MMP14

Matrix metalloproteinase-14 is an enzyme that in humans is encoded by the MMP14 gene.[4]

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
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q11.2 Start 22,836,560 bp[1] End 22,849,027 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • zinc ion binding • metal ion binding • integrin binding • peptidase activity • GO:0001948 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 • cell membrane • integral component of plasma membrane • macropinosome • Golgi lumen • cytoplasmic vesicle • extracellular • cell 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	n/a
UniProt	P50281	P53690
RefSeq (mRNA)	NM_004995	NM_008608
RefSeq (protein)	NP_004986	NP_032634
Location (UCSC)	Chr 14: 22.84 – 22.85 Mb	n/a
PubMed search	[2]	[3]
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. Deficits in MMP14 leads to premature aging, short lifespan, and cell senescence in mice,[5] 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."[6]

Interactions

MMP14 has been shown to interact with TIMP2.[7]

See also

• Matrix metalloproteinase
• ARK5

References

1. GRCh38: Ensembl release 89: ENSG00000157227 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. 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. doi:10.1038/370061a0. PMID 8015608.
5. Gutiérrez‐Fernández, Ana; Soria‐Valles, Clara; Osorio, Fernando G.; Gutiérrez‐Abril, Jesús; Garabaya, Cecilia; Aguirre, Alina; Fueyo, Antonio; Fernández‐García, María Soledad; Puente, Xose S. (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.
6. "Entrez Gene: MMP14 matrix metallopeptidase 14 (membrane-inserted)".
7. 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