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Information on EC 3.4.22.B28 - calpain 8 and Organism(s) Mus musculus and UniProt Accession Q91VA3

for references in articles please use BRENDA:EC3.4.22.B28
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.B28 calpain 8
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This record set is specific for:
Mus musculus
UNIPROT: Q91VA3
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
broad endopeptidase specificity
Synonyms
calpain, capn9, capn8, ncl-2', calpain 8, capn 8, stomach-specific calpain, ncl-2/calpain 8, calpain 8/ncl-2, calpain-8a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calpain 8/nCL-2
-
calpain
-
-
calpain-8a
-
-
CAPN 8
-
-
-
-
nCL-2
nCL-2'
-
-
-
-
nCL-2/calpain 8
-
-
stomach specific calpain nCL-2
-
-
-
-
stomach-specific calpain
-
-
-
-
additional information
calpains constitute a superfamily of Ca2+-dependent cysteine proteases
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
peptide + H2O
hydrolyzed peptide
show the reaction diagram
-
-
-
?
beta-subunit of the coat protein + H2O
?
show the reaction diagram
-
30°C, 5 mM Ca2+
-
-
?
calpain 8 + H2O
?
show the reaction diagram
-
one of the autolysis sites is between Ala5 and Ala6
-
-
?
peptide + H2O
hydrolyzed peptide
show the reaction diagram
additional information
?
-
calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, in which both molecules are essential for activity, and that is involved in gastric mucosal defense. Calpains 8 and 9 are regulated differently from each other and from conventional calpains and, thus, have potentially important, specific functions in the gastrointestinal tract. Calpains 8 and 9 are molecular chaperones for each other, overview
-
-
?
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
peptide + H2O
hydrolyzed peptide
show the reaction diagram
-
specific regulatory function of the enzyme in digestive tract
-
-
?
additional information
?
-
calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, in which both molecules are essential for activity, and that is involved in gastric mucosal defense. Calpains 8 and 9 are regulated differently from each other and from conventional calpains and, thus, have potentially important, specific functions in the gastrointestinal tract. Calpains 8 and 9 are molecular chaperones for each other, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
dependent on
Ca2+
-
Ca2+-dependent activity, with half-maximal activity at about 0.3 mM Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
calpain inhibitor I
-
0.010 mM
calpeptin
-
0.010 mM
E64c
-
0.050 mM
MG132
-
0.010 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
optimal temperature for nCL-2 activity is 20°C. The time courses of nCL-2 activity at various temperatures shows that the initial rates are maximal at 30-37°C, whereas maximal activity is achieved at 15°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
gastric
Manually annotated by BRENDA team
calpain 8/nCL-2 is predominantly expressed in the gastrointestinal tract and is restricted to the gastric surface mucus cells in the stomach
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
in the gastric epithelium
Manually annotated by BRENDA team
-
mucus-secreting goblet cell in the duodenum
Manually annotated by BRENDA team
-
diaphragm
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
mucous cells
Manually annotated by BRENDA team
-
COS7 cells
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
calpain 8 is involved in vesicle trafficking between endoplasmic reticulum and Golgi. Calpain 8/nCL-2 is also involved in the mucosal defense against stress-induced gastropathies
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAN8_MOUSE
703
0
79335
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
oligomer
-
stomach-specific calpain, nCL-2/calpain 8, is active without calpain regulatory subunit and oligomerizes through C2-like domains. nCL-2 exists in both monomeric and homo-oligomeric forms, but not as a heterodimer with 30K or 30K-2, and that the oligomerization occurs through domains other than the 5EF-hand domain IV, most probably through domain III
additional information
enzyme domain structure with prodomain, protease domain, C2-like domain, and 5EF-hand domain
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
generation of Capn8-/- mice, that are fertile and whose gastric mucosae appears normal. However, the mutant mice are susceptible to gastric mucosal injury induced by ethanol administration, and the Capn8-/- stomach shows significant decreases in both calpains 9 and 8, and the same was true for Capn9-/-. Effects of calpain 8 deficiency on mucous granule formation and secretion, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
recombinant protein from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expression in Escherichia coli
-
nCL-2 and nCL-2' are generated by alternative splicing of the same gene Capn8
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hata, S.; Nishi, K.; Kawamoto, T.; lee, H.; Kawahara, H.; Maeda, T.; Shintani, Y.; Sorimachi, H.; Suzuki, K.
Both the conserved and unique gene structure of stomach-specific calpains reveal processes of calpain gene evolution
J. Mol. Evol.
53
191-203
2001
Mus musculus, Mus musculus (Q91VA3)
Manually annotated by BRENDA team
Braun, C.; Engel, M.; Theisinger, B.; Welter, C.; Seifert, M.
CAPN 8: isolation of a new mouse calpain-isoenzyme
Biochem. Biophys. Res. Commun.
260
671-675
1999
Mus musculus
Manually annotated by BRENDA team
Hata, S.; Koyama, S.; Kawahara, H.; Doi, N.; Maeda, T.; Toyama-Sorimachi, N.; Abe, K.; Suzuki, K.; Sorimachi, H.
Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the beta-subunit of coatomer complex, beta-COP
J. Biol. Chem.
281
11214-11224
2006
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Hata, S.; Doi, N.; Kitamura, F.; Sorimachi, H.
Stomach-specific calpain, nCL-2/calpain 8, is active without calpain regulatory subunit and oligomerizes through C2-like domains
J. Biol. Chem.
282
27847-27856
2007
Mus musculus
Manually annotated by BRENDA team
Hata, S.; Abe, M.; Suzuki, H.; Kitamura, F.; Toyama-Sorimachi, N.; Abe, K.; Sakimura, K.; Sorimachi, H.
Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense
PLoS Genet.
6
e1001040
2010
Mus musculus (Q91VA3)
Manually annotated by BRENDA team