MMP20

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]

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)[1] Band 11q22.2 Start 102,576,832 bp[1] End 102,625,332 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 A1 Start 7,628,232 bp[2] End 7,674,980 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 9313 30800 Ensembl ENSG00000137674 ENSMUSG00000018620 UniProt O60882 P57748 RefSeq (mRNA) NM_004771 NM_013903 RefSeq (protein) NP_004762 NP_038931 Location (UCSC) Chr 11: 102.58 – 102.63 Mb Chr 9: 7.63 – 7.67 Mb PubMed search [3] [4]
Wikidata
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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]