MMP14

Matrix metalloproteinase-14 is an enzyme that in humans is encoded by the MMP14 gene.^[5]

MMP14
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BQQ, 1BUV, 2MQS, 3C7X, 3MA2, 4P3C, 4P3D, 4QXU, 3X23
Identifiers
Aliases	MMP14, MMP-14, MMP-X1, MT-MMP, MT-MMP 1, MT1-MMP, MT1MMP, MTMMP1, WNCHRS, matrix metallopeptidase 14
External IDs	OMIM: 600754; MGI: 101900; HomoloGene: 21040; GeneCards: MMP14; OMA:MMP14 - orthologs
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q11.2 Start 22,836,560 bp[1] End 22,849,041 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14 C2|14 27.79 cM Start 54,669,069 bp[2] End 54,682,821 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium gastric mucosa gallbladder canal of the cervix body of uterus ectocervix smooth muscle tissue right coronary artery popliteal artery tibial arteries Top expressed in calvaria body of femur umbilical cord molar stroma of bone marrow external carotid artery uterus internal carotid artery endothelial cell of lymphatic vessel lip More reference expression data BioGPS More reference expression data
Gene ontology Molecular function zinc ion binding metal ion binding integrin binding peptidase activity protein binding metalloendopeptidase activity peptidase activator activity metallopeptidase activity hydrolase activity serine-type endopeptidase activity metalloaminopeptidase activity endopeptidase activity Cellular component cytoplasm integral component of membrane membrane focal adhesion extracellular matrix melanosome plasma membrane integral component of plasma membrane macropinosome Golgi lumen cytoplasmic vesicle extracellular space nucleus cytosol intermediate filament cytoskeleton Biological process positive regulation of myotube differentiation male gonad development response to hypoxia endodermal cell differentiation response to organic cyclic compound ossification lung development astrocyte cell migration positive regulation of cell migration positive regulation of B cell differentiation zymogen activation response to mechanical stimulus extracellular matrix disassembly endochondral ossification response to oxidative stress craniofacial suture morphogenesis proteolysis positive regulation of peptidase activity response to estrogen positive regulation of cell growth endothelial cell proliferation chondrocyte proliferation angiogenesis collagen catabolic process ovarian follicle development embryonic cranial skeleton morphogenesis response to hormone tissue remodeling bone development branching morphogenesis of an epithelial tube negative regulation of focal adhesion assembly cell migration negative regulation of Notch signaling pathway protein processing cell motility positive regulation of macrophage migration response to odorant positive regulation of protein processing head development regulation of protein localization to plasma membrane skeletal system development extracellular matrix organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4323 17387 Ensembl ENSG00000157227 ENSMUSG00000000957 UniProt P50281 P53690 RefSeq (mRNA) NM_004995 NM_008608 RefSeq (protein) NP_004986 NP_032634 Location (UCSC) Chr 14: 22.84 – 22.85 Mb Chr 14: 54.67 – 54.68 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. Deficits in MMP14 leads to premature aging, short lifespan, and cell senescence in mice,^[6] suggesting an important role of MMP14 in extracellular matrix remodeling during aging. Most MMP's are secreted as inactive pro-proteins which are activated when cleaved by extracellular proteinases.

However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are tethered to the cell surface rather than secreted.

"This protein activates MMP2 protein, and this activity may be involved in tumor invasion."^[7]

Interactions

MMP14 has been shown to interact with TIMP2.^[8]

See also

• Matrix metalloproteinase
• ARK5

References

1. GRCh38: Ensembl release 89: ENSG00000157227 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000000957 – 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. Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, Seiki M (Jul 1994). "A matrix metalloproteinase expressed on the surface of invasive tumour cells". Nature. 370 (6484): 61–5. Bibcode:1994Natur.370...61S. doi:10.1038/370061a0. PMID 8015608. S2CID 4275857.
6. Gutiérrez-Fernández A, Soria-Valles C, Osorio FG, Gutiérrez-Abril J, Garabaya C, Aguirre A, Fueyo A, Fernández-García MS, Puente XS (2015-07-14). "Loss of MT1-MMP causes cell senescence and nuclear defects which can be reversed by retinoic acid". The EMBO Journal. 34 (14): 1875–1888. doi:10.15252/embj.201490594. ISSN 0261-4189. PMC 4547893. PMID 25991604.
7. "Entrez Gene: MMP14 matrix metallopeptidase 14 (membrane-inserted)".
8. Zucker S, Drews M, Conner C, Foda HD, DeClerck YA, Langley KE, Bahou WF, Docherty AJ, Cao J (Jan 1998). "Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)". J. Biol. Chem. 273 (2): 1216–22. doi:10.1074/jbc.273.2.1216. PMID 9422789.

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.

External links

• The MEROPS online database for peptidases and their inhibitors: M10.014