MMP17

Matrix metallopeptidase 17 (membrane-inserted)

Identifiers

MMP17 ; MT4-MMP

External IDs

OMIM: 602285 MGI: 1346076 HomoloGene: 22669 IUPHAR: 1641 ChEMBL: 2937 GeneCards: MMP17 Gene

3.4.24.-

Gene ontology
Molecular function	• metalloendopeptidase activity • calcium ion binding • enzyme activator activity • zinc ion binding
Cellular component	• proteinaceous extracellular matrix • integral component of plasma membrane • anchored component of membrane
Biological process	• proteolysis • positive regulation of catalytic activity
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
131.83 – 131.85 Mb

Chr 5:
129.58 – 129.61 Mb

PubMed search

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.^[1]^[2]

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. However, this protein is unique among the MT-MMP's in that it is a GPI-anchored protein rather than a transmembrane protein. The protein activates MMP2 by cleavage.^[2]

In melanocytic cells MMP17 gene expression may be regulated by MITF.^[3]

References

↑ 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.
1 2 "Entrez Gene: MMP17 matrix metallopeptidase 17 (membrane-inserted)".
↑ 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.

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.
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.
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.
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.
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. 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.
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

Proteases: metalloendopeptidases (EC 3.4.24)

ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13

Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28

Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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MMP17

Function

References

Further reading

External links