Information on EC 3.4.22.B36 - calpain A

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The expected taxonomic range for this enzyme is: Drosophila melanogaster

EC NUMBER
COMMENTARY hide
3.4.22.B36
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
calpain A
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
broad endopeptidase specificity
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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endopeptidase; peptides, endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY hide
78990-62-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Berkeley
SwissProt
Manually annotated by BRENDA team
strain Canton-S
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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calpainA knockdowns increase Cactus levels, shifting the dorsal gradient and dorsal-ventral patterning. Decapentaplegic protein signals increase Cactus levels through calpain A inhibition, thereby interfering with Dorsal gene activation
physiological function
additional information
cactus protein levels affect the cellular localization of the enzyme, overview. Wild-type syncytial blastoderm embryo show endogenous calpain A beneath the plasma membrane, while in loss-of-function cact mutants calpain A is diffuse in the cytoplasm. In a gain-of-function cact mutant, calpain A distribution is patchy during interphase and remains so during mitosis. Cactus regulates calpain A activity and localization
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cactus + H2O
?
show the reaction diagram
casein + H2O
hydrolyzed casein
show the reaction diagram
-
-
-
-
?
N-succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
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-
-
-
?
peptide + H2O
hydrolyzed peptide
show the reaction diagram
additional information
?
-
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the enzyme undergoes N-terminal autolysis in a Ca2+-dependent manner
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cactus + H2O
?
show the reaction diagram
Q11002
an IkappaB homo­logue, Cactus and calpain A physically interact, calpain A generates a C-terminal–truncated Cactus fragment devoid of Toll-responsive sequences, cleavage analysis in vivo, overview
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-
?
peptide + H2O
hydrolyzed peptide
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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slight activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NF-kappa-B inhibitor cactus
negatively regulates calpain A activity. In Drosophila cactus exists as free and NFkappaB-bound forms
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphatidic acid
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activates
phosphatidylinositol
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activates
phosphatidylinositol 4,5-bisphosphate
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activates
phosphatidylinositol 4-monophosphate
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activates
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression during early embryogenesis
Manually annotated by BRENDA team
CalpA protein is apically enriched in the submembranous cyto­plasm of the embryo syncytium
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and inducible expression of C-terminally V5/His-tagged CalpA in S2 cells
expression of wild-type and truncated enzyme form, lacking the CALPA-specific unique insertion region
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the truncated enzyme form lacking the CALPA-specific unique insertion region. Although it lacks the 16-amino acid long putative membrane-anchoring segment, its activation by phospholipids is similar to that of the full-length CALPA protein