3.4.24.B5: matrix metalloproteinase-15

This is an abbreviated version!
For detailed information about matrix metalloproteinase-15, go to the full flat file.

Reaction

proteolytic degradation of proteins =

Synonyms

M10.015, matrix metalloproteinase 15, membrane type 2 matrix metalloproteinase, membrane type 2-Mmp, membrane-type matrix metalloproteinase, membrane-type matrix metalloproteinase 2, membrane-type-1 matrix metalloproteinase, membrane-type-2 matrix metalloproteinase, membrane-type-3 matrix metalloproteinase, MMP-15, MMP15, MT MMP, MT-MMP 2, MT1 MMP, MT2 MMP, MT2-MMP, Mt2-mmp/Mmp15, MT2MMP, MT3 MMP, MTMMP2, SMCP-2

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.B5 matrix metalloproteinase-15

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5	Activating Compound
4	AA Sequence
4	Application
1	CAS Registry Number
7	Cloned(Commentary)
717	Disease/ Diagnostics
5	Expression
6	General Information
6	Inhibitors
9	Localization
3	Metals/Ions
4	Molecular Weight [Da]
8	Natural Substrates/ Products (Substrates)
16	Organism
2	pH Optimum
2	Protein Variants
1	Purification (Commentary)
1	Reaction
5	Reaction Type
16	Reference
57	Source Tissue
1	Specific Activity [micromol/min/mg]
16	Substrates and Products (Substrate)
1	Subunits
54	Synonyms
2	Temperature Optimum [°C]

General Information

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General Information on EC 3.4.24.B5 - matrix metalloproteinase-15

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

Oryzias latipes

H2MKS4

inhibition of follicle ovulation, by the inhibitors roscovitine or CDK9-inhibitor II, is accompanied by the suppression of Mmp15 expression in the follicle. In follicles treated with the inhibitors, the formation of the phosphorylated nuclear progestin receptor (Pgr) is inhibited. Roscovitine treatment causes a reduction in the binding of Pgr to the promoter region of gene mmp15

753226

metabolism

2 entries

physiological function

3 entries

metabolism

Mus musculus

O54732

branching morphogenesis is thought to depend on the mobilization of the membrane-anchored matrix metalloproteinases MMP14 (MT1-MMP) and MMP15 (MT2-MMP), which drive epithelial cell invasion by remodeling the extracellular matrix and triggering associated signaling cascades. Different roles played by MMP14 or MMP15 in the mammary gland epithelial compartment and in development of mammary gland, overview. Whereas MMP14 promotes white fat-associated adipogenesis in the developing mammary gland, MMP15 serves as an endogenous suppressor of beige/brown fat production

753384

metabolism

Homo sapiens

P51511

MMP14 and MMP15 are involved in trophoblast invasion

753776

physiological function

Homo sapiens

P51511

enzyme MMP15 mainly play roles in extracellular matrix disassembly

754240

physiological function

Mus musculus

O54732

metalloproteinase MMP15 (MT2-MMP) drives epithelial cell invasion by remodeling the extracellular matrix and triggering associated signaling cascades. It plays a role in mammary gland development. Transcriptome profiling reveals a key role for MMP14 and MMP15 in regulating mammary gland adipocyte differentiation. MMP15 differentially controls the formation of thermogenic brown fat. Neonatal mammary gland branching proceeds in the absence of MMP15, early mammary epithelial branching is Mmp15 independent

753384

physiological function

Oryzias latipes

H2MKS4

nuclear progestin receptor phosphorylation by Cdk9 is required for the expression of Mmp15, a protease indispensable for ovulation in Medaka. The enzyme MMP-15 is involved in follicle layer extracellular matrix hydrolysis

753226