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Information on EC 3.4.23.B1 - napsin and Organism(s) Homo sapiens and UniProt Accession O96009

for references in articles please use BRENDA:EC3.4.23.B1
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.B1 napsin
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This record set is specific for:
Homo sapiens
UNIPROT: O96009
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
proteolytic cleavage of polypeptides to large and stable peptides
belongs to the aspartic proteinases
Synonyms
napsin a, napsin, napsin-a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TA02 protein
-
napsin-A
-
-
TAO2
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic cleavage of polypeptides to large and stable peptides
show the reaction diagram
belongs to the aspartic proteinases
show the reaction diagram
active site S1/S3 region
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
CAS REGISTRY NUMBER
COMMENTARY hide
208934-04-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
K(dabsyl)-TSLLMAAPQ-Lucifer yellow + H2O
K(dabsyl)-TSLL + MAAPQ-Lucifer yellow
show the reaction diagram
-
-
-
?
K(dabsyl)-TSVLMAAPQ-Lucifer yellow + H2O
K(dabsyl)-TSVL + MAAPQ-Lucifer yellow
show the reaction diagram
polypeptide + H2O
peptides
show the reaction diagram
precursor form of surfactant protein B + H2O
fragments of precursor form of surfactant protein B
show the reaction diagram
pulmonary surfactant protein B + H2O
?
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
pulmonary surfactant protein B + H2O
?
show the reaction diagram
pulmonary surfactant protein C + H2O
?
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
K(dabsyl)-TSLLMAAPQ-Lucifer yellow + H2O
K(dabsyl)-TSLL + MAAPQ-Lucifer yellow
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
precursor form of surfactant protein B + H2O
fragments of precursor form of surfactant protein B
show the reaction diagram
napsin A is involved in the N- and C-terminal processing of proSP-B in type II pneumocytes
-
-
?
pulmonary surfactant protein B + H2O
?
show the reaction diagram
-
-
-
?
polypeptide + H2O
peptides
show the reaction diagram
-
-
-
?
pulmonary surfactant protein B + H2O
?
show the reaction diagram
pulmonary surfactant protein C + H2O
?
show the reaction diagram
-
napsin A is involved in the post-translational processing of pulmonary surfactant protein B and C in multivesivular bodies of type II pneumocytes
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17 kDa protein of Ascaris lumbricoides
weak inhibition
-
ABT-538
HIV proteinase inhibitor
Ac-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
-
ethoxycarbonyl-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
-
isobutyryl-HPFA-statine-LF-NH2
-
isobutyryl-HPFH-statine-LF-NH2
-
isobutyryl-HPFY-statine-LF-NH2
-
isovaleryl-HPF-2-naphthylalanine-statine-LF-NH2
-
isovaleryl-HPF-homophenylalanine-statine-LF-NH2
-
isovaleryl-HPFH-(4-amino-3-hydroxy-5-phenylpentanoic acid)-LF-NH2
-
isovaleryl-HPFH-(4-amino-3-hydroxy-6-methylheptanoic acid)-LF-NH2
-
isovaleryl-HPFH-statine-delta-N-acetylornithine-F-NH2
-
isovaleryl-HPFH-statine-IF-NH2
-
isovaleryl-HPFH-statine-IH-NH2
-
isovaleryl-HPFH-statine-LF-NH2
-
isovaleryl-pepstatin
strong inhibition
-
lactoyl-pepstatin
strong inhibition
pepstatin
-
pepstatin A
napsin A binds over a broad pH range to this inhibitor, highly selective binding of napsin A
t-butoxycarbonyl-HPFH-statine-LF-NH2
-
t-butoxycarbonyl-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
-
t-butoxycarbonyl-Phe-His-statine-Leu-Phe-NH2
-
TLIRIPLHRVQPGRRILNL
biotinylated, derived from residues 1P-19P of the 34 amino acid propart of pronapsin A
pepstatin
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017
K(dabsyl)-TSLLMAAPQ-Lucifer yellow
pH 4.7, 25°C
0.0062
K(dabsyl)-TSVLMAAPQ-Lucifer yellow
pH 4.7, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
17 kDa protein of Ascaris lumbricoides
pH 4.7, 37°C
-
0.00011
ABT-538
pH 4.7, 37°C
0.00001
Ac-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
pH 4.7, 37°C
0.00002
ethoxycarbonyl-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
pH 4.7, 37°C
0.00007
isobutyryl-HPFA-statine-LF-NH2
pH 4.7, 37°C
0.00016
isobutyryl-HPFH-statine-LF-NH2
pH 4.7, 37°C
0.001
isobutyryl-HPFY-statine-LF-NH2
pH 4.7, 37°C
0.000105
isovaleryl-HPF-2-naphthylalanine-statine-LF-NH2
pH 4.7, 37°C
0.000003
isovaleryl-HPF-homophenylalanine-statine-LF-NH2
pH 4.7, 37°C
0.000012
isovaleryl-HPFH-(4-amino-3-hydroxy-5-phenylpentanoic acid)-LF-NH2
pH 4.7, 37°C
0.000065
isovaleryl-HPFH-(4-amino-3-hydroxy-6-methylheptanoic acid)-LF-NH2
pH 4.7, 37°C
0.00014
isovaleryl-HPFH-statine-delta-N-acetylornithine-F-NH2
pH 4.7, 37°C
0.000055
isovaleryl-HPFH-statine-IF-NH2
pH 4.7, 37°C
0.00057
isovaleryl-HPFH-statine-IH-NH2
pH 4.7, 37°C
0.0002
isovaleryl-HPFH-statine-LF-NH2
pH 4.7, 37°C
0.00000015
isovaleryl-pepstatin
pH 4.7, 37°C
-
0.000016
lactoyl-pepstatin
pH 4.7, 37°C
0.000002
pepstatin
pH 4.7, 25°C
0.003
t-butoxycarbonyl-HPFH-statine-LF-NH2
pH 4.7, 37°C
0.000185
t-butoxycarbonyl-Phe-His-(4-amino-3-hydroxy-6-methylheptanoic acid)-Leu-Phe-NH2
pH 4.7, 37°C
0.000012
t-butoxycarbonyl-Phe-His-statine-Leu-Phe-NH2
pH 4.7, 37°C
0.0005
TLIRIPLHRVQPGRRILNL
pH 4.7, 37°C
0.000002
pepstatin
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5.5
recombinant enzyme, at room temperature
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
in pleural effusions
Manually annotated by BRENDA team
bronchoalveolar lavage fluid (BALF), expression in
Manually annotated by BRENDA team
napsin A expression in 82% of 65 samples
Manually annotated by BRENDA team
napsin A expression in 37% of 19 samples
Manually annotated by BRENDA team
of peripheral blood
Manually annotated by BRENDA team
napsin A expression in 60% of 45 samples
Manually annotated by BRENDA team
the distribution of histotypes for 279 ovarian tumours are analysed
Manually annotated by BRENDA team
napsin A expression in 92% of 101 samples
Manually annotated by BRENDA team
napsin A expression in 100% of 7 samples
Manually annotated by BRENDA team
-
weak detection of napsin A in cytoplasm of lung sarcomatoid carcinoma cells
Manually annotated by BRENDA team
-
enzymatically active napsin A can be detected in urine of healthy individuals or in patients with transplanted kidney whose kidney function appears half to fully normal. Low activity in samples from patients with diseased kidneys
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
foci of Arias-Stella reaction are napsin A positive, expression analysis
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
napsin A is an intracellular aspartic protease and biomarker of various malignancies like lung adenocarcinoma and ovarian clear cell carcinoma
additional information
pepstatin pull-down at high pH is a powerful tool for detection and analysis of napsin A. Method development for specific enrichment of napsin A from clinical or biological specimens, that facilitates detailed analysis of the protein, evaluation, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NAPSA_HUMAN
420
0
45387
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
x * 37000, deglycosylated protein, SDS-PAGE
38000
x * 38000, SDS-PAGE
39000
x * 39000, glycosylated protein, SDS-PAGE
39000
-
1 * 39000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 39000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
deglycosylation by PNGase F
proteolytic modification
model of successive maturation, overview
proteolytic modification
-
napsin A is expressed as preproenzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
10 h, 37°C, stable
658595
6
10 h, 37°C, stable
658595
5 - 6
-
half-life more than 10 h
668762
7
-
half-life is around 4 h
668762
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
recombinant from HEK-293 cells, to homogeneity, 1-step procedure with propeptide of napsin A as affinity ligand
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, expression in HEK-293 cells
enzyme expression analysis
expression in HEK-293 cells
recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21 (DE3), recombinant overexpression in HEK-293 cells
DNA sequence determination and analysis, expression in HEK-293 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
napsin-A is decreased in stage IIIA primary lesions, napsin-A shows reduced expression in both IIIA primary sites and IIIA lymph nodes
napsin-A is highly expressed in stage IA primary lesions
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
diagnostics
medicine
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ueno, T.; Linder, S.; Elmberger, G.
Aspartic proteinase napsin is a useful marker for diagnosis of primary lung adenocarcinoma
Br. J. Cancer
88
1229-1233
2003
Homo sapiens (O96009)
Manually annotated by BRENDA team
Schauer-Vukasinovic, V.; Bur, D.; Kitas, E.; Schlatter, D.; Rosse, G.; Lahm, H.W.; Giller, T.
Purification and characterization of active recombinant human napsin A
Eur. J. Biochem.
267
2573-2580
2000
Homo sapiens (O96009), Homo sapiens
Manually annotated by BRENDA team
Tatnell, P.J.; Powell, D.J.; Hill, J.; Smith, T.S.; Tew, D.G.; Kay, J.
Napsins: new human aspartic proteinases. Distinction between two closely related genes
FEBS Lett.
441
43-48
1998
Homo sapiens, Homo sapiens (O96009)
Manually annotated by BRENDA team
Chuman, Y.; Bergman, A.; Ueno, T.; Saito, S.; Sakaguchi, K.; Alaiya, A.A.; Franzen, B.; Bergman, T.; Arnott, D.; Auer, G.; Appella, E.; Jornvall, H.; Linder, S.
Napsin A, a member of the aspartic protease family, is abundantly expressed in normal lung and kidney tissue and is expressed in lung adenocarcinomas
FEBS Lett.
462
129-134
1999
Homo sapiens (O96009), Homo sapiens
Manually annotated by BRENDA team
Schauer-Vukasinovic, V.; Bur, D.; Kling, D.; Gruninger, F.; Giller, T.
Human napsin A: expression, immunochemical detection, and tissue localization
FEBS Lett.
462
135-139
1999
Homo sapiens (O96009), Homo sapiens
Manually annotated by BRENDA team
Brasch, F.; Ochs, M.; Kahne, T.; Guttentag, S.; Schauer-Vukasinovic, V.; Derrick, M.; Johnen, G.; Kapp, N.; Muller, K.M.; Richter, J.; Giller, T.; Hawgood, S.; Buhling, F.
Involvement of napsin A in the C- and N-terminal processing of surfactant protein B in type-II-pneumocytes of the human lung
J. Biol. Chem.
278
49006-49014
2003
Homo sapiens (O96009), Homo sapiens
Manually annotated by BRENDA team
Rosse, G.; Kueng, E.; Page, M.G.; Schauer-Vukasinovic, V.; Giller, T.; Lahm, H.W.; Hunziker, P.; Schlatter, D.
Rapid identification of substrates for novel proteases using a combinatorial peptide library
J. Comb. Chem.
2
461-466
2000
Homo sapiens (O96009)
Manually annotated by BRENDA team
Hirano, T.; Gong, Y.; Yoshida, K.; Kato, Y.; Yashima, K.; Maeda, M.; Nakagawa, A.; Fujioka, K.; Ohira, T.; Ikeda, N.; Ebihara, Y.; Auer, G.; Kato, H.
Usefulness of TA02 (napsin A) to distinguish primary lung adenocarcinoma from metastatic lung adenocarcinoma
Lung Cancer
41
155-162
2003
Homo sapiens (O96009)
Manually annotated by BRENDA team
Benson, D.A.; Boguski, M.S.; Lipman, D.J.; Ostell, J.; Ouellette, B.F.F.; Rapp, B.A.; Wheeler, D.L.
GenBank
Nucleic Acids Res.
27
12-17
1999
Homo sapiens (O96009)
Manually annotated by BRENDA team
Cronshaw, R.F.; Schauer-Vukasinovic, V.; Powell, D.J.; Giller, T.; Bur, D.; Kay, J.
Inhibition of human napsin A
Protein Pept. Lett.
10
35-42
2003
Homo sapiens (O96009), Homo sapiens
Manually annotated by BRENDA team
Giller, T.; Schauer-Vukasinovic, V.
Napsin A
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
1
52-53
2004
Homo sapiens
-
Manually annotated by BRENDA team
Ueno, T.; Linder, S.; Na, C.L.; Rice, W.R.; Johansson, J.; Weaver, T.E.
Processing of pulmonary surfactant protein B by napsin and cathepsin H
J. Biol. Chem.
279
16178-16184
2004
Homo sapiens
Manually annotated by BRENDA team
Suzuki, A.; Shijubo, N.; Yamada, G.; Ichimiya, S.; Satoh, M.; Abe, S.; Sato, N.
Napsin A is useful to distinguish primary lung adenocarcinoma from adenocarcinomas of other organs
Pathol. Res. Pract.
201
579-586
2005
Homo sapiens
Manually annotated by BRENDA team
Woischnik, M.; Bauer, A.; Aboutaam, R.; Pamir, A.; Stanzel, F.; de Blic, J.; Griese, M.
Cathepsin H and napsin A are active in the alveoli and increased in alveolar proteinosis
Eur. Respir. J.
31
1197-1204
2008
Homo sapiens (O96009), Homo sapiens
Manually annotated by BRENDA team
Dejmek, A.; Naucler, P.; Smedjeback, A.; Kato, H.; Maeda, M.; Yashima, K.; Maeda, J.; Hirano, T.
Napsin A (TA02) is a useful alternative to thyroid transcription factor-1 (TTF-1) for the identification of pulmonary adenocarcinoma cells in pleural effusions
Diagn. Cytopathol.
35
493-497
2007
Homo sapiens (O96009)
Manually annotated by BRENDA team
Ueno, T.; Elmberger, G.; Weaver, T.E.; Toi, M.; Linder, S.
The aspartic protease napsin A suppresses tumor growth independent of its catalytic activity
Lab. Invest.
88
256-263
2008
Mus musculus (O09043), Homo sapiens (O96009), Homo sapiens
Manually annotated by BRENDA team
Stoll, L.M.; Johnson, M.W.; Gabrielson, E.; Askin, F.; Clark, D.P.; Li, Q.K.
The utility of napsin-A in the identification of primary and metastatic lung adenocarcinoma among cytologically poorly differentiated carcinomas
Cancer Cytopathol.
118
441-449
2010
Homo sapiens
Manually annotated by BRENDA team
Takeshima, Y.; Amatya, V.J.; Kushitani, K.; Kaneko, M.; Inai, K.
Value of immunohistochemistry in the differential diagnosis of pleural sarcomatoid mesothelioma from lung sarcomatoid carcinoma
Histopathology
54
667-676
2009
Homo sapiens
Manually annotated by BRENDA team
Bishop, J.A.; Sharma, R.; Illei, P.B.
Napsin A and thyroid transcription factor-1 expression in carcinomas of the lung, breast, pancreas, colon, kidney, thyroid, and malignant mesothelioma
Hum. Pathol.
41
20-25
2010
Homo sapiens
Manually annotated by BRENDA team
Nishimura, T.; Nomura, M.; Tojo, H.; Hamasaki, H.; Fukuda, T.; Fujii, K.; Mikami, S.; Bando, Y.; Kato, H.
Proteomic analysis of laser-microdissected paraffin-embedded tissues: (2) MRM assay for stage-related proteins upon non-metastatic lung adenocarcinoma
J. Proteomics
73
1100-1110
2010
Homo sapiens (O96009), Homo sapiens
Manually annotated by BRENDA team
Kim, J.H.; Kim, Y.S.; Choi, Y.D.; Lee, J.S.; Park, C.S.
Utility of napsin A and thyroid transcription factor 1 in differentiating metastatic pulmonary from non-pulmonary adenocarcinoma in pleural effusion
Acta Cytol.
55
266-270
2011
Homo sapiens
Manually annotated by BRENDA team
Rossi, G.; Cadioli, A.; Mengoli, M.; Piccioli, S.; Cavazza, A.
Napsin A expression in pulmonary sclerosing haemangioma
Histopathology
60
361-363
2012
Homo sapiens
Manually annotated by BRENDA team
Mukhopadhyay, S.; Katzenstein, A.L.
Comparison of monoclonal napsin A, polyclonal napsin A, and TTF-1 for determining lung origin in metastatic adenocarcinomas
Am. J. Clin. Pathol.
138
703-711
2012
Homo sapiens (O96009)
Manually annotated by BRENDA team
Schmidt, L.A.; Myers, J.L.; McHugh, J.B.
Napsin A is differentially expressed in sclerosing hemangiomas of the lung
Arch. Pathol. Lab. Med.
136
1580-1584
2012
Homo sapiens (O96009), Homo sapiens
Manually annotated by BRENDA team
Iwamoto, M.; Nakatani, Y.; Fugo, K.; Kishimoto, T.; Kiyokawa, T.
Napsin A is frequently expressed in clear cell carcinoma of the ovary and endometrium
Hum. Pathol.
46
957-962
2015
Homo sapiens (O96009)
Manually annotated by BRENDA team
Maurer, A.; Kalbacher, H.
Pepstatin pull-down at high pH is a powerful tool for detection and analysis of napsin A
Biochem. Biophys. Res. Commun.
515
145-148
2019
Homo sapiens (O96009)
Manually annotated by BRENDA team
Iwamoto, M.; Nakatani, Y.; Fugo, K.; Kishimoto, T.; Kiyokawa, T.
Napsin A is frequently expressed in clear cell carcinoma of the ovary and endometrium
Hum. Pathol.
46
957-962
2015
Homo sapiens (O96009)
Manually annotated by BRENDA team
Yamashita, Y.; Nagasaka, T.; Naiki-Ito, A.; Sato, S.; Suzuki, S.; Toyokuni, S.; Ito, M.; Takahashi, S.
Napsin A is a specific marker for ovarian clear cell adenocarcinoma
Mod. Pathol.
28
111-117
2015
Homo sapiens (O96009), Homo sapiens
Manually annotated by BRENDA team
Fadare, O.; Zhao, C.; Khabele, D.; Parkash, V.; Quick, C.M.; Gwin, K.; Desouki, M.M.
Comparative analysis of Napsin A, alpha-methylacyl-coenzyme A racemase (AMACR, P504S), and hepatocyte nuclear factor 1 beta as diagnostic markers of ovarian clear cell carcinoma an immunohistochemical study of 279 ovarian tumours
Pathology
47
105-111
2015
Homo sapiens (O96009)
Manually annotated by BRENDA team