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
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 7,628,231 bp[2] End 7,674,979 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • zinc ion binding • peptidase activity • metalloendopeptidase activity • GO:0001948 protein binding • hydrolase activity • metallopeptidase activity • metal ion binding • serine-type endopeptidase activity Cellular component • extracellular matrix • extracellular region • extracellular 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
View/Edit Human View/Edit Mouse

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

1. GRCh38: Ensembl release 89: ENSG00000137674 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000018620 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: MMP20 matrix metallopeptidase 20 (enamelysin)".
7. Moradian-Oldak J (2012). "Protein-mediated enamel mineralization". Front. Biosci. 17: 1996–2023. doi:10.2741/4034. PMC 3442115. PMID 22652761.

Further reading

• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–21494. doi:10.1074/jbc.274.31.21491. PMID 10419448.
• Bartlett JD, Simmer JP (2000). "Proteinases in developing dental enamel". Crit. Rev. Oral Biol. Med. 10 (4): 425–441. doi:10.1177/10454411990100040101. PMID 10634581.
• Pendás AM, Santamaría I, Alvarez MV, et al. (1997). "Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3". Genomics. 37 (2): 266–269. doi:10.1006/geno.1996.0557. PMID 8921407.
• Stracke JO, Fosang AJ, Last K, et al. (2000). "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)". FEBS Lett. 478 (1–2): 52–56. doi:10.1016/S0014-5793(00)01819-6. PMID 10922468.
• Terp GE, Christensen IT, Jørgensen FS (2000). "Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes". J. Biomol. Struct. Dyn. 17 (6): 933–46. doi:10.1080/07391102.2000.10506582. PMID 10949161.
• Väänänen A, Srinivas R, Parikka M, et al. (2001). "Expression and regulation of MMP-20 in human tongue carcinoma cells". J. Dent. Res. 80 (10): 1884–1889. doi:10.1177/00220345010800100501. PMID 11706946.
• Väänänen A, Tjäderhane L, Eklund L, et al. (2005). "Expression of collagen XVIII and MMP-20 in developing teeth and odontogenic tumors". Matrix Biol. 23 (3): 153–161. doi:10.1016/j.matbio.2004.04.003. PMID 15296943.
• Kim JW, Simmer JP, Hart TC, et al. (2006). "MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta". J. Med. Genet. 42 (3): 271–275. doi:10.1136/jmg.2004.024505. PMC 1736010. PMID 15744043.

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.