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Information on EC 3.4.22.B36 - calpain A and Organism(s) Drosophila melanogaster and UniProt Accession Q11002

for references in articles please use BRENDA:EC3.4.22.B36
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B36 calpain A
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This record set is specific for:
Drosophila melanogaster
UNIPROT: Q11002
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Drosophila melanogaster
Reaction Schemes
broad endopeptidase specificity
Synonyms
calpain a, calcium-activated neutral proteinase, calpa, calpa protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calcium-activated neutral proteinase
-
-
-
-
CALPA protein
-
-
-
-
CANP
-
-
-
-
CAPLA
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
78990-62-2
-
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
peptide + H2O
hydrolyzed peptide
show the reaction diagram
calpain is involved in the dynamic changes in the embryonic cytoskeleton, especially actin-related structures, during early embryogenesis prior to cellularization
-
-
?
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
-
-
-
-
?
additional information
?
-
-
the enzyme undergoes N-terminal autolysis in a Ca2+-dependent manner
-
-
?
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
cactus + H2O
?
show the reaction diagram
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
-
-
?
peptide + H2O
hydrolyzed peptide
show the reaction diagram
calpain is involved in the dynamic changes in the embryonic cytoskeleton, especially actin-related structures, during early embryogenesis prior to cellularization
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates, half-maximal activation of the full-length enzyme at 2.18 mM and for the truncated enzyme at 3.23 mM
Mn2+
-
slight activation
INHIBITOR
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphatidic acid
-
activates
phosphatidylinositol
-
activates
phosphatidylinositol 4,5-bisphosphate
-
activates
phosphatidylinositol 4-monophosphate
-
activates
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
in blood cell line mbn-2 the enzyme is associated with a granular component in the cytoplasm
Manually annotated by BRENDA team
at cleavage cycles 8 and 9, when nuclei reach the egg surface, calpain is localized between the nuclei at the surface beneath the precleavage furrows. Calpain condenses specifically at the edge of and between actin caps that underlie the plasma membrane immediately above each nucleus
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
malfunction
-
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
-
calpain A alters the size and position of Dorsal target gene expression domains, Cactus is regulated by calpain A, calpain A is regulated by Decapentaplegic signaling
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CANA_DROME
828
0
93963
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
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
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
-
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 (Q11002), Drosophila melanogaster Berkeley (Q11002)
Manually annotated by BRENDA team
Theopold, U.; Pinter, M.; Daffre, S.; Tryselius, Y.; Friedrich, P.; Nassel, D.R.; Hultmark, D.
CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells
Mol. Cell. Biol.
15
824-834
1995
Drosophila melanogaster (Q11002), Drosophila melanogaster, Drosophila melanogaster Canton-S (Q11002)
Manually annotated by BRENDA team
Emori, Y.; Saigo, K.
Calpain localization changes in coordination with actib-related cytoskeletal changes during early embryonic development of Drosophila
J. Biol. Chem.
269
25137-25142
1994
Drosophila melanogaster (Q11002), Drosophila melanogaster, Drosophila melanogaster Canton-S (Q11002)
Manually annotated by BRENDA team
Stapleton, M.; Carlson, J.W.; Brokstein, P.; Yu, C.; et al.
A Drosophila full-length cDNA resource
Genome Biol.
3
research0080.1-0080.8
2002
Drosophila melanogaster (Q11002), Drosophila melanogaster Berkeley (Q11002)
-
Manually annotated by BRENDA team
Jekely, G.; Friedrich, P.
Characterization of two recombinant Drosophila calpains. CALPA and a novel homolog, CALPB
J. Biol. Chem.
274
23893-23900
1999
Drosophila melanogaster
Manually annotated by BRENDA team
Fontenele, M.; Carneiro, K.; Agrellos, R.; Oliveira, D.; Oliveira-Silva, A.; Vieira, V.; Negreiros, E.; Machado, E.; Araujo H.
The Ca2+-dependent protease calpain A regulates cactus/I kappaB levels during Drosophila development in response to maternal Dpp signals
Mech. Dev.
126
737-751
2009
Drosophila melanogaster
Manually annotated by BRENDA team
Fontenele, M.; Lim, B.; Oliveira, D.; Buffolo, M.; Perlman, D.H.; Schupbach, T.; Araujo, H.
Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis
Mol. Biol. Cell
24
2966-2980
2013
Drosophila melanogaster (Q11002), Drosophila melanogaster
Manually annotated by BRENDA team
Vieira, V.; Cardoso, M.; Araujo, H.
Calpain A controls mitotic synchrony in the Drosophila blastoderm embryo
Mech. Dev.
144
141-149
2017
Drosophila melanogaster (Q11002)
Manually annotated by BRENDA team