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Information on EC 2.7.11.12 - cGMP-dependent protein kinase and Organism(s) Drosophila melanogaster and UniProt Accession P32023

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EC Tree
IUBMB Comments
CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates . The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase .
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This record set is specific for:
Drosophila melanogaster
UNIPROT: P32023
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
cgmp-dependent protein kinase, protein kinase g, cyclic gmp-dependent protein kinase, cgkii, pkg-i, cgmp kinase, prkg1, pkg ii, cgk ii, cgmp-dependent protein kinase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cGMP-dependent protein kinase, isozyme 2 forms cD5/T2
-
CGK 1 alpha
-
-
-
-
CGK 1 beta
-
-
-
-
CGKI-alpha
-
-
-
-
cGKI-beta
-
-
-
-
cGKII
-
-
-
-
cGMP-dependent protein kinase
-
-
-
-
cGMP-dependent protein kinase, isozyme 1
-
DG1 protein kinase
-
Foraging protein
-
-
-
-
protein kinase G
-
-
-
-
Type II cGMP-dependent protein kinase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (cGMP-dependent)
CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates [3]. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase [4].
CAS REGISTRY NUMBER
COMMENTARY hide
141588-27-4
-
141588-27-4
cGMP-dependent protein kinase
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + histone
ADP + phosphorylated histone
show the reaction diagram
-
DG1
-
-
?
ATP + RKRSRAE
ADP + RKRS(P)RAE
show the reaction diagram
-
cGK-specific peptide substrate
-
-
?
additional information
?
-
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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-bromo-cAMP
50% activation at 0.00062 mM
8-bromo-cGMP
50% activation at 0.00004 mM
cIMP
50% activation at 0.0053 mM
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KT5823
-
a specific PKG inhibitor, PKG inhibition induces rapid thermotolerance of neural circuitry
Rp-8-pCPT-cGMP
-
i.e. 8-(4-chlorophenylthio)guanosine-3',5'-cyclic monophosphorothionate Rp isomer, inhibits DG2P1 and DG2P2 at 0.01 and 0.1 mM, respectively
additional information
the enzyme possesses an N-terminal autoinhibitory sequence
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-bromo-cGMP
-
PKG activator 8-bromo-cGMP abolishes thermoprotective effect of a prior heat shock
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
Drosophila embryos display targeting defects during axon development in the absence of the enzyme gene
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KGP25_DROME
934
0
105907
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
-
x * 65000, recombinant DG1, SDS-PAGE, x * 84000, recombinant DG2P1 and DG2P2, SDS-PAGE
84000
-
x * 65000, recombinant DG1, SDS-PAGE, x * 84000, recombinant DG2P1 and DG2P2, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
domain structure
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
autophosphorylation
phosphoprotein
-
autophosphorylation by DG1
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of transgenic flies by targeted expression of DG2P1 and DG2P2, and DG1 in malpigian tubule using the UAS/GAL4 system, differential localization of all 3 enzyme forms in transgenic flies, phenotypes, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
phylogenetic analysis
expressed in Sf9 cells
in vitro transcription of DG2P1 and DG2P2, and DG1 by RT-PCR of cDNAs from tubule cells, targeted expression of DG2P1 and DG2P2, and DG1 in malpigian tubule using the UAS/GAL4 system, differential localization of all 3 enzyme forms in transgenic flies
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the enzyme is encoded by the foraging gene for which shows polymorphisms associated with the allelic variation in for
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Adams, M.D.; Celniker, S.E.; Holt, R.A.; Evans, C.A.; Gocayne, J.D.; et al.
The genome sequence of Drosophila melanogaster
Science
287
2185-2195
2000
Drosophila melanogaster (Q03042)
Manually annotated by BRENDA team
Kalderon, D.; Rubin, G.M.
cGMP-dependent protein kinase genes in Drosophila
J. Biol. Chem.
264
10738-10748
1989
Drosophila melanogaster (P32023), Drosophila melanogaster (Q03042), Drosophila melanogaster (Q03043)
Manually annotated by BRENDA team
Foster, J.L.; Higgins, G.C.; Jackson, F.R.
Biochemical properties and cellular localization of the Drosophila DG1 cGMP-dependent protein kinase
J. Biol. Chem.
271
23322-23328
1996
Drosophila melanogaster (Q03042)
Manually annotated by BRENDA team
Baker, D.A.; Deng, W.
Cyclic GMP-dependent protein kinases in protozoa
Front. Biosci.
10
1229-1238
2005
Aplysia californica, Bos taurus, Caenorhabditis elegans, Chlamydomonas reinhardtii, Homo sapiens, Plasmodium falciparum, Plasmodium yoelii, Tetrahymena sp., Hydra oligactis (O17474), Drosophila melanogaster (P32023), Paramecium tetraurelia (Q869J9), Paramecium tetraurelia (Q869K0), Toxoplasma gondii (Q8MMP4), Eimeria maxima (Q8MMZ5), Cryptosporidium parvum (Q8MMZ6), Eimeria tenella (Q8MMZ8), Apis mellifera (Q8SSX4)
Manually annotated by BRENDA team
MacPherson, M.R.; Lohmann, S.M.; Davies, S.A.
Analysis of Drosophila cGMP-dependent protein kinases and assessment of their in vivo roles by targeted expression in a renal transporting epithelium
J. Biol. Chem.
279
40026-40034
2004
Drosophila melanogaster
Manually annotated by BRENDA team
Dawson-Scully, K.; Armstrong, G.A.; Kent, C.; Robertson, R.M.; Sokolowski, M.B.
Natural variation in the thermotolerance of neural function and behavior due to a cGMP-dependent protein kinase
PLoS ONE
2
e773
2007
Drosophila melanogaster
Manually annotated by BRENDA team
Dason, J.S.; Allen, A.M.; Vasquez, O.E.; Sokolowski, M.B.
Distinct functions of a cGMP-dependent protein kinase in nerve terminal growth and synaptic vesicle cycling
J. Cell Sci.
132
jcs227165
2019
Drosophila melanogaster
Manually annotated by BRENDA team
Peng, Q.; Wang, Y.; Li, M.; Yuan, D.; Xu, M.; Li, C.; Gong, Z.; Jiao, R.; Liu, L.
cGMP-Dependent protein kinase encoded by foraging regulates motor axon guidance in Drosophila by suppressing Lola function
J. Neurosci.
36
4635-4646
2016
Drosophila melanogaster
Manually annotated by BRENDA team