Information on EC 3.4.22.B27 - calpain 7

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.B27
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
calpain 7
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
broad endopeptidase specificity
show the reaction diagram
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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epidermal growth factor receptor degradation is slightly delayed in CAPN7-knockdown HeLa cells, the effect can be reversed by re-expression of wild-type enzyme CAPN7 but not a protease-inactive mutant
physiological function
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the enzyme is involved in membrane trafficking. The proteolytic activity of CAPN7 is important for the acceleration of epidermal growth factor receptor degradation via the endosomal sorting pathway utilizing a part of the endosomal sorting complex required for transport, ESCRT, system
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
C-terminally truncated ALG-2-interacting protein X + H2O
?
show the reaction diagram
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limited proteolysis of C-terminally truncated ALG-2-interacting protein X , but not full-length ALIX. Importance of the CHMP4-ALIX interaction for ALIX truncated mutant cleavage, CHMP4 proteins are part of the ESCRT system
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-
?
domain 1 of calpastatin-Bro1 domain fuion protein + H2O
?
show the reaction diagram
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the calpain-7 cleavage site is located between ELLAK (207-211) and KEGIT(212-216) at the C-terminal border of sub-domain B
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-
?
increased sodium tolerance-1 protein + H2O
?
show the reaction diagram
-
-
-
-
?
peptide + H2O
hydrolyzed peptide
show the reaction diagram
additional information
?
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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
increased sodium tolerance-1 protein + H2O
?
show the reaction diagram
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-
-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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dependent on
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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endosomal sorting complex required for transport (ESCRT) system proteins increase the enzyme activity and autolysis, overview
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
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x * 100000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 100000, SDS-PAGE
additional information
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the enzyme possesses two MIT domains (MITa and MITb) at its N-terminus, a catalytic cysteine protease domain that is composed of PC-1 and PC-2 in the middle, and two CBSW, calpain-type beta-sandwich domains (CBSW) at its C-terminus
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose beads chromatography and Strep-Tactin Sepharose beads chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in HEK293T cells
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expression in COS cells
recombinant expression of GFP-tagged enzyme, recombinant overexpression of wild-type and mutant enzymes in HEK-293T cells, coexpression with FLAG-tagged full-length and C-terminally truncated ALG-2-interacting protein X
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recombinant expression of wild-type enzyme and monomeric GFP-tagged protease-inactive CAPN7 mutant C290S in HeLa cells. The monomeric GFP-tagged inactive CAPN7 mutant C290S is mobilized to EGFR-positive endosomes upon epidermal growth factor stimulation in HeLa cells
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stable HEK293T transfectants of Strep-tagged calpain 7
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C290A
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active site mutant