MMP16

Matrix metallopeptidase 16 (membrane-inserted)
File:PBB Protein MMP16 image.jpg PDB rendering based on 1rm8.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1rm8​
Identifiers
Symbols	MMP16 ; MMP-X2; MT-MMP2; MT-MMP3; MT3-MMP
External IDs	Template:OMIM5 Template:MGI HomoloGene: 55939
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE MMP16 208166 at tn.png
File:PBB GE MMP16 208167 s at tn.png
File:PBB GE MMP16 207012 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Matrix metallopeptidase 16 (membrane-inserted), also known as MMP16, is a human gene.

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. This gene produces at least two transcripts, one which encodes a membrane-bound form and another a soluble form of the protein. Both forms of the protein activate MMP2 by cleavage. This gene was once referred to as MT-MMP2, but was renamed as MT-MMP3 or MMP16.

Further reading

• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. PMID 10419448.
• Takino T, Sato H, Shinagawa A, Seiki M (1995). "Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family". J. Biol. Chem. 270 (39): 23013–20. PMID 7559440.CS1 maint: Multiple names: authors list (link)
• Andersson B, Wentland MA, Ricafrente JY; et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mattei MG, Roeckel N, Olsen BR, Apte SS (1997). "Genes of the membrane-type matrix metalloproteinase (MT-MMP) gene family, MMP14, MMP15, and MMP16, localize to human chromosomes 14, 16, and 8, respectively". Genomics. 40 (1): 168–9. doi:10.1006/geno.1996.4559. PMID 9070935.CS1 maint: Multiple names: authors list (link)
• Shofuda K, Yasumitsu H, Nishihashi A; et al. (1997). "Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain". J. Biol. Chem. 272 (15): 9749–54. PMID 9092507.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yu W, Andersson B, Worley KC; et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. PMID 9110174.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Sato H, Tanaka M, Takino T; et al. (1997). "Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization". Genomics. 39 (3): 412–3. doi:10.1006/geno.1996.4496. PMID 9119382.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Matsumoto S, Katoh M, Saito S; et al. (1998). "Identification of soluble type of membrane-type matrix metalloproteinase-3 formed by alternatively spliced mRNA". Biochim. Biophys. Acta. 1354 (2): 159–70. PMID 9396633.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 10949161.CS1 maint: Multiple names: authors list (link)
• Iida J, Pei D, Kang T; et al. (2001). "Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen". J. Biol. Chem. 276 (22): 18786–94. doi:10.1074/jbc.M010053200. PMID 11278606.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Jung M, Römer A, Keyszer G; et al. (2003). "mRNA expression of the five membrane-type matrix metalloproteinases MT1-MT5 in human prostatic cell lines and their down-regulation in human malignant prostatic tissue". Prostate. 55 (2): 89–98. doi:10.1002/pros.10194. PMID 12661033.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Takino T, Koshikawa N, Miyamori H; et al. (2003). "Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases". Oncogene. 22 (30): 4617–26. doi:10.1038/sj.onc.1206542. PMID 12879005.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rozanov DV, Hahn-Dantona E, Strickland DK, Strongin AY (2004). "The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells". J. Biol. Chem. 279 (6): 4260–8. doi:10.1074/jbc.M311569200. PMID 14645246.CS1 maint: Multiple names: authors list (link)
• Lang R, Braun M, Sounni NE; et al. (2004). "Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features". J. Mol. Biol. 336 (1): 213–25. PMID 14741217.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Shofuda T, Shofuda K, Ferri N; et al. (2004). "Cleavage of focal adhesion kinase in vascular smooth muscle cells overexpressing membrane-type matrix metalloproteinases". Arterioscler. Thromb. Vasc. Biol. 24 (5): 839–44. doi:10.1161/01.ATV.0000126680.78500.4c. PMID 15044209.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wang SC, Lien HC, Xia W; et al. (2004). "Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2". Cancer Cell. 6 (3): 251–61. doi:10.1016/j.ccr.2004.07.012. PMID 15380516.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kimura K, Wakamatsu A, Suzuki Y; et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)