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Information on EC 3.4.24.B3 - matrix metalloproteinase-11 and Organism(s) Xenopus laevis and UniProt Accession Q11005
for references in articles please use BRENDA:EC3.4.24.B3preliminary BRENDA-supplied EC number
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3.4.24.B3 matrix metalloproteinase-11Specify your search results
Word Map
- 3.4.24.B3
- metalloproteinases
- metastasis
- mmp-2
- timps
- gelatinase
-
microperoxidase-11
-
metamorphosis
- tadpole
- matrilysin
-
menstrual
- medicine
- stromelysin-2
-
microperoxidase
- collagenase-3
- pharmacology
- diagnostics
The taxonomic range for the selected organisms is: Xenopus laevis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
mmp-11, mmp11, stromelysin-3, mp-11, stromelysin 3, matrix metalloproteinase 11, matrix metalloproteinase-11, mmp stromelysin-3, mmp-11 proteinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MMP11
ST3
additional information
-
the enzyme belongs to the matrix metalloproteinase superfamily of Zn2+-dependent proteases
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
145267-01-2
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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
Human alpha1-proteinase inhibitor + H2O
?
-
preferred cleavage site: (A)/(G/A)(A)(M)(F/A)(L) (P3-P3') inability of Xenopus alpha1-proteinase inhibitor to be cleaved
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-
?
laminin receptor precursor + H2O
?
-
laminin receptor precursor is a likely in vivo substrate of stromelysin-3. Its cleavage may alter cell-extracellular matrix interaction, thus playing a role in mediating the effects of stromelysin-3 on cell fate and behavior observed during development and pathogenesis. Human laminin receptor precursor is cleaved by stromelysin-3 at the same two sites as in Xenopus laminin receptor precursor, yielding two N-terminal fragments of sizes identical to the corresponding Xenopus laminin receptor precursor fragments due to amino acid insertion in the C-terminus part of Xenopus laminin receptor precursor
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-
?
additional information
?
-
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the enzyme regulates cell fate and tissue morphogenesis through direct or indirect remodeling of extracellular matrix
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-
?
additional information
?
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stromelysin-3 expression, in the absence of thyroid hormone, causes significant muscle cell death in the tail of premetamorphic transgenic tadpoles. On the other hand, only relatively low levels of epidermal cell death are induced by precocious thyroid hormone expression in the tail
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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
laminin receptor precursor + H2O
?
-
laminin receptor precursor is a likely in vivo substrate of stromelysin-3. Its cleavage may alter cell-extracellular matrix interaction, thus playing a role in mediating the effects of stromelysin-3 on cell fate and behavior observed during development and pathogenesis. Human laminin receptor precursor is cleaved by stromelysin-3 at the same two sites as in Xenopus laminin receptor precursor, yielding two N-terminal fragments of sizes identical to the corresponding Xenopus laminin receptor precursor fragments due to amino acid insertion in the C-terminus part of Xenopus laminin receptor precursor
-
-
?
additional information
?
-
-
the enzyme regulates cell fate and tissue morphogenesis through direct or indirect remodeling of extracellular matrix
-
-
?
additional information
?
-
-
stromelysin-3 expression, in the absence of thyroid hormone, causes significant muscle cell death in the tail of premetamorphic transgenic tadpoles. On the other hand, only relatively low levels of epidermal cell death are induced by precocious thyroid hormone expression in the tail
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-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thyroid hormone T3
ST3 transcription is highly upregulated by thyroid hormone T3, T3 induces strong activation of the promoter through the intronic thyroid hormone response element
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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ST3 expression during amphibian metamorphosis, strong spatiotemporal correlation of its expression with apoptosis in various organs, overview
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expression of wild-type stromelysin-3 leads to extracellular matrix degradation and larval epithelial cell death in the intestine. Stromelysin-3 plays a role in remodeling of extracellular matrix, as a mechanism of T3-induced apoptosis during intestinal metamorphosis
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expression of wild-type stromelysin-3 leads to extracellular matrix degradation and larval epithelial cell death in the intestine. Stromelysin-3 plays a role in remodeling of extracellular matrix, as a mechanism of T3-induced apoptosis during intestinal metamorphosis
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stromelysin-3 expression, in the absence of thyroid hormone, causes significant muscle cell death in the tail of premetamorphic transgenic tadpoles. On the other hand, only relatively low levels of epidermal cell death are induced by precocious thyroid hormone expression in the tail
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ST3 has little expression in premetamorphic tadpoles, but reaches very high levels by stage 60 when cell death is at high levels in the larval epithelium. It is absent by the end of metamorphosis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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role of MMP11 or stromelysin-3, during the thyroid hormone-dependent amphibian metamorphosis, a process that resembles the so-called postembryonic development in mammals, overview. The metamorphosis requires the removal of unwanted larval cells through programmed cell death, or apoptosis, and proliferation followed by differentiation of adult cell types. Stromelysin-3 controls apoptosis in different tissues via at least two distinct mechanisms, detailed 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). PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
transgenic overexpression in tadpoles of ST3 alone is able to induce larval epithelial apoptosis, accompanied by the activation of fibroblasts (i.e. with enriched rough endoplasmic reticulum) just beneath the epithelium and cell-cell contacts between epithelial cells and the fibroblasts. Transgenic overexpression of ST3 preferentially induces apoptosis in the muscles of the tadpole tail, but also in the epidermis, low levels in the connective tissue underlying epidermis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ST3 is thyroid hormone T3-inducible in Xenopus laevis. the mRNA is strongly upregulated by stage 58 in the tadpole intestine, prior to any detectable epithelial apoptosis
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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 (P24347), Xenopus laevis (Q11005)
Amano, T.; Kwak, O.; Fu, L.; Marshak, A.; Shi, Y.B.
The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain
Cell Res.
15
150-159
2005
Xenopus laevis
Amano, T.; Fu, L.; Sahu, S.; Markey, M.; Shi, Y.B.
Substrate specificity of Xenopus matrix metalloproteinase stromelysin-3
Int. J. Mol. Med.
14
233-239
2004
Xenopus laevis
Fu, L.; Ishizuya-Oka, A.; Buchholz, D.R.; Amano, T.; Matsuda, H.; Shi, Y.B.
A causative role of stromelysin-3 in extracellular matrix remodeling and epithelial apoptosis during intestinal metamorphosis in Xenopus laevis
J. Biol. Chem.
280
27856-27865
2005
Xenopus laevis
Fu, L.; Tomita, A.; Wang, H.; Buchholz, D.R.; Shi, Y.B.
Transcriptional regulation of the Xenopus laevis stromelysin-3 gene by thyroid hormone is mediated by a DNA element in the first intron
J. Biol. Chem.
281
16870-16878
2006
Xenopus laevis (Q71VB9), Xenopus laevis
Shi, Y.B.; Fu, L.; Hasebe, T.; Ishizuya-Oka, A.
Regulation of extracellular matrix remodeling and cell fate determination by matrix metalloproteinase stromelysin-3 during thyroid hormone-dependent post-embryonic development
Pharmacol. Ther.
116
391-400
2007
Xenopus laevis
Mathew, S.; Fu, L.; Fiorentino, M.; Matsuda, H.; Das, B.; Shi, Y.B.
Differential regulation of cell type specific apoptosis by stromelysin-3: A potential mechanism via the cleavage of the laminin receptor during tail resorption in Xenopus laevis
J. Biol. Chem.
284
18545-18556
2009
Xenopus laevis
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