MMP7
Sign in to saveAlso known as MMP-7, MPSL1, PUMP-1, matrix metallopeptidase 7
Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene. The enzyme () has also been known as matrin, putative (or punctuated) metalloproteinase-1, matrix metalloproteinase pump 1, PUMP-1 proteinase, PUMP, metalloproteinase pump-1, putative metalloproteinase, MMP). Human MMP-7 has a molecular weight around 30 kDa.
In the Vinony graph
Within Vinony's link graph, MMP7 is referenced by 154 other articles, and connects out to PubMed, PubMed Central and peptidase.
It sits within the topics EC 3.4.24, Genes on human chromosome 11 and Matrix metalloproteinases.
Its subject is documented across 5 Wikipedia language editions.
Gene data
MMP7- Name
- matrix metallopeptidase 7
- Type
- protein-coding
- Position
- 102,520,508–102,530,853 (−)
- Aliases
- MMP-7, MPSL1, PUMP-1
- Ensembl
- ENSG00000137673
- RefSeq RNA
- NM_002423.5
- RefSeq protein
- NP_002414.1
This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). Proteins in this 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. The encoded preproprotein is proteolytically processed to generate the mature protease. This secreted protease breaks down proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal hemopexin 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 on chromosome 11. This gene exhibits elevated expression levels in multiple human cancers. [provided by RefSeq, Jan 2016].
Gene Ontology
Biological process
Molecular function
Pathways
via MyGene.info
Gene · Ensembl
matrix metallopeptidase 7
- Symbol
- MMP7
- Biotype
- Protein coding
- Organism
- Homo sapiens
- Location
- 11:102,520,508-102,530,853
- Strand
- Reverse (−)
- Assembly
- GRCh38
via Ensembl · EMBL-EBI
Wikidata facts
- Instance of
- gene
- Image
- Protein MMP7 PDB 1mmp.png
Show 7 more facts
- HomoloGene ID
- 37619
- found in taxon
- Homo sapiens
- exact match
- identifiers.org/ncbigene/4316
- genomic end
- 102530750
- genomic start
- 102391239
- chromosome
- human chromosome 11
- cytogenetic location
- 11q22.2
via Wikidata · CC0
~10 min read
Encyclopedic overview
12 sectionsContents
- Gene, regulation, and expression
- Structure
- Interactions
- Function
- Normal tissue development
- Tissue remodeling
- Clinical significance
- Role in Cancer
- Colon cancer and MMP7 expression
- References
- Further reading
- External links
Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is encoded by the MMP7 gene. The enzyme () has also been known as matrin, putative (or punctuated) metalloproteinase-1, matrix metalloproteinase pump 1, PUMP-1 proteinase, PUMP, metalloproteinase pump-1, putative metalloproteinase, MMP). Human MMP-7 has a molecular weight around 30 kDa.
Matrilysin was discovered by Sellers and Woessner in the uterus of the rat in 1988. The complementary DNA (cDNA) of human MMP7 was isolated in 1988 by Muller et al. MMP7 is a member of the matrix metalloproteinase (MMP) family consisting of structural-related zinc-dependent endopeptidases. The primary role of cleaved/activated MMP7 is to break down extracellular matrix by degrading macromolecules including casein, type I, II, IV, and V gelatins, fibronectin, and proteoglycan.
Excerpted from Wikipedia’s “MMP7” article, available under the CC BY-SA 4.0 licence.