Activates progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin.
Subcellular Location:
Processed matrix metalloproteinase-24
Secreted
extracellular space
extracellular matrix
Also shed from cell surface as soluble proteinase, by a proteolytic cleavage.
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Precision
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Recovery
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Linearity
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References
1.
"Identification of a new membrane-type matrix metalloproteinase, MT5-MMP, that is expressed predominantly in cerebellum." Seiki M.
Submitted (1998-12) to the EMBL/GenBank/DDBJ databases
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];MUTAGENESIS OF GLU-256;ACTIVE SITE
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: SUBCELLULAR LOCATION;PROTEOLYTIC PROCESSING;MUTAGENESIS OF GLU-256 AND 549-ARG--ARG-555
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Cited for: FUNCTION;TISSUE SPECIFICITY;DEVELOPMENTAL STAGE
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Cited for: SUBCELLULAR LOCATION;INTERACTION WITH APBA3;MUTAGENESIS OF 616-GLU--VAL-618
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: FUNCTION;TISSUE SPECIFICITY;DISRUPTION PHENOTYPE
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: FUNCTION;TISSUE SPECIFICITY;DISRUPTION PHENOTYPE