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Information on EC 3.4.22.B27 - calpain 7
for references in articles please use BRENDA:EC3.4.22.B27preliminary BRENDA-supplied EC number
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EC Tree
3.4.22.B27 calpain 7Specify your search results
Word Map
- 3.4.22.B27
- calpains
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endosomal
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escrt
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escrt-iii
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penta-ef-hand
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hek293t
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autolytic
- ist1
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mit-interacting
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flag-tagged
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microtubule-interacting
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pulldown
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multivesicular
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strep-tagged
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epitope-tagged
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chmp1b
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calpain-like
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calcium-activated
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dominant-negative
The enzyme appears in viruses and cellular organisms
Synonyms
calpain-7, capn7, calpain 7, palbh, capn 7, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
calpain-7
capn 7
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-
-
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PalB homolog
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-
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PalBH
PalBH
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
broad endopeptidase specificity
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-
-
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broad endopeptidase specificity
the cleavage site of calpain-7 is P4-LLAK-P1 and P1'-KEGITGP-P7'
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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endopeptidase
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hydrolysis of peptide bond
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peptides, endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY
78990-62-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
C-terminally truncated ALG-2-interacting protein X + H2O
?
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
?
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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-
?
additional information
?
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calpain 7 plays roles in the endosomal pathway by interacting with a subset of ESCRT-III-related proteins
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?
additional information
?
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C-terminal deletion mutants of charged multivesicular body protein 1B enhances autolytic activity of calpain-7 in cells
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-
?
additional information
?
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GST-MIM protein enhances the autolysis of purified Strep-tagged monomeric green fluorescent protein-fused calpain 7. Calpain 7 is activated in the endosomal sorting complex required for transport system
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-
?
additional information
?
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GST-MIM protein enhances the autolysis of purified Strep-tagged monomeric green fluorescent protein-fused calpain 7. Calpain 7 is activated in the endosomal sorting complex required for transport system
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-
?
additional information
?
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the enzyme interacts with a subset of endosomal sorting complex required for transport (ESCRT)-III and ESCRT-III-related proteins, including charged multivesicular body protein 1
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-
?
additional information
?
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calpain-7 performs autolysis, ESCRT proteins enhance the calpain-7 autolysis. Engineered FLAG-tagged casein-Bro1 domain is no substrate
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
calpain 7 plays roles in the endosomal pathway by interacting with a subset of ESCRT-III-related proteins
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-
?
additional information
?
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C-terminal deletion mutants of charged multivesicular body protein 1B enhances autolytic activity of calpain-7 in cells
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-
?
additional information
?
-
GST-MIM protein enhances the autolysis of purified Strep-tagged monomeric green fluorescent protein-fused calpain 7. Calpain 7 is activated in the endosomal sorting complex required for transport system
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-
?
additional information
?
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GST-MIM protein enhances the autolysis of purified Strep-tagged monomeric green fluorescent protein-fused calpain 7. Calpain 7 is activated in the endosomal sorting complex required for transport system
-
-
?
additional information
?
-
the enzyme interacts with a subset of endosomal sorting complex required for transport (ESCRT)-III and ESCRT-III-related proteins, including charged multivesicular body protein 1
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
endosomal sorting complex required for transport (ESCRT) system proteins increase the enzyme activity and autolysis, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Colonic Neoplasms
LINC00657 promotes the development of colon cancer by activating PI3K/AKT pathway.
Neoplasms
[Mir-29c-3p targeting TUG1 affects migration and invasion of bladder cancer cells by regulating CAPN7 expression].
Urinary Bladder Neoplasms
[Mir-29c-3p targeting TUG1 affects migration and invasion of bladder cancer cells by regulating CAPN7 expression].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme functions on the endosomal membranes. Involvement of IST1 in mobilization of the enzyme to epidermal growth factor receptor-positive endosomes
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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
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
additional information
calpain-7 is a unique intracellular cysteine protease that has a tandem repeat of microtubule interacting and trafficking domains and lacks a penta-EF-hand domain. The catalytic residues are C290, H458 and N478
additional information
importance of not only the N-terminal microtubule-interacting and trafficking domains but also the C-terminal C2 domain-like domains for proteolytic activity of the enzyme
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C290S
C290S
site-directed mutagenesis, active site mutant, catalytically inactive mutant
C290S
site-directed mutagenesis, catalytically inactive mutant, the mGFP-CAPN7C290S mutant exhibits dominant-negative effects on epidermal growth factor receptor degradation
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose beads chromatography and Strep-Tactin Sepharose beads chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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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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
Homo sapiens (Q7Z479), Homo sapiens (Q9Y6W3), Mus musculus (Q9R1S8)
brenda
Strausberg R.L.; Feingold E.A.; Grouse L.H.; Derge J.G.; et al.
Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences
Proc. Natl. Acad. Sci. USA
99
16899-16903
2002
Homo sapiens (Q7Z479)
brenda
Futai, E.; Kubo, T.; Sorimachi, H.; Suzuki, K.; Maeda, T.
Molecular cloning of PalBH, a mammalian homologue of the Aspergillus atypical calpain PALB.
Biochim. Biophys. Acta
1517
316-319
2001
Mus musculus (Q9R1S8), Mus musculus, Homo sapiens (Q9Y6W3), Homo sapiens
brenda
Franz, T.; Vingron, M.; Boehm, T.; Dear.T.N.
Capn7: a highly divergent vertebrate calpain with a novel C-terminal domain
Mamm. Genome
10
318-321
1999
Mus musculus (Q9R1S8)
brenda
Yorikawa, C.; Takaya, E.; Osako, Y.; Tanaka, R.; Terasawa, Y.; Hamakubo, T.; Mochizuki, Y.; Iwanari, H.; Kodama, T.; Maeda, T.; Hitomi, K.; Shibata, H.; Maki, M.
Human calpain 7/PalBH associates with a subset of ESCRT-III-related proteins in its N-terminal region and partly localizes to endocytic membrane compartments
J. Biochem.
143
731-745
2008
Homo sapiens
brenda
Osako, Y.; Maemoto, Y.; Tanaka, R.; Suzuki, H.; Shibata, H.; Maki, M.
Autolytic activity of human calpain 7 is enhanced by ESCRT-III-related protein IST1 through MIT-MIM interaction
FEBS J.
277
4412-4426
2010
Homo sapiens (Q9Y6W3), Homo sapiens
brenda
Maemoto, Y.; Osako, Y.; Goto, E.; Nozawa, E.; Shibata, H.; Maki, M.
Calpain-7 binds to CHMP1B at its second alpha-helical region and forms a ternary complex with IST1
J. Biochem.
150
411-421
2011
Homo sapiens
brenda
Maemoto, Y.; Kiso, S.; Shibata, H.; Maki, M.
Analysis of limited proteolytic activity of calpain-7 using non-physiological substrates in mammalian cells
FEBS J.
280
2594-2607
2013
Homo sapiens (Q9Y6W3)
brenda
Maemoto, Y.; Ono, Y.; Kiso, S.; Shibata, H.; Takahara, T.; Sorimachi, H.; Maki, M.
Involvement of calpain-7 in epidermal growth factor receptor degradation via the endosomal sorting pathway
FEBS J.
281
3642-3655
2014
Homo sapiens (Q9Y6W3)
brenda
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Release 2023.1 (January 2023)
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