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Information on EC 3.4.22.B24 - calpain 4

for references in articles please use BRENDA:EC3.4.22.B24
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.B24 calpain 4
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This record set is specific for:
UNIPROT: Q64537
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
broad endopeptidase specificity
Synonyms
capn4, calpain small subunit 1, calpain 4, css-1, calpain regulatory subunit, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calcium-activated neutral proteinase
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-
-
-
calpain regulatory subunit
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-
-
-
CANP
-
-
-
-
Capn4
-
-
-
-
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
-
-
-
?
additional information
?
-
limited proteolysis of substrates involved in cytoskeletal remodelling and signal transduction
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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
additional information
?
-
limited proteolysis of substrates involved in cytoskeletal remodelling and signal transduction
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
the enzyme contains 4 EF-hand calcium-binding domains
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
translocates to the plasma membrane upon Ca2+ binding
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CPNS1_RAT
270
0
28570
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
heterodimer of a large and a small subunit
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Bos taurus (P13135), Homo sapiens (P04632), Mus musculus (O88456), Rattus norvegicus (Q64537), Sus scrofa (P04574)
Manually annotated by BRENDA team
Sorimachi, H.; Amano, S.; Ishiura, S.; Suzuki, K.
Primary sequences of rat mu-calpain large and small subunits are, respectively, moderately and highly similar to those of human
Biochim. Biophys. Acta
1309
37-41
1996
Rattus norvegicus (Q64537)
Manually annotated by BRENDA team
Graham-Siegenthaler, K.; Gauthier, S.; Davies, P.L.; Elce, J.S.
Active recombinant rat calpain II. Bacterially produced large and small subvunits associate both in vivo and in vitro
J. Biol. Chem.
269
30457-30460
1994
Rattus norvegicus (Q64537)
Manually annotated by BRENDA team
Blanchard, H.; Grochulski, P.; Li, Y.; Arthur, J.S.C.; Davies, P.L.; Elce, J.S.; Cygler, M.
Structure of a calapin ca2+-binding domain revewals a novel EF-hand and Ca(2+)-induced conformation changes
Nat. Struct. Biol.
4
532-538
1997
Rattus norvegicus (Q64537)
Manually annotated by BRENDA team