Misplaced Pages

MMP17
Identifiers
Aliases	MMP17, MT4-MMP, MMP-17, MT4MMP, MTMMP4, matrix metallopeptidase 17
External IDs	OMIM: 602285; MGI: 1346076; HomoloGene: 22669; GeneCards: MMP17; OMA:MMP17 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) Band 12q24.33 Start 131,828,393 bp End 131,851,783 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5 G1.3|5 68.18 cM Start 129,661,233 bp End 129,688,163 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right frontal lobe anterior cingulate cortex nucleus accumbens prefrontal cortex caudate nucleus putamen Brodmann area 9 Amygdala granulocyte tibial nerve Top expressed in primary motor cortex dentate gyrus olfactory tubercle prefrontal cortex subiculum ascending aorta dentate gyrus of hippocampal formation granule cell CA3 field anterior amygdaloid area hippocampus proper More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metallopeptidase activity enzyme activator activity metal ion binding peptidase activity hydrolase activity zinc ion binding metalloendopeptidase activity metalloaminopeptidase activity Cellular component integral component of plasma membrane membrane extracellular region extracellular matrix anchored component of membrane plasma membrane extracellular space Biological process drinking behavior positive regulation of catalytic activity kidney development proteolysis extracellular matrix organization collagen catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4326 23948 Ensembl ENSG00000198598 ENSMUSG00000029436 UniProt Q9ULZ9 Q8IWC3 Q9R0S3 RefSeq (mRNA) NM_016155 NM_011846 RefSeq (protein) NP_057239 NP_057239.4 NP_035976 Location (UCSC) Chr 12: 131.83 – 131.85 Mb Chr 5: 129.66 – 129.69 Mb PubMed search
Wikidata
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Matrix metalloproteinase-17 (MMP-17) also known as membrane-type matrix metalloproteinase 4 (MT-MMP 4) is an enzyme that in humans is encoded by the MMP17 gene.

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. The protein encoded by this gene is considered a member of the membrane-type MMP (MT-MMP) subfamily. MMP17 and MMP25 are to this day the only known GPI-anchored membrane-type MMPs, opposite to the more common transmembrane MMPs. The protein activates MMP2 by cleavage.

In melanocytic cells MMP17 gene expression may be regulated by MITF.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000198598 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000029436 – 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. Puente XS, Pendas AM, Llano E, Lopez-Otin C (Feb 1999). "Localization of the human membrane type 4-matrix metalloproteinase gene (MMP17) to chromosome 12q24". Genomics. 54 (3): 578–9. doi:10.1006/geno.1998.5564. PMID 9878265.
6. ^ "Entrez Gene: MMP17 matrix metallopeptidase 17 (membrane-inserted)".
7. Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971. S2CID 24698373.

Further reading

• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
• Puente XS, Pendás AM, Llano E, et al. (1996). "Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma". Cancer Res. 56 (5): 944–9. PMID 8640782.
• Kajita M, Kinoh H, Ito N, et al. (1999). "Human membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a novel major transcript: isolation of complementary DNA clones for human and mouse mt4-mmp transcripts". FEBS Lett. 457 (3): 353–6. doi:10.1016/S0014-5793(99)01065-0. PMID 10471807. S2CID 46523417.
• Kolkenbrock H, Essers L, Ulbrich N, Will H (1999). "Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase". Biol. Chem. 380 (9): 1103–8. doi:10.1515/BC.1999.137. PMID 10543448. S2CID 11192061.
• Wang Y, Johnson AR, Ye QZ, Dyer RD (2000). "Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain". J. Biol. Chem. 274 (46): 33043–9. doi:10.1074/jbc.274.46.33043. PMID 10551873.
• Itoh Y, Kajita M, Kinoh H, et al. (1999). "Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase". J. Biol. Chem. 274 (48): 34260–6. doi:10.1074/jbc.274.48.34260. PMID 10567400.
• Kinoh H, Hayashita H, Kajita M, et al. (2000). "Assignment of the genes for membrane-type-4 matrix metalloproteinase (Mmp17, MMP17) to mouse chromosome 5, human chromosome band 12q24.3 and membrane-type-5 matrix metalloproteinase (Mmp24, MMP24) to mouse chromosome 2 and human chromosome band 20q11.2→q12, respectively, by radiation hybrid and in situ hybridization". Cytogenet. Cell Genet. 87 (1–2): 97–8. doi:10.1159/000015402. PMID 10640822. S2CID 24060884.
• English WR, Puente XS, Freije JM, et al. (2000). "Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2". J. Biol. Chem. 275 (19): 14046–55. doi:10.1074/jbc.275.19.14046. PMID 10799478.
• 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. S2CID 1270176.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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. S2CID 21596144.
• Gauthier MC, Racine C, Ferland C, et al. (2004). "Expression of membrane type-4 matrix metalloproteinase (metalloproteinase-17) by human eosinophils". Int. J. Biochem. Cell Biol. 35 (12): 1667–73. doi:10.1016/S1357-2725(03)00136-5. PMID 12962706.
• 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.
• Gao G, Plaas A, Thompson VP, et al. (2004). "ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1". J. Biol. Chem. 279 (11): 10042–51. doi:10.1074/jbc.M312100200. PMID 14701864.
• Atkinson SJ, Roghi C, Murphy G (2006). "MT1-MMP hemopexin domain exchange with MT4-MMP blocks enzyme maturation and trafficking to the plasma membrane in MCF7 cells". Biochem. J. 398 (1): 15–22. doi:10.1042/BJ20060243. PMC 1525013. PMID 16686598.

External links

• The MEROPS online database for peptidases and their inhibitors: M10.017

• Biology

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