MMP14

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MMP14
Protein MMP14 PDB 1bqq.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases MMP14, MMP-14, MMP-X1, MT-MMP, MT-MMP 1, MT1-MMP, MT1MMP, MTMMP1, WNCHRS, matrix metallopeptidase 14
External IDs MGI: 101900 HomoloGene: 21040 GeneCards: MMP14
Gene location (Human)
Chromosome 14 (human)
Chr. Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for MMP14
Genomic location for MMP14
Band 14q11.2 Start 22,836,557 bp[1]
End 22,849,027 bp[1]
RNA expression pattern
PBB GE MMP14 160020 at fs.png

PBB GE MMP14 202828 s at fs.png

PBB GE MMP14 202827 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004995

NM_008608

RefSeq (protein)

NP_004986

NP_032634

Location (UCSC) Chr 14: 22.84 – 22.85 Mb Chr 14: 54.43 – 54.45 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

Function[edit]

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[edit]

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

See also[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000157227 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000000957 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  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. doi:10.1038/370061a0. PMID 8015608. 
  6. ^ 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 4547893Freely accessible. 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[edit]

External links[edit]

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