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Information on EC 3.4.22.54 - calpain-3 and Organism(s) Rattus norvegicus and UniProt Accession P16259

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.54 calpain-3
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This record set is specific for:
Rattus norvegicus
UNIPROT: P16259 not found.
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
broad endopeptidase specificity
broad endopeptidase activity
Synonyms
capn3, calpain 3, calpain-3, ncl-1, calpain3, muscle calpain, skeletal muscle-specific calpain, muscle-specific calpain, calpain p94, calpain 3 (p94), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calcium-activated neutral proteinase 3
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-
-
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calpain 3
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calpain L3
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-
-
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calpain p94
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-
-
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CANP 3
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-
-
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Cn94
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-
-
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muscle-specific calcium-activated neutral protease 3
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-
-
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nCL-1
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-
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p94-calpain
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
657407-83-5
-
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
alpha-actinin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
filamin C + H2O
?
show the reaction diagram
tropomyosin + H2O
?
show the reaction diagram
-
-
-
-
?
troponin I + H2O
?
show the reaction diagram
-
-
-
-
?
troponins T + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
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important protein for normal muscle function. Mutations in the c3 gene result in limb-girdle muscular dystrophy type 2A
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-
?
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
alpha-actinin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
filamin C + H2O
?
show the reaction diagram
-
enzyme specifically cleaves the C-terminal portion in living cells. Filamin C may be an in vivo substrate to c3, functioning to regulate protein-protein interactions with the sarcoglycans
-
-
?
tropomyosin + H2O
?
show the reaction diagram
-
-
-
-
?
troponin I + H2O
?
show the reaction diagram
-
-
-
-
?
troponins T + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
important protein for normal muscle function. Mutations in the c3 gene result in limb-girdle muscular dystrophy type 2A
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
dependent on Ca2+
Na+
-
calpain 3/p94 is activated by Na+ and undergoes Na+-dependent, but not Cs+-dependent, autolysis in the absence of Ca2+. Na+ and Ca2+ complementarily activate autolysis of calpain3/p94 at physiological concentrations. Na+ and Ca2+ direct calpain3/p94 to proteolyze different substrates
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no influence of muscle stretching to activation of calpain-3
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
mRNA for p94 exists only in skeletal muscle with none detected in other tissues including heart muscle and smooth muscles such as intestine
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
bound to the N2A line on titin or at the triad junctions
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAN3_RAT
821
0
94127
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
94084
x * 94084, calculation from nucleotide sequence
94000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 94084, calculation from nucleotide sequence
?
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x * 94000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C129S
N358D
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activity-attenuated mutant, in contrast to wild type, which autolyses quickly in the absence of Ca2+, the mutant N358D expressed in Sf-9 cells can be partially purified, N358D is very unstable in solutions with high salt concentrations, autolysis of N358D is NaCl-dependent
W99R/I135T/K347E/F779L
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mutant enzyme form does not autolyze and does not cleave filamin C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is not autolyzed with exhaustive exercise in humans
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no autolysis after 1 min exposure to 0.0025 mM Ca2+
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up to 60 min, in presence of 200 nM Ca2+, no spontaneous autolysation
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Toyopearl column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
COS-7 cells are transfected with C3 construct ssubcloned into pcDNA 3.1 and/or a C-terminal human FLNC construct subcloned into pCMV Tag2B
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sorimachi H.; Imajoh-Ohmi S.; Emori Y.; Kawasaki H.; Ohno S.; Minami Y.; Suzuki K.
Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle
J. Biol. Chem.
264
20106-20111
1989
Homo sapiens (P20807), Rattus norvegicus (P16259)
Manually annotated by BRENDA team
Guyon, J.R.; Kudryashova, E.; Potts, A.; Dalkilic, I.; Brosius, M.A.; Thompson, T.G.; Beckmann, J.S.; Kunkel, L.M.; Spencer, M.J.
Calpain 3 cleaves filamin C and regulates its ability to interact with gamma- and delta-sarcoglycans
Muscle Nerve
28
472-483
2003
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Sorimachi, H.; Saido, T.C.; Suzuki, K.
New era of calpain research. Discovery of tissue-specific calpains
FEBS Lett.
343
1-5
1994
Gallus gallus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Murphy, R.M.; Snow, R.J.; Lamb, G.D.
m-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans
Am. J. Physiol.
290
C116-C122
2006
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Murphy, R.M.; Lamb, G.D.
Endogenous calpain-3 activation is primarily governed by small increases in resting cytoplasmic [Ca2+] and is not dependent on stretch
J. Biol. Chem.
284
7811-7819
2009
Rattus norvegicus
Manually annotated by BRENDA team
Ono, Y.; Ojima, K.; Torii, F.; Takaya, E.; Doi, N.; Nakagawa, K.; Hata, S.; Abe, K.; Sorimachi, H.
Skeletal muscle-specific calpain is an intracellular Na+-dependent protease
J. Biol. Chem.
285
22986-22998
2010
Rattus norvegicus
Manually annotated by BRENDA team