MMP7

Matrix metallopeptidase 7 (matrilysin, uterine)
PDB rendering based on 1mmp.
Available structures PDB 1MMP, 1MMQ, 1MMR, 2DDY
Identifiers
Symbols	MMP7; MMP-7; MPSL1; PUMP-1
External IDs	OMIM: 178990 MGI: 103189 HomoloGene: 37619 GeneCards: MMP7 Gene
EC number	3.4.24.23
Gene Ontology Molecular function • metalloendopeptidase activity • peptidase activity • zinc ion binding • metal ion binding Cellular component • extracellular region • proteinaceous extracellular matrix • extracellular space Biological process • antibacterial peptide secretion • proteolysis • metabolic process • collagen catabolic process • regulation of cell proliferation • response to drug • defense response to Gram-negative bacterium • defense response to Gram-positive bacterium Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4316	17393
Ensembl	ENSG00000137673	ENSMUSG00000018623
UniProt	P09237	Q10738
RefSeq (mRNA)	NM_002423.3	NM_010810.4
RefSeq (protein)	NP_002414.1	NP_034940.2
Location (UCSC)	Chr 11: 102.39 – 102.4 Mb	Chr 9: 7.69 – 7.7 Mb
PubMed search	[1]	[2]

Matrilysin also known as matrix metalloproteinase-7 (MMP-7) is an enzyme that in humans is encoded by the MMP7 gene.^[1]

Function

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.^[2]

References

1. ^ Knox JD, Boreham DR, Walker JA, Morrison DP, Matrisian LM, Nagle RB, Bowden GT (Jan 1997). "Mapping of the metalloproteinase gene matrilysin (MMP7) to human chromosome 11q21-->q22". Cytogenet Cell Genet 72 (2–3): 179–82. doi:10.1159/000134181. PMID 8978768. 
2. ^ "Entrez Gene: MMP7 matrix metallopeptidase 7 (matrilysin, uterine)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4316. 

Further reading

• Massova I, Kotra LP, Fridman R, Mobashery S (1998). "Matrix metalloproteinases: structures, evolution, and diversification". FASEB J. 12 (12): 1075–95. doi:10.1142/S0217984998001256. PMID 9737711. 
• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448. 

External links

• The MEROPS online database for peptidases and their inhibitors: M10.008