MMP20

MMP20
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2JSD
Identifiers
Aliases	MMP20, AI2A2, MMP-20, matrix metallopeptidase 20
External IDs	OMIM: 604629; MGI: 1353466; HomoloGene: 21001; GeneCards: MMP20; OMA:MMP20 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	102,625,332 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	7,674,980 bp
RNA expression pattern
	Top expressed in
	left testis; ; right testis; ; sperm; ; gonad; ; sural nerve; ; gallbladder; ; duodenum; ; lymph node; ; endometrium; ; salivary gland;
	Top expressed in
	molar; ; Paneth cell; ; mandibular molars; ; tooth germ; ; Enamel organ; ; jejunum; ; ileum;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	zinc ion binding; peptidase activity; metalloendopeptidase activity; protein binding; hydrolase activity; metallopeptidase activity; metal ion binding; serine-type endopeptidase activity;
Cellular component	extracellular matrix; extracellular region; extracellular space;
Biological process	collagen catabolic process; protein catabolic process; regulation of enamel mineralization; proteolysis; amelogenesis; extracellular matrix disassembly; extracellular matrix organization;
	Sources:Amigo / QuickGO
Orthologs
	9313
	30800
	ENSG00000137674
	ENSMUSG00000018620
	O60882
	P57748
	NM_004771
	NM_013903
	NP_004762
	NP_038931
	Wikidata
View/Edit Human	View/Edit Mouse

Matrix metalloproteinase-20 (MMP-20) also known as enamel metalloproteinase or enamelysin is an enzyme that in humans is encoded by the MMP20 gene.^[5]^[6]

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.

MMP-20, also known as enamelysin, appears to be the only MMP that is tooth-specific and it is expressed by cells of different developmental origin (i.e. epithelial ameloblasts and mesenchymal odontoblasts).

Clinical significance

The human MMP-20 gene contains 10 exons and is part of a cluster of matrix metalloproteinase genes that localize to human chromosome 11q22.3.^[6] A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with amelogenesis imperfecta. Enamel in the absence of MMP-20 is hypoplastic (thin), contains less mineral (only one-third as much total mineral as wild type), and contains more protein and water. In general, MMP-20 functions in enamel are to cleave enamel matrix proteins at specific cleavage sites.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000137674 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000018620 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Llano E, Pendas AM, Knauper V, Sorsa T, Salo T, Salido E, Murphy G, Simmer JP, Bartlett JD, Lopez-Otin C (Jan 1998). "Identification and structural and functional characterization of human enamelysin (MMP-20)". Biochemistry. 36 (49): 15101–15108. doi:10.1021/bi972120y. PMID 9398237.
^ ^a ^b "Entrez Gene: MMP20 matrix metallopeptidase 20 (enamelysin)".
^ Moradian-Oldak J (2012). "Protein-mediated enamel mineralization". Front. Biosci. 17 (7): 1996–2023. doi:10.2741/4034. PMC 3442115. PMID 22652761.

External links

The MEROPS online database for peptidases and their inhibitors: M10.019
Overview of all the structural information available in the PDB for UniProt: O60882 (Human Matrix metalloproteinase-20) at the PDBe-KB.