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Information on EC 3.4.22.B27 - calpain 7 and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC3.4.22.B27
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.B27 calpain 7
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This record set is specific for:
Homo sapiens
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Word Map
  • 3.4.22.B27
  • calpains
  • endosomal
  • escrt
  • escrt-iii
  • penta-ef-hand
  • hek293t
  • autolytic
  • ist1
  • mit-interacting
  • flag-tagged
  • microtubule-interacting
  • pulldown
  • multivesicular
  • strep-tagged
  • epitope-tagged
  • chmp1b
  • calpain-like
  • calcium-activated
  • dominant-negative
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
broad endopeptidase specificity
Synonyms
calpain-7, capn7, calpain 7, palbh, capn 7, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calpain 7/PalBH
-
-
calpain-7
capn 7
-
-
-
-
PalB homolog
-
-
-
-
PalBH
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
broad endopeptidase specificity
show the reaction diagram
the cleavage site of calpain-7 is P4-LLAK-P1 and P1'-KEGITGP-P7'
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
C-terminally truncated ALG-2-interacting protein X + H2O
?
show the reaction diagram
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
-
-
?
domain 1 of calpastatin-Bro1 domain fuion protein + H2O
?
show the reaction diagram
the calpain-7 cleavage site is located between ELLAK (207-211) and KEGIT(212-216) at the C-terminal border of sub-domain B
-
-
?
increased sodium tolerance-1 protein + H2O
?
show the reaction diagram
peptide + H2O
hydrolyzed peptide
show the reaction diagram
additional information
?
-
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
increased sodium tolerance-1 protein + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
dependent on
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
endosomal sorting complex required for transport (ESCRT) system proteins increase the enzyme activity and autolysis, overview
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q7Z479_HUMAN
813
0
92653
TrEMBL
-
CAN7_HUMAN
813
0
92652
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
x * 100000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 100000, SDS-PAGE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C290A
active site mutant
C290S
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose beads chromatography and Strep-Tactin Sepharose beads chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK293T cells
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
stable HEK293T transfectants of Strep-tagged calpain 7
-
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Homo sapiens (Q9Y6W3), Homo sapiens, Mus musculus (Q9R1S8), Mus musculus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team