alpha subunit
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GNAI1_RAT
354
0
40345
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
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Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RGS4 complexed with Gialpha1-Mg2+-GDP-AlF4
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C351G
-
mutation of Gi1alpha or Gi3alpha, pertussis toxin-resistant mutant
C352G
-
mutation of Gi2alpha, pertussis toxin-resistant mutant
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293T cells
-
Galpha subunit is subcloned into pcDNA3.1+
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rouot, B.; Brabet, P.; Homburger, V.; Toutant, M.; Bockaert, J.
Go, a major brain GTP binding protein in search of a function: purification, immunological and biochemical characteristics
Biochimie
69
339-349
1987
Bos taurus, Canis lupus familiaris, Gallus gallus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Wise, A.; Watson-Koken, M.A.; Rees, S.; Lee, M.; Milligan, G.
Interactions of the alpha2A-adrenoceptor with multiple Gi-family G-proteins: studies with pertussis toxin-resistant G-protein mutants
Biochem. J.
321
721-728
1997
Rattus norvegicus
Manually annotated by BRENDA team
Soomets, U.; Mahlapuu, R.; Tehranian, R.; Jarvet, J.; Karelson, E.; Zilmer, M.; Iverfeldt, K.; Zorko, M.; Graeslund, A.; Langel, U.
Regulation of GTPase and adenylate cyclase activity by amyloid beta-peptide and its fragments in rat brain tissue
Brain Res.
850
179-188
1999
Rattus norvegicus
Manually annotated by BRENDA team
Tesmer, J.J.G.; Berman, D.M.; Gilman, A.G.; Sprang, S.R.
Structure of RGS4 bound to AlF4-activated Gialpha1: stabilization of the transition state for GTP hydrolysis
Cell
89
251-261
1997
Rattus norvegicus, Rattus norvegicus Gialpha1
Manually annotated by BRENDA team
Hallbrink, M.; Holmqvist, T.; Olsson, M.; Ostenson, C.G.; Efendic, S.; Langel, U.
Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Galpha(s) and Galpha(i)/Galpha(o) activation
Biochim. Biophys. Acta
1546
79-86
2001
Rattus norvegicus
Manually annotated by BRENDA team
Masuho, I.; Itoh, M.; Itoh, H.; Saitoh, O.
The mechanism of membrane-translocation of regulator of G-protein signaling (RGS) 8 induced by Galpha expression
J. Neurochem.
88
161-168
2004
Rattus norvegicus
Manually annotated by BRENDA team
Clark, M.A.; Lambert, N.A.
Endogenous regulator of G-protein signaling proteins regulate the kinetics of Galphaq/11-mediated modulation of ion channels in central nervous system neurons
Mol. Pharmacol.
69
1280-1287
2006
Rattus norvegicus
Manually annotated by BRENDA team
Dave, R.H.; Saengsawang, W.; Yu, J.Z.; Donati, R.; Rasenick, M.M.
Heterotrimeric G-proteins interact directly with cytoskeletal components to modify microtubule-dependent cellular processes
Neurosignals
17
100-108
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team