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Information on EC 3.4.24.23 - matrilysin and Organism(s) Rattus norvegicus and UniProt Accession P50280
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3.4.24.23 matrilysinSpecify your search results
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- 3.4.24.23
- metalloproteinases
- mmp-2
- metastasis
- timp-1
- colorectal
- fibrosis
- collagen
- endothelial
- node
- gelatinase
- e-cadherin
-
clinicopathological
-
zymography
-
interstitial
- gastric
- epithelium
- tumour
- adenocarcinoma
- pulmonary
-
basement
- prostate
-
invasiveness
- tumorigenesis
- beta-catenin
- gelatin
- carcinogenesis
-
resect
- mt1-mmp
- cyclin
- c-myc
- adenoma
- plasminogen
-
transwell
- osteopontin
- metalloelastase
- stromelysin-1
- laminin-5
-
hemopexin-like
- pharmacology
- upa
- drug development
- alpha-defensins
- collagenase-3
- analysis
- medicine
- diagnostics
-
gelatinolytic
-
matrix-degrading
-
paneth
-
membrane-type
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Cleavage of Ala14-/-Leu and Tyr16-/-Leu in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha2(I) > alpha1(I)
Synonyms
mmp-7, matrilysin, matrix metalloproteinase-7, matrix metalloproteinase 7, matrin, pump-1, matrix metallopeptidase 7, metalloproteinase-7, matrilysin-1, mmp 7, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Matrin
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-
-
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Matrix metalloproteinase 7
Matrix metalloproteinase pump 1
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-
-
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Matrix metalloproteinase-7
MMP
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-
-
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MMP 7
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-
-
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Proteinase, metallo-, pump-1
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-
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Proteinase, PUMP-1
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-
-
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PUMP
-
-
-
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Pump-1 protease
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-
-
-
Putative (or punctuated) metalloproteinase-1
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-
-
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Putative metalloproteinase
-
-
-
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Uterine metalloendopeptidase
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-
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Uterine metalloproteinase
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-
-
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Matrix metalloproteinase 7
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-
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Matrix metalloproteinase-7
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
141256-52-2
-
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
Insulin B-chain + H2O
?
-
cleavage at 2 points: Ala14-Leu15 and Tyr16-Leu17
-
-
?
Gelatin + H2O
?
-
digests the alpha2(I) chain of gelatin in preference to the alpha1(I) chain
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-
?
Gelatin + H2O
?
-
cleaves the alpha2(I) chain of rat gelatin producing major cuts at Gly713-Ile714, Gly775-Leu776, Gly809-Ile810
-
-
?
additional information
?
-
the enzyme is involved in the pivotal wingless-type signaling pathway and in tolerance of MHC-incompatible allografts, overview
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-
?
additional information
?
-
-
rat and human enzyme do not activate rat collagenase 3
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-
?
additional information
?
-
-
maximum activation of human interstitial collagenase 1 (pro-matrix metalloproteinase 1) when added in presence of 4-aminophenylmercuric acetate by cleaving the Gln80-Phe81 bond
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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
?
-
the enzyme is involved in the pivotal wingless-type signaling pathway and in tolerance of MHC-incompatible allografts, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
enzyme expression is upregulated in kidneys that are MHC-incompatible allografts but are tolerated through induction by the administration of anti-donor class II antibodies, as part of the pivotal non-canonical wingless-type signaling pathway, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8.8
-
5.5: about 30% of activity maximum, 8.8: about 40% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression analysis in kidneys after transplantation, overview
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
MMP-7 controls the transcription of the disintegrin and metalloproteinase-12, ADAM-12, the major metalloproteinase implicated in cardiac hypertrophy. Matrix metalloproteinase-7 and ADAM-12 form a novel signaling axis in a variety of cardiovascular processes, including hypertension and hypertrophy, overview. Induction of acute hypertension by vasoconstrictors, i.e. catecholamines, angiotensin II, and the nitric oxide synthase inhibitor NG-nitro-L-arginine methyl ester, require the posttranscriptional activation of vascular MMP-7. Sustained agonist stimulation regulates the development and progression of hypertension and hypertrophy processes through posttranscriptional, short-term and transcriptional , ong-term mechanisms involving metalloproteinases such as MMP-7 and ADAM-12
additional information
-
MMP-7 expression regulation, high expression of ADAM-12 observed under sustained agonist stimulation acts in a negative feedback loop to inhibit MMP-7 transcription, overview
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). MMP7_RAT
267
0
29885
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
MMP-7 gene knockout or knockdown of MMP-7 by RNA interference, results in attenuation of hypertension and stops development of cardiac hypertrophy in spontaneously hypertensive rats, and in decreased levels of myocardial ADAM-12 mRNA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
MMP-7 promotes tolerance of incompatibel allografts and may help in development of strategies to improve long-term graft outcome in transplantation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Quantin, B.; Murphy, G.; Breathnach, R.
Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members
Biochemistry
28
5327-5334
1989
Homo sapiens, Rattus norvegicus
Woessner, J.F.; Taplin, C.J.
Purification and properties of a small latent matrix metalloproteinase of the rat uterus
J. Biol. Chem.
263
16918-16925
1988
Rattus norvegicus
Abramson, S.R.; Conner, G.E.; Nagase, H.; Neuhaus, I.; Woessner, J.F.
Characterization of rat uterine matrilysin and its cDNA. Relationship to human pump-1 and activation of procollagenases
J. Biol. Chem.
270
16016-16022
1995
Rattus norvegicus
Welch, A.R.; Holman, C.M.; Browner, M.F.; Gehring, M.R.; Kan, C.C.; van Wart, H.E.
Purification of human matrilysin produced in Escherichia coli and characterization using a new optimized fluorogenic peptide substrate
Arch. Biochem. Biophys.
324
59-64
1995
Homo sapiens, Rattus norvegicus
Woessner, J.F.
Matrilysin
Methods Enzymol.
248
485-495
1995
Homo sapiens, Rattus norvegicus
Yu, W.H.; Woessner, J.F.Jr.
Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)
J. Biol. Chem.
275
4183-4191
2000
Homo sapiens, Rattus norvegicus
Jovanovic, V.; Dugast, A.S.; Heslan, J.M.; Ashton-Chess, J.; Giral, M.; Degauque, N.; Moreau, A.; Pallier, A.; Chiffoleau, E.; Lair, D.; Usal, C.; Smit, H.; Vanhove, B.; Soulillou, J.P.; Brouard, S.
Implication of matrix metalloproteinase 7 and the noncanonical wingless-type signaling pathway in a model of kidney allograft tolerance induced by the administration of anti-donor class II antibodies
J. Immunol.
180
1317-1325
2008
Rattus norvegicus (P50280)
Wang, X.; Chow, F.L.; Oka, T.; Hao, L.; Lopez-Campistrous, A.; Kelly, S.; Cooper, S.; Odenbach, J.; Finegan, B.A.; Schulz, R.; Kassiri, Z.; Lopaschuk, G.D.; Fernandez-Patron, C.
Matrix metalloproteinase-7 and ADAM-12 (a disintegrin and metalloproteinase-12) define a signaling axis in agonist-induced hypertension and cardiac hypertrophy
Circulation
119
2480-2489
2009
Mus musculus, Rattus norvegicus
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