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Information on EC 3.4.24.14 - procollagen N-endopeptidase and Organism(s) Bos taurus and UniProt Accession P79331
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3.4.24.14 procollagen N-endopeptidaseSpecify your search results
Word Map
- 3.4.24.14
- procollagens
- thrombospondin
-
disintegrin
- ehlers-danlos
-
dermatosparaxis
- n-propeptide
-
c-proteinase
- imperfecta
-
aminopropeptide
-
pro-alpha
-
disintegrin-like
-
adamts-3
-
dermatosparactic
-
col5a1
-
hennekam
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
Cleaves the N-propeptide of collagen chain alpha1(I) at Pro-/-Gln and of alpha1(II) and alpha2(I) at Ala-/-Gln
Synonyms
adamts2, adamts-2, adamts3, adamts14, procollagen n-proteinase, adamts 3, procollagen i n-proteinase, aminoprocollagen peptidase, adam-ts2, procollagen n-protease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADAM-TS2
-
-
-
-
aminoprocollagen peptidase
-
-
-
-
aminoterminal procollagen peptidase
-
-
-
-
PC I-NP
-
-
-
-
pNPI
-
-
-
-
procollagen aminopeptidase
-
-
-
-
procollagen aminoterminal protease
-
-
-
-
Procollagen I N-proteinase
Procollagen I/II amino-propeptide processing enzyme
-
-
-
-
Procollagen N-endopeptidase
-
-
-
-
procollagen N-protease
procollagen N-proteinase
procollagen N-terminal peptidase
-
-
-
-
procollagen N-terminal proteinase
-
-
-
-
Procollagen peptidase
type I/II procollagen N-proteinase
-
-
-
-
Procollagen I N-proteinase
-
-
-
-
procollagen N-protease
-
-
-
-
procollagen N-proteinase
-
-
-
-
Procollagen peptidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
68651-94-5
-
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
procollagen I + H2O
pCCollagen I + oligopeptide
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
partially processed procollagen containing only the C-propeptides
?
pNcollagen, carboxymethylated + H2O
?
-
pN collagen is collagen containing the N-terminal pro- peptide only
-
-
?
procollagen I + H2O
?
-
-
-
-
?
procollagen II + H2O
?
-
-
-
-
?
procollagen III + H2O
pCCollagen III + oligopeptide
-
removes the N-terminal propeptide from the native procollagen III, ADAMTS2 purified from skin is unable to process type III procollagen despite its activity on type I procollagen
-
-
?
procollagen V + H2O
pCCollagen V + oligopeptide
-
processes the aminopropetide at the end of the variable domain, cleavage sequence is different from previously described sites for ADAMTS-2
-
-
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
processing of either type I/II or type III procollagen
-
-
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
removal of the N-terminal propeptide, cleavage of the substrate in native conformation but not after heat denaturation
-
-
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
removal of the N-terminal propeptide, cleavage of the substrate in native conformation but not after heat denaturation
-
-
?
additional information
?
-
sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The bovine enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), and at 178NFAA-/-QMAG185 in chain alpha1(II), as well as at 76NFAA-/-QFDA83 in chains alpha2(I), respectively
-
-
?
additional information
?
-
sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The bovine enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), and at 178NFAA-/-QMAG185 in chain alpha1(II), as well as at 76NFAA-/-QFDA83 in chains alpha2(I), respectively
-
-
?
additional information
?
-
sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The bovine enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), and at 178NFAA-/-QMAG185 in chain alpha1(II), as well as at 76NFAA-/-QFDA83 in chains alpha2(I), respectively
-
-
?
additional information
?
-
ADAMTS2 displays some affinity for type XIV collagen
-
-
?
additional information
?
-
-
no cleavage of native procollagen III or collagen XIV, recombinant ADAMTS2 produced in 293 cells can process the N-propeptide of procollagen III in vitro
-
-
?
additional information
?
-
ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site
-
-
?
additional information
?
-
ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site
-
-
?
additional information
?
-
ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site
-
-
?
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
procollagen I + H2O
?
-
-
-
-
?
procollagen II + H2O
?
-
-
-
-
?
additional information
?
-
sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The bovine enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), and at 178NFAA-/-QMAG185 in chain alpha1(II), as well as at 76NFAA-/-QFDA83 in chains alpha2(I), respectively
-
-
?
additional information
?
-
sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The bovine enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), and at 178NFAA-/-QMAG185 in chain alpha1(II), as well as at 76NFAA-/-QFDA83 in chains alpha2(I), respectively
-
-
?
additional information
?
-
sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The bovine enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), and at 178NFAA-/-QMAG185 in chain alpha1(II), as well as at 76NFAA-/-QFDA83 in chains alpha2(I), respectively
-
-
?
additional information
?
-
ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site
-
-
?
additional information
?
-
ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site
-
-
?
additional information
?
-
ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Zn2+
Ca2+
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by serine protease inhibitors, lysine or serum
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity
-
additional information
proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity
-
additional information
proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
propeptide of collagen alpha-1 chain, propeptide of collagen alpha-2 chain
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme requires a neutral to slightly basic pH for activity
additional information
the enzyme requires a neutral to slightly basic pH for activity
additional information
the enzyme requires a neutral to slightly basic pH for activity
additional information
the enzyme requires a neutral to slightly basic pH for activity
additional information
the enzyme requires a neutral to slightly basic pH for activity
additional information
the enzyme requires a neutral to slightly basic pH for activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7 - 9.5
-
procollagen I as substrate, 45% of optimum activity at pH 6.7 and pH 9.5
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
high expression of ADAMTS2 is detected in all type I collagen-rich tissues from fetal calf such as skin, bones, tendons and aorta, which supports its importance for type I collagen maturation
additional information
ADAMTS14 is usually co-expressed with ADAMTS2, although at a lower level, suggesting potential functional redundancy
additional information
ADAMTS14 is usually co-expressed with ADAMTS2, although at a lower level, suggesting potential functional redundancy
additional information
ADAMTS14 is usually co-expressed with ADAMTS2, although at a lower level, suggesting potential functional redundancy
additional information
ADAMTS14 is usually co-expressed with ADAMTS2, although at a lower level, suggesting potential functional redundancy
additional information
ADAMTS14 is usually co-expressed with ADAMTS2, although at a lower level, suggesting potential functional redundancy
additional information
ADAMTS14 is usually co-expressed with ADAMTS2, although at a lower level, suggesting potential functional redundancy
additional information
ADAMTS3 is mainly expressed in cartilage, where it colocalizes with type II procollagen, and in the nervous system
additional information
ADAMTS3 is mainly expressed in cartilage, where it colocalizes with type II procollagen, and in the nervous system
additional information
ADAMTS3 is mainly expressed in cartilage, where it colocalizes with type II procollagen, and in the nervous system
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch
physiological function
malfunction
-
an anti-tumoral activity is also observed when using cells expressing recombinant deleted forms of ADAMTS-2, including catalytically inactive enzyme
physiological function
additional information
physiological function
enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity
physiological function
type I collagen is a heterotrimer composed of 2 alpha1 chains and one alpha2 chain (which are the products of different genes) forming a typical triple helical domain. Besides the removal of the signal peptide, the maturation of type I procollagen into mature alpha chains involves cleavages of the aminopropeptide and the carboxypropeptide by aminoprocollagen peptidases (mainly ADAMTS2) and carboxyprocollagen peptidases (BMP1 and tolloids), respectively. In vivo in physiological conditions, only the fully processed alpha alpha1 and alpha2 chains are present in significant amounts. The excision of the aminopropeptide by ADAMTS2 converts the pro-chains into pC-chains, and the pN-chains into mature alpha chains
physiological function
-
ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity
physiological function
ADAMTS14, which is coexpressed with ADAMTS2 in different connective tissues, might be responsible for this partial alternative aminoprocollagen endopeptidase activity
physiological function
ADAMTS3 promotes the release of a proteolytically cleaved active form of VEGF-C, a process that increases VEGF-R3 signaling
additional information
the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components
additional information
the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components
additional information
the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components
additional information
the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components
additional information
the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components
additional information
the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components
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). ATS2_BOVIN
1205
0
133888
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
177000
-
immunoprecipitation, full size enzyme after removal of the signal peptide
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
ADAMTS2 mutated at the furin-cleavage site separating the pro domain and the metalloprotease domain lacks enzymatic activity
additional information
-
removal of the PNP domain, which significantly increases enzyme activity, removal of the fourth and the second TSPI repeats, which represses the enzymatic activity, no activity when lacking the central domain or mutated at the catalytic site, mutation of the potential cleavage site by furin strongly represses, but not abolishes enzyme activity, removal of adjacent domains completely suppresses activity, use of chimeric enzyme shows significant level of activity only when the metalloprotease domain or the other central domains are present, replacement of the C-terminal domains by GON-1 or ADAMTS-14 results in reduced activity
additional information
-
three constructs coding for catalytically inactive ADAMTS-2 or for ADAMTS-2 lacking either the central or the C-terminal domains are created and used for stable transfection of HEK 293-EBNA cells. Results show that the catalytic activity of ADAMTS-2 is dispensable for antiangiogenic activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from cell-free extract or extracellular recombinant enzyme secreted from HEK-293 cells by concanavalin A affinity chromatography, elution with alpha-methyl-D-mannoside, followed by heparin affinity chromatography and dialysis
400-6000fold purified by ammonium sulfate precipitation, concanavalin A and heparin-Sepharose chromatography and affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloned in a pCDNA3 vector, expression in HT1080, W126, COS, Balb, MCF7, SaOS2 and 293EBNA cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
ADAMTS2 diplays procollagen III N-endopeptidase activity, proteolytic processing of ADAMTS2 may generate fragments displaying specifically either procollagen I/II or procollagen III N-endopeptidase acitvity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hojima, Y.; McKenzie, J.A.; Van der Rest, M.; Prockop, D.J.
Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptides
J. Biol. Chem.
264
11336-11345
1989
Bos taurus, Gallus gallus
Prockop, D.L.; Sieron, A.L.; Li, S.W.
Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling
Matrix Biol.
16
399-408
1998
Bos taurus, Gallus gallus
Prockop, D.J.; Tuderman, L.
Posttranslational enzymes in the biosynthesis of collagen: extracellular enzymes
Methods Enzymol.
82
305-319
1982
Bos taurus, Gallus gallus
Arnold, W.V.; Fertala, A.; Sieron, A.L.; Hattori, H.; Mechling, D.; Bchinger, H.P.; Prockop.D.L.
Recombinant procollagen II: Deletion of D period segments identifies sequences that are required for helix stabilization and generates a temperature-sensitive N-proteinase cleavage site
J. Biol. Chem.
273
31822-31828
1998
Bos taurus, Gallus gallus
Nusgens, B.; Lapiere, C.M.
A simplified procedure for measuring amino-procollagen peptidase type I
Anal. Biochem.
95
406-412
1979
Bos taurus, Gallus gallus
Kohn, L.D.; Isersky, C.; Zupnik, J.; Lenaers, A.; Lee, G.; Lapiere, C.M.
Calf tendon procollagen peptidase: its purification and endopeptidase mode of action
Proc. Natl. Acad. Sci. USA
71
40-44
1974
Bos taurus
Hojima, Y.; Morgelin, M.M.; Engel, J.; Boutillon, M.M.; Van der Rest, M.; McKenzie, J.; Chen, G.C.; Rafi, N.; Romanic, A.M.; Prockop, D.J.
Characterization of type I procollagen N-proteinase from fetal bovine tendon and skin. Purification of the 500-kilodalton form of the enzyme from bovine tendon
J. Biol. Chem.
269
11381-11390
1994
Bos taurus
Colige, A.; Beschin, A.; Damyn, B.; Goebels, Y.; Van Beeumen, J.; Nusgens, B.V.; Lapiere, C.M.
Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen
J. Biol. Chem.
270
16725-16730
1995
Bos taurus
-
Kadler, E.K.; Lightfoot, S.J.; Watson, R.B.
Procollagen N-peptidases: procollagen N-proteinases
Methods Enzymol.
248
756-771
1995
Bos taurus, Gallus gallus
Colige, A.; Li, S.W.; Sieron, A.L.; Nusgens, B.V.; Prockop, D.J.
cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components
Proc. Natl. Acad. Sci. USA
94
2374-2379
1997
Bos taurus (P79331), Bos taurus
Colige, A.
Procollagen III N-proteinase
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
458-460
2004
Bos taurus, Homo sapiens
-
Colige, A.
Procollagen N-endopeptidase, ADAMTS2
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
737-740
2004
Bos taurus, Gallus gallus, Homo sapiens
-
Colige, A.; Ruggiero, F.; Vandenberghe, I.; Dubail, J.; Kesteloot, F.; Van Beeumen, J.; Beschin, A.; Brys, L.; Lapiere, C.M.; Nusgens, B.
Domains and maturation processes that regulate the activity of ADAMTS-2, a metalloproteinase cleaving the aminopropeptide of fibrillar procollagens types I-III and V
J. Biol. Chem.
280
34397-34408
2005
Bos taurus
Dubail, J.; Kesteloot, F.; Deroanne, C.; Motte, P.; Lambert, V.; Rakic, J.M.; Lapiere, C.; Nusgens, B.; Colige, A.
ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity
Cell. Mol. Life Sci.
67
4213-4232
2010
Bos taurus
Bekhouche, M.; Colige, A.
The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology
Matrix Biol.
44-46C
46-53
2015
Bos taurus (E1BC50), Bos taurus (E1BFV4), Bos taurus (P79331), Canis lupus familiaris (E2R8G2), Gallus gallus, Homo sapiens (O15072), Homo sapiens (O95450), Homo sapiens (Q8WXS8), Mus musculus (Q8C9W3), Ovis aries (W5P0Z2), Rattus norvegicus (D3ZTE7), Sus scrofa (I3LAK9)
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Release 2023.1 (January 2023)
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