3.4.22.54: calpain-3
This is an abbreviated version!
For detailed information about calpain-3, go to the full flat file.
Word Map on EC 3.4.22.54
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3.4.22.54
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calpains
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dystrophy
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muscular
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limb-girdle
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girdle
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lgmd2a
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limb
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calpainopathy
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titin
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calpastatin
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myopathy
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dysferlin
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tender
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autolytic
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sarcomere
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mu-calpains
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sarcoglycans
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myofibrillar
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telethonin
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scapular
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alpha-sarcoglycan
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merosin
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autolyzed
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caveolin-3
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nebulin
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lumborum
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m-lines
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dysferlinopathy
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sarcoglycanopathy
- 3.4.22.54
- calpains
- dystrophy
- muscular
-
limb-girdle
-
girdle
-
lgmd2a
- limb
-
calpainopathy
- titin
- calpastatin
- myopathy
-
dysferlin
-
tender
-
autolytic
- sarcomere
- mu-calpains
-
sarcoglycans
- myofibrillar
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telethonin
-
scapular
-
alpha-sarcoglycan
-
merosin
-
autolyzed
-
caveolin-3
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nebulin
- lumborum
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m-lines
-
dysferlinopathy
- sarcoglycanopathy
Reaction
broad endopeptidase activity =
Synonyms
C3DIV, calcium-activated neutral proteinase 3, Calp3, calpain 3, calpain 3 (p94), calpain 3 domain IV, calpain 3/p94, calpain L3, calpain M, calpain p94, calpain-3, calpain3, CANP 3, CAPN3, Cn94, MP78, Mp84, muscle calpain, muscle-specific calcium-activated neutral protease 3, muscle-specific calpain, nCL-1, p94, p94-calpain, p94/calpain 3, skeletal muscle-specific calpain
ECTree
3.4.22.54 calpain-3Advanced search results
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results (Source Tissue
Source Tissue on EC 3.4.22.54 - calpain-3
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
numerous splice variants of Capn3 are expressed, they contain deletions or insertions in or around the IS1, IS2, and NS regions
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calpain 3 or its isoforms is necessary for formation of the nuclear cataract that is observed in the alpha3Cx46-/- lens. In the absence of the CAPN3 gene, the formation of a cataract is delayed, and its appearance is changed to a more diffuse, pulverulent type
two novel splicing variants (hMp78 and hMp84) of calpain-3 gene (CAPN3) have a significant lower expression in vertical growth phase melanomas and, even lower, in metastases, compared to benign nevi
the single large catalytic subunit of calpain 3 is expressed predominantly in the submandibular gland at markedly higher levels in males than in females and in a manner dependent on androgens. In granular convoluted tubule cell calpain 3 immunoreactivity is localized predominantly in the cytosolic region and is absent in the secretory granules. Granular convoluted tubule is the primary site of production of calpain 3 submandibular gland
papillomavirus-associated urothelial tumors of the urinary bladder
additional information
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activity is almost undetectable in polymorphonuclear cells
alternatively exon-spliced isoforms of calpain 3 expressed in human leukocytes
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of normal and of patients with limb girdle muscular dystrophy. Screening of calpain-3 autolytic activity in limb girdle muscular dystrophy muscle. Missense mutations localized in calpain-3 domains II and III would impair its autolytic activity, possibly because of the charge variation in the residues involved in internal salt bridges. This would finally result in a reduced sensitivity to Ca2+-ions. The pathogenetic effect of these mutations may be understood in terms of impaired communications between protein interdomains
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calpain-3 is localized at the skeletal muscle M-line, Z-band, and the N2A region of the large myofibrillar protein, titin
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isolated from LGMD2A patients. CAPN3 intervenes in the regulation of the expression of NF-kappaB-dependent survival genes to prevent apoptosis in skeletal muscle. Deregulations in the NF-kappaB pathway could be part of the mechanism responsible for the muscle wasting resulting from CAPN3 deficiency
mRNA for p94 exists only in skeletal muscle with none detected in other tissues including heart muscle and smooth muscles such as intestine
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fast-twitch and slow-twitch fibers. In this tissue, calpain 3 localizes at several regions of the sarcomere through binding to the giant protein, titin
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calpain 3 activity promotes turnover of AHNAK in cell culture and in skeletal muscle
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fasting and refeeding has no effect on calpain-3 mRNA or protein level
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the amount of autolyzed calpain-3 is unchanged immediately and 3 h after exercise, but increases markedly (from 16% to 35% of total) 24 h after the exercise, and returns to preexercise levels within 7 days
mRNA level of calpain 3 is highest in the longissimus thoracis et lumborum, followed by semimembranosus, psoas major, and semitendinosus
mRNA for p94 exists only in skeletal muscle with none detected in other tissues including heart muscle and smooth muscles such as intestine
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virtually all calpain-3 present in mature muscle fibers is tightly bound in the vicinity of the titin N2A line and triad junctions, most calpain-3 is evidently bound within the contractile filament lattice
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calpain 3 may be involved in the mechanism of exogenous growth hormone action on skeletal muscle growth. Recombinant porcine growth hormone up-regulates mRNA expression of calpain 3 in a muscle type-specific manner, being more remarkable in semitendinosus muscles than in longissimus dorsi
from quadriceps femoris and the soleus muscles. A series of p94 splice variants is expressed immediately after muscle differentiation and differentially change localization during myofibrillogenesis. Endogenous N-terminal (but not C-terminal) domain of p94 is not only localized in the Z-bands but also directly bound to sarcomeric alpha-actinin. Incorporation of proteolytic N-terminal fragments of p94 into the Z-bands. In myofibrils localization of exogenously expressed p94 shifts from the M-line to N2A as the sarcomere lengthens beyond about 0.0026 and 0.0028 mm for wild-type and protease inactive p94, respectively
from quadriceps femoris and the soleus muscles. A series of p94 splice variants is expressed immediately after muscle differentiation and differentially change localization during myofibrillogenesis. Endogenous N-terminal (but not C-terminal) domain of p94 is not only localized in the Z-bands but also directly bound to sarcomeric alpha-actinin. Incorporation of proteolytic N-terminal fragments of p94 into the Z-bands. In myofibrils localization of exogenously expressed p94 shifts from the M-line to N2A as the sarcomere lengthens beyond about 0.0026 and 0.0028 mm for wild-type and protease inactive p94, respectively
