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Information on EC 3.4.22.41 - cathepsin F
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3.4.22.41 cathepsin FSpecify your search results
Word Map
- 3.4.22.41
- cathepsins
- diagnostics
- westermani
- viroid
- paragonimus
-
f-like
- food industry
- metalloproteinase-10
-
cystatin-like
- viverrini
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
cathepsin f, cf-11, ov-cf-1, pwcp2, pwcp5, cat f, tci-cf-1, pwcp1, pwcp3, pwcp4, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CatF
cathepsin f
CATSF
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (kcat/Km) comparable to that of cathepsin L
The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (kcat/Km) comparable to that of cathepsin L
endopeptidase
-
-
-
The recombinant enzyme cleaves synthetic substrates with Phe and Leu (better than Val) in P2, with high specificity constant (kcat/Km) comparable to that of cathepsin L
Cathepsin F is a lysosomal cysteine endopeptidase of family C1, papain family, most activite at pH 5.9. The enzyme is unstable at neutral pH values and is inhibited by compound E-64. Cathepsin F is expressed in most tissues of human, mouse and rat. Human gene locus: 11q13.1-13.3
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
65997-74-2
-
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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
Albumin + H2O
?
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
low activity
-
-
?
benzyloxycarbonyl-L-leucine-L-arginine-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-leucine-L-arginine + 7-amino-4-methylcoumarin
-
high catalytic activity with isozymes CF-4 and CF-11
-
-
?
benzyloxycarbonyl-L-leucyl-L-arginyl-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-leucyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-phenylalanine-L-arginine-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-phenylalanine-L-arginine + 7-amino-4-methylcoumarin
-
high catalytic activity with isozymes CF-4 and CF-11
-
-
?
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
high activity
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
high activity
-
-
?
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin + H2O
?
-
very low activity
-
-
?
Collagen + H2O
?
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
Gelatin + H2O
?
purified CtF is capable of hydrolyzing 0.1% gelatin at pH 7.5
-
-
?
immunoglobulin A + H2O
?
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
immunoglobulin G + H2O
?
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
immunoglobulin M + H2O
?
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
N-acetyl-DEVD-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Arg-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
N-benzyloxycarbonyl-L-Val-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
very low activity
-
-
?
tert-butyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
-
highest activity
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
very low activity
-
-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
very low activity
-
-
?
tosyl-Gly-Pro-Lys-7-amido-4-methylcoumarin + H2O
?
-
very low activity
-
-
?
Hemoglobin + H2O
?
-
substrate of isozyme CF-4 at pH 6.5 and CF-11 at pH 5.5 but not at neutral pH
-
-
?
Hemoglobin + H2O
?
-
cathepsin F and cathepsin B can work in concert to hydrolyse hemoglobin at low pH
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
?
additional information
?
-
-
the isozymes CF-4, CF-6, and CF-11 do not hydrolyze benzyloxycarbonyl-L-arginine-L-arginine-7-amido-4-methylcoumarin and benzyloxycarbonyl-L-arginine-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
the enzyme likely plays a regulatory role in the processing in the invariant chain that is assoviated with the major histocompatibility complex class II
-
?
additional information
?
-
-
the enzyme plays a role in tumor-induced angiogenesis, cell migration, proliferation, apoptosis, and connective tissue degradation
-
-
?
additional information
?
-
-
the enzyme is a cysteine protease and modifies low density lipoprotein particles in vitro
-
-
?
additional information
?
-
-
involved in atherosclerotic inflammatory processes
-
-
?
additional information
?
-
-
cathepsin F degrades extracellular matrix proteins more effectively than capthespin B1 at physiological pH
-
-
?
additional information
?
-
-
the fully activated cathepsin F cleaves fluorogenic-NHMec substrates with the preference Val-Leu-Arg>Leu-Arg>Phe-Arg>Arg-Arg with little or no activity against Pro-Arg or Pro-Lys substrates
-
-
?
additional information
?
-
the enzyme is not able to hydrolyze protein substrates such as azocasein, fibrinogen, and bovine serum albumin
-
-
?
additional information
?
-
-
the enzyme is not able to hydrolyze protein substrates such as azocasein, fibrinogen, and bovine serum albumin
-
-
?
additional information
?
-
cathepsin F-1 is developmentally regulated
-
-
?
additional information
?
-
-
cathepsin F-1 is developmentally regulated
-
-
?
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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
Hemoglobin + H2O
?
-
cathepsin F and cathepsin B can work in concert to hydrolyse hemoglobin at low pH
-
-
?
additional information
?
-
-
the enzyme likely plays a regulatory role in the processing in the invariant chain that is assoviated with the major histocompatibility complex class II
-
?
additional information
?
-
-
the enzyme plays a role in tumor-induced angiogenesis, cell migration, proliferation, apoptosis, and connective tissue degradation
-
-
?
additional information
?
-
-
involved in atherosclerotic inflammatory processes
-
-
?
additional information
?
-
-
cathepsin F degrades extracellular matrix proteins more effectively than capthespin B1 at physiological pH
-
-
?
additional information
?
-
cathepsin F-1 is developmentally regulated
-
-
?
additional information
?
-
-
cathepsin F-1 is developmentally regulated
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
JPM565
-
radioactive-labeling by 125I, irrevrsible inhibitor of papin-type cathepsins, active site labeling
morpholine urea-Leu-homophenylalaninevinyl sulfone-phenyl
potent and irreversible inhibitor of cysteine proteases
additional information
-
the prodomain effectively inhibits the enzyme in which the ERFNAQ motif plays a critical role in the inhibition, but the GTFD motif is also required for complete inhibition
-
additional information
downregulation of cathepsin F mRNA by E-64d; treatment with retinol/palmitic acid increases mRNA-level of cystatin B coupled with decrease in cathepsin F activity; treatment with retinol/palmitic acid increases mRNA-level of cystatin C coupled with decrease in cathepsin F activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
human aortic proteoglycans
-
activates apoB-100/LDL degradation by cathepsin F
-
additional information
-
cathepsin F is secreted as an inactive zymogen that autocatalytically processes and activates to a mature enzyme at pH 4.5 (after 6 h incubation) via an intermolecular cleavage at the prosegment-mature domain junction, the active cathepsin B1 zymogen is capable of trans-activating cathepsin F by proteolytic removal of its prosegment at pH 5.5
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Long noncoding RNA LINC00982 upregulates CTSF expression to inhibit gastric cancer progression via the transcription factor HEY1.
Atherosclerosis
Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro.
Carcinogenesis
Long noncoding RNA LINC00982 upregulates CTSF expression to inhibit gastric cancer progression via the transcription factor HEY1.
cathepsin f deficiency
Murine cathepsin f deficiency causes neuronal lipofuscinosis and late-onset neurological disease.
Cholangiocarcinoma
Secreted cysteine proteases of the carcinogenic liver fluke, Opisthorchis viverrini: regulation of cathepsin F activation by autocatalysis and trans-processing by cathepsin B.
Infections
Expression of Cathepsin F in response to bacterial challenges in Yesso scallop Patinopecten yessoensis.
Neoplasms
Cathepsin F Knockdown Induces Proliferation and Inhibits Apoptosis in Gastric Cancer Cells.
Neuronal Ceroid-Lipofuscinoses
Cathepsin F mutations cause Type B Kufs disease, an adult-onset neuronal ceroid lipofuscinosis.
Opisthorchiasis
Chicken IgY-based coproantigen capture ELISA for diagnosis of human opisthorchiasis.
Paragonimiasis
Cloning and characterization of a new cysteine proteinase secreted by Paragonimus westermani adult worms.
Paragonimiasis
Expression characteristics and specific antibody reactivity of diverse cathepsin F members of Paragonimus westermani.
Radiodermatitis
Adipose-derived stem cells alleviate radiation-induced dermatitis by suppressing apoptosis and downregulating cathepsin F expression.
Stomach Neoplasms
Cathepsin F Knockdown Induces Proliferation and Inhibits Apoptosis in Gastric Cancer Cells.
Stomach Neoplasms
Long noncoding RNA LINC00982 upregulates CTSF expression to inhibit gastric cancer progression via the transcription factor HEY1.
Uterine Cervical Neoplasms
Overexpression of cathepsin f, matrix metalloproteinases 11 and 12 in cervical cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
pH 6.5, room temperature, mutant enzyme N97Q/N108Q/N170Q
0.017
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
pH 6.5, room temperature, wild-type enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
pH 6.5, room temperature, mutant enzyme N97Q/N108Q/N170Q
2.9
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide
-
pH 6.5, room temperature, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.3
benzyloxycarbonyl-L-leucine-L-arginine-7-amido-4-methylcoumarin
-
isozyme CF-11, in 100 mM sodium phosphate (pH 5.5), at 37°C
7.6
benzyloxycarbonyl-L-leucine-L-arginine-7-amido-4-methylcoumarin
-
isozyme CF-4, in 100 mM sodium phosphate (pH 6.5), at 37°C
6
benzyloxycarbonyl-L-phenylalanine-L-arginine-7-amido-4-methylcoumarin
-
isozyme CF-11, in 100 mM sodium phosphate (pH 5.5), at 37°C
8.2
benzyloxycarbonyl-L-phenylalanine-L-arginine-7-amido-4-methylcoumarin
-
isozyme CF-4, in 100 mM sodium phosphate (pH 6.5), at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
adding E-64d (inhibitor) results in drastically inhibition of enzyme activity in cytosol and nucleus, fluorescence-labeled peptide substrate (benzyloxycarbonyl-Leu-Arg-4-methylcoumaryl-7-amide) with excitation wavelength 380 nm and emission wavelength 460 nm, confirmed by cathepsin F siRNA treatment
additional information
higher activity in nucleus than in cytosol, fluorescence-labeled peptide substrate (benzyloxycarbonyl-Leu-Arg-4-methylcoumaryl-7-amide) with excitation wavelength 380 nm and emission wavelength 460 nm, differentiation between cathepsin F and other cathepsins by using specific inhibitors and substrates
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6.5
5.5
substrate benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6
modest enzyme activity, substrates hemoglobin and gelatin
4.5 - 8
substrate benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide
additional information
-
slightly acidic pH optimum, rapid inactivation at neutral pH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
production of cathepsin F is increased by stimulation of cells with angiotensin, level of lysosomal enzyme remains unaffected but more enzyme is secreted
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
immunostaining using anti-PoCtF antibody was strongest on the epidermal mucus in the fin
brenda
expression in hepatopancreas is significantly the highest among all different healthy tissues. More than 100fold compared to its expression in adductor muscle and more than 10fold compared to its expression in kidney
brenda
expressed at the lowest level in muscles
brenda
additional information
-
CFs are synthesized in the epithelial cells lining the parasite intestine and secreted into the intestinal lumen
brenda
additional information
-
expression mainly in coronary atherosclerotic plaques
brenda
additional information
-
no CTSF expression in healthy cervical epithelium
brenda
additional information
ubiquitous expression throughout the entirety of healthy tissues
brenda
additional information
-
ubiquitous expression throughout the entirety of healthy tissues
brenda
additional information
temporal/developmental expression pattern
brenda
additional information
-
temporal/developmental expression pattern
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
lysosomal enzyme can be secreted into the extracellular medium
-
brenda
immunofluorescence microscopy, fluorescence-labeled peptide substrate (benzyloxycarbonyl-Leucin-Arginin-4-methylcoumaryl-7-amide) with excitation wavelength 380 nm and emission wavelength 460 nm
brenda
Western blot, immunofluorescence microscopy, fluorescence-labeled peptide substrate (benzyloxycarbonyl-Leu-Arg-4-methylcoumaryl-7-amide) with excitation wavelength 380 nm and emission wavelength 460 nm
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
secreted cysteine protease Clonorchis sienesis cathepsin F plays a critical role as a virulence factor in the development and progression of various diseases. The enzyme plays an important role in parasite nutrition and hostparasite interaction
physiological function
physiological function
cathepsin F is implicated in the growth and reproduction regulation
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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). CATF_HUMAN
484
0
53366
Swiss-Prot
Secretory Pathway (Reliability: 1)
CATF_MOUSE
462
0
51661
Swiss-Prot
Secretory Pathway (Reliability: 1)
G7JL32_MEDTR
331
1
37102
TrEMBL
Secretory Pathway (Reliability: 1)
G7JIL2_MEDTR
362
0
39844
TrEMBL
Secretory Pathway (Reliability: 2)
C4B4C8_MANSE
2676
0
303616
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8B6GN74_MYTGA
630
0
71546
TrEMBL
other Location (Reliability: 2)
A0A5B7A823_DAVIN
322
0
35660
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9H3L9_9LAMI
384
0
42353
TrEMBL
Secretory Pathway (Reliability: 1)
C1L5B1_SCHJA
454
0
52108
TrEMBL
Secretory Pathway (Reliability: 4)
Q2I8Y2_TELCI
364
0
41097
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7CDV4_DAVIN
265
0
28672
TrEMBL
Mitochondrion (Reliability: 4)
A0A5B7BLW9_DAVIN
119
0
14418
TrEMBL
other Location (Reliability: 1)
A0A6J8DYP3_MYTCO
329
0
36596
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8B6FYR5_MYTGA
205
0
23770
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9G4W9_9LAMI
379
0
41447
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7BB88_DAVIN
240
0
26718
TrEMBL
Secretory Pathway (Reliability: 2)
Q08CH0_DANRE
473
0
52724
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7C4I5_DAVIN
173
0
18569
TrEMBL
other Location (Reliability: 2)
G7JMA4_MEDTR
327
1
36550
TrEMBL
Secretory Pathway (Reliability: 1)
A8E4X3_XENTR
463
0
52137
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6J8BXE3_MYTCO
363
0
41607
TrEMBL
other Location (Reliability: 2)
Q0Q4H0_PIG
131
0
14566
TrEMBL
other Location (Reliability: 3)
A0A8B6FWY3_MYTGA
381
0
42328
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6J8E119_MYTCO
279
0
31688
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6J8EVJ6_MYTCO
789
0
89756
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6PPQ1_ROSCH
374
0
41474
TrEMBL
Secretory Pathway (Reliability: 2)
A0A5B7A577_DAVIN
353
0
39096
TrEMBL
Secretory Pathway (Reliability: 3)
A0A5B7A6V3_DAVIN
276
0
31292
TrEMBL
Secretory Pathway (Reliability: 3)
A0A396I7A4_MEDTR
372
0
41858
TrEMBL
Mitochondrion (Reliability: 5)
E0VNU3_PEDHC
434
0
49781
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9GCC8_9LAMI
370
0
40516
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7BVE4_DAVIN
228
0
25030
TrEMBL
other Location (Reliability: 2)
A0A2P6RA02_ROSCH
146
0
16277
TrEMBL
Mitochondrion (Reliability: 5)
A0A061I8I4_CRIGR
456
0
50987
TrEMBL
Secretory Pathway (Reliability: 1)
B9T558_RICCO
381
1
41728
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7A5C4_DAVIN
277
0
31260
TrEMBL
Secretory Pathway (Reliability: 2)
O46177_9TREM
325
0
36722
TrEMBL
Chloroplast (Reliability: 2)
Q218Y2_RHOPB
Rhodopseudomonas palustris (strain BisB18)
121
0
13126
TrEMBL
-
Q2QKD7_9TREM
322
0
36023
TrEMBL
Chloroplast (Reliability: 3)
Q2QKD8_9TREM
325
0
36638
TrEMBL
Chloroplast (Reliability: 1)
Q2QKD9_9TREM
325
0
36511
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33860
302 amino acid protein composed of a 88 residue propeptide and a 214 residue mature enzyme
41000
-
cathepsin F proenzyme in the yeast medium is present as two major protein bands migrating at 41000 Da and 47000 Da as a result of differential addition of N-linked glycans
47000
-
cathepsin F proenzyme in the yeast medium is present as two major protein bands migrating at 41000 Da and 47000 Da as a result of differential addition of N-linked glycans
additional information
additional information
composed of a 88 residue propeptide and a 214 residue mature enzyme, no signal peptide
additional information
-
composed of a 88 residue propeptide and a 214 residue mature enzyme, no signal peptide
additional information
cathepsin F exhibits a very long propeptide of 251 residues which distinguishes this enzyme form all other cathepsins
additional information
-
cathepsin F exhibits a very long propeptide of 251 residues which distinguishes this enzyme form all other cathepsins
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
additional information
glycoprotein
four putative N-glycosylation site, one in the propeptide at Asn13, three in the mature region at Asn185, Asn196, Asn258 , no evidence of usage for in vivo glycosylation
glycoprotein
five potential glycosylation sites at positions 141p, 176p of the signal sequence and 97, 108, 170 of the mature enzyme
glycoprotein
-
the enzyme contains three potential N-linked glycosylation sites in the mature region: N97 and N108 and N170
additional information
recombinant expression results in zymogen which needs to be activated, recombinant Ov-CF-1 does not autocatalytically process and activate at pH 4.5, activation can be accomplished by Fasciola hepatica cathepsin L1
additional information
-
recombinant expression results in zymogen which needs to be activated, recombinant Ov-CF-1 does not autocatalytically process and activate at pH 4.5, activation can be accomplished by Fasciola hepatica cathepsin L1
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method, 1.7 A structure of the mature domain of cathepsin F associated with an irreversible vinyl sulfone inhibitor
-
hanging-drop vapour diffusion method, mutant cathepsin F, N97Q/N108Q/N170Q, complexed with an irreversible vinyl sulfone inhibitor
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N97Q/N108Q/N170Q
-
KM-value for benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide is 2fold higher than that of the wild-type enzyme, the turnover number is 2fold lower
additional information
-
generation of cat F-deficient mice by homologous recombination, the mutation leads to weight loss and death within 6 months, deficient neurons accumulate eosiniophilic granules causing neuronal ceroid lipofuscinosis beginning as early as 6 weeks of age, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
-
isozyme CF-4 is relatively stable at slight acidic and neutral pHs, but is comparatively unstable in acidic pHs, isozyme CF-11 is stable at acidic pHs, but is highly unstable in neutral and alkaline pH values
709866
4.5
5
activity is greatly decreased at pH 5 (lysosomal pH) and below
708220
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
enhanced production and release of cathepsins in tumor cells leads to tumor cell growth, invasion and metastasis
-
expressed in Escherichia coli DH5alphaMCR cells using the pGEX-4 T-1 expression vector system
PCR with primers specific for the Camellia sinensis cathepsin F gene, 5'- and 3'-RACE used to clone and identify a coding sequence of 981 bp (AY821800). The Ov-cf-1 gene is organized into 7 exons. Phylogenetic analysis confirms relationship of Ov-CF-1 with other cathepsin F proteases.
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CtF expressions increases significantly in gill at 3 h post-injection with lipopolysaccharide
the accumulation of cathepsin F mRNA in early stage of development increases with development
the isozymes CF-4, CF-6, and CF-11 are expressed throughout various developmental stages of the parasite and the transcripts increased gradually in accordance with the maturation of the parasite
-
up-regulation of the gene in hemocytes in response to both Gram-negative and Gram-positive bacteria. Significantly up-regulated 3 h after infection of Vibrio anguillarum in hemocytes
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
for isozyme CF-4, the purified recombinant protein (10 mg) is slowly added to 1 l of 100 mM Tris-HCl (pH 8.0) containing 1 mM EDTA, 250 mM L-arginine, 5 mM reduced glutathione, and 1 mM oxidized glutathione and gently stirred at 4°C for 20 h. Isozyme CF-11 is refolded in 100 mM Tris-HCl (pH 8.0) containing 1 mM EDTA, 250 mM L-arginine, 10 mM reduced glutathione, and 1 mM oxidized glutathione with the same method
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
food industry
medicine
the enzyme is immunogenic and a possible target for development of vaccines for teladorsagiosis
diagnostics
paragonimiasis, caused by the lung fluke Paragonimus, is a major food-borne helminthic disease. Differential diagnosis of paragonimiasis from tuberculosis and other infectious granulomas in the lung is a prerequisite to proper management of patients. Diverse Cysteine proteases of Paragonimus westermani of the cathepsin F family participate in inducing specific antibody responses. Most Paragonimus westermani cathepsin F, except for PwCP2 (AAF21461),which shows negligible antibody responses, might be applicable for paragonimiasis serodiagnosis
diagnostics
paragonimiasis, caused by the lung fluke Paragonimus, is a major food-borne helminthic disease. Differential diagnosis of paragonimiasis from tuberculosis and other infectious granulomas in the lung is a prerequisite to proper management of patients. Diverse Cysteine proteases of Paragonimus westermani of the cathepsin F family participate in inducing specific antibody responses. Most Paragonimus westermani cathepsin F, except for PwCP2 (Q9U0G8),which shows negligible antibody responses, might be applicable for paragonimiasis serodiagnosis
food industry
-
CTSF gene (encoding cathepsin F) is a suitable marker for screening pigs to improve cured weight and yield for country ham production
food industry
-
CTSF gene is a suita marker for screening pigs to leimprove meat quality. CTSF gene is associated with estimated breeding values: average daily gain, lean cuts, and backfat thickness
food industry
-
CTSF gene is a suitable marker for screening pigs to improve meat quality. CTSF gene is associated with estimated breeding values: average daily gain, lean cuts, and backfat thickness
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Santamaria, I.; Velasco, G.; Pendas, A.M.; Paz, A.; Lopez-Otin, C.
Molecular cloning and structural and functional characterization of cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain
J. Biol. Chem.
274
13800-13809
1999
Homo sapiens (Q9UBX1), Homo sapiens
brenda
Nägler, D.K.; Sulea, T.; Menard, R.
Full length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen
Biochem. Biophys. Res. Commun.
257
313-318
1999
Homo sapiens (Q9UBX1), Homo sapiens
brenda
Wex, T.; Levy, B.; Wex, H.; Brömme, D.
Human cathepsins F and W: A new subgroup of cathepsins
Biochem. Biophys. Res. Commun.
259
401-407
1999
Homo sapiens
brenda
Wang, B.; Shi, G.P.; Yao, P.M.; Li, Z.; Chapman, H.A.; Brömme, D.
Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization
J. Biol. Chem.
273
32000-32008
1998
Homo sapiens (Q9UBX1), Homo sapiens
brenda
Wex, T.; Wex, H.; Brömme, D.
The human cathepsin F gene - a fusion product between an ancestral cathepsin and cystatin gene
Biol. chem.
380
1439-1442
1999
Homo sapiens
brenda
Shi, G.P.; Bryant, R.A.R.; Riese, R.; Verhelst, S.; Driessen, C.; Li, Z.; Brömme, D.; Ploegh, H.L.; Capman, H.A.
Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
J. Exp. Med.
191
1177-1185
2000
Mus musculus
brenda
Dingle, J.T.; Blow, A.M.J.; Barrett, A.J.; Martin, P.E.N.
Proteoglycan-degrading enzymes. A radiochemical assay method and the detection of a new enzyme, cathepsin F
Biochem. J.
167
775-785
1977
Oryctolagus cuniculus, Homo sapiens
brenda
Ho, J.D.; Meltser, Y.; Buggy, J.J.; Palmer, J.T.; Elrod, K.C.; Chan, H.; Mortara, K.D.; Somoza, J.R.
Expression, purification, crystallization and preliminary X-ray diffraction studies of human cathepsin F complexed with an irreversible vinyl sulfone inhibitor
Acta Crystallogr. Sect. D
58
2187-2190
2002
Homo sapiens
brenda
Somoza, J.R.; Palmer, J.T.; Ho, J.D.
The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators
J. Mol. Biol.
322
559-568
2002
Homo sapiens
brenda
Vazquez-Ortiz, G.; Pina-Sanchez, P.; Vazquez, K.; Duenas, A.; Taja, L.; Mendoza, P.; Garcia, J.A.; Salcedo, M.
Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer
BMC Cancer
5
68
2005
Homo sapiens
brenda
Redmond, D.L.; Smith, S.K.; Halliday, A.; Smith, W.D.; Jackson, F.; Knox, D.P.; Matthews, J.B.
An immunogenic cathepsin F secreted by the parasitic stages of Teladorsagia circumcincta
Int. J. Parasitol.
36
277-286
2006
Teladorsagia circumcincta (Q218Y2), Teladorsagia circumcincta
brenda
Oeoerni, K.; Sneck, M.; Broemme, D.; Pentikaeinen, M.O.; Lindstedt, K.A.; Maeyraenpaeae, M.; Aitio, H.; Kovanen, P.T.
Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro
J. Biol. Chem.
279
34776-34784
2004
Homo sapiens
brenda
Tang, C.H.; Lee, J.W.; Galvez, M.G.; Robillard, L.; Mole, S.E.; Chapman, H.A.
Murine cathepsin F deficiency causes neuronal lipofuscinosis and late-onset neurological disease
Mol. Cell. Biol.
26
2309-2316
2006
Mus musculus
brenda
Kaakinen, R.; Lindstedt, K.A.; Sneck, M.; Kovanen, P.T.; Ooerni, K.
Angiotensin II increases expression and secretion of cathepsin F in cultured human monocyte-derived macrophages: an angiotensin II type 2 receptor-mediated effect
Atherosclerosis
192
323-327
2007
Homo sapiens
brenda
Ramos, A.M.; Glenn, K.L.; Serenius, T.V.; Stalder, K.J.; Rothschild, M.F.
Genetic markers for the production of US country hams
J. Anim. Breed. Genet.
125
248-257
2008
Sus scrofa
brenda
Russo, V.; Fontanesi, L.; Scotti, E.; Beretti, F.; Davoli, R.; Nanni Costa, L.; Virgili, R.; Buttazzoni, L.
Single nucleotide polymorphisms in several porcine cathepsin genes are associated with growth, carcass, and production traits in Italian Large White pigs
J. Anim. Sci.
86
3300-3314
2008
Sus scrofa
brenda
Maubach, G.; Lim, M.C.; Zhuo, L.
Nuclear cathepsin F regulates activation markers in rat hepatic stellate cells
Mol. Biol. Cell
19
4238-4248
2008
Rattus norvegicus (Q499S6)
brenda
Kuester, D.; Lippert, H.; Roessner, A.; Krueger, S.
The cathepsin family and their role in colorectal cancer
Pathol. Res. Pract.
204
491-500
2008
Homo sapiens
brenda
Pinlaor, P.; Kaewpitoon, N.; Laha, T.; Sripa, B.; Kaewkes, S.; Morales, M.E.; Mann, V.H.; Parriott, S.K.; Suttiprapa, S.; Robinson, M.W.; To, J.; Dalton, J.P.; Loukas, A.; Brindley, P.J.
Cathepsin F cysteine protease of the human liver fluke, Opisthorchis viverrini
PLoS Negl. Trop. Dis.
3
e398
2009
Opisthorchis viverrini (Q5PXS3), Opisthorchis viverrini
brenda
Sripa, J.; Laha, T.; To, J.; Brindley, P.J.; Sripa, B.; Kaewkes, S.; Dalton, J.P.; Robinson, M.W.
Secreted cysteine proteases of the carcinogenic liver fluke, Opisthorchis viverrini: regulation of cathepsin F activation by autocatalysis and trans-processing by cathepsin B
Cell. Microbiol.
12
781-795
2010
Opisthorchis viverrini
brenda
Ahn, S.J.; Kim, N.Y.; Seo, J.S.; Je, J.E.; Sung, J.H.; Lee, S.H.; Kim, M.S.; Kim, J.K.; Chung, J.K.; Lee, H.H.
Molecular cloning, mRNA expression and enzymatic characterization of cathepsin F from olive flounder (Paralichthys olivaceus)
Comp. Biochem. Physiol. B
154
211-220
2009
Paralichthys olivaceus (B2Z446), Paralichthys olivaceus
brenda
Kang, J.M.; Bahk, Y.Y.; Cho, P.Y.; Hong, S.J.; Kim, T.S.; Sohn, W.M.; Na, B.K.
A family of cathepsin F cysteine proteases of Clonorchis sinensis is the major secreted proteins that are expressed in the intestine of the parasite
Mol. Biochem. Parasitol.
170
7-16
2010
Clonorchis sinensis
brenda
Kim, Y.; Paik, E.; Nam, B.; Kong, H.; Kim, W.; Lee, S.; Kim, K.
Molecular cloning and characterization of cathepsin F gene from olive flounder Paralichthys Olivaceus
Genes Genomics
32
137-142
2010
Paralichthys olivaceus (D2D3C5)
-
brenda
Jeric, B.; Dolenc, I.; Mihelic, M.; Klaric, M.; Zavasnik-Bergant, T.; Guncar, G.; Turk, B.; Turk, V.; Stoka, V.
N-terminally truncated forms of human cathepsin F accumulate in aggresome-like inclusions
Biochim. Biophys. Acta
1833
2254-2266
2013
Homo sapiens
brenda
Fuzita, F.J.; Pinkse, M.W.; Verhaert, P.D.; Lopes, A.R.
Cysteine cathepsins as digestive enzymes in the spider Nephilengys cruentata
Insect Biochem. Mol. Biol.
60
47-58
2015
Nephilengys cruentata
brenda
Kang, J.M.; Ju, H.L.; Sohn, W.M.; Na, B.K.
Defining the regulatory and inhibitory elements within the prodomain of CsCF-6, a cathepsin F cysteine protease of Clonorchis sinensis
Mol. Biochem. Parasitol.
190
92-96
2013
Clonorchis sinensis
brenda
Park, S.Y.; Jeong, M.S.; Park, S.A.; Ha, S.C.; Na, B.K.; Jang, S.B.
Structural basis of the cystein protease inhibitor Clonorchis sinensis Stefin-1
Biochem. Biophys. Res. Commun.
498
9-17
2018
Clonorchis sinensis
brenda
Guo, H.; Li, Y.; Zhang, M.; Li, R.; Li, W.; Lou, J.; Bao, Z.; Wang, Y.
Expression of cathepsin F in response to bacterial challenges in Yesso scallop Patinopecten yessoensis
Fish Shellfish Immunol.
80
141-147
2018
Mizuhopecten yessoensis (A0A210PXH4), Mizuhopecten yessoensis
brenda
Ahn, C.; Na, B.; Chung, D.; Kim, J.; Kim, J.; Kong, Y.
Expression characteristics and specific antibody reactivity of diverse cathepsin F members of Paragonimus westermani
Parasitol. Int.
64
37-42
2015
Paragonimus westermani (O46177), Paragonimus westermani (Q2QKD6), Paragonimus westermani (Q2QKD7), Paragonimus westermani (Q2QKD8), Paragonimus westermani (Q2QKD9), Paragonimus westermani (Q2QKE0), Paragonimus westermani (Q2QKE1), Paragonimus westermani (Q2QKE2), Paragonimus westermani (Q5IH77), Paragonimus westermani (Q5IH78), Paragonimus westermani (Q9U0G8), Paragonimus westermani
brenda
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