MMP14

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)
End	22,849,041 bp
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)
End	54,682,821 bp
RNA expression pattern
	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
	; ; ; ;
	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
	4323
	17387
	ENSG00000157227
	ENSMUSG00000000957
	P50281
	P53690
	NM_004995
	NM_008608
	NP_004986
	NP_032634
	Wikidata
View/Edit Human	View/Edit Mouse

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

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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000157227 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000000957 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ "Entrez Gene: MMP14 matrix metallopeptidase 14 (membrane-inserted)".
^ 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.

External links

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

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000157227 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid8015608-5] 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)".

[pmid9422789-8] 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.

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MMP14

Function

Interactions

See also

References

Further reading

External links