MMP14

Protein-coding gene in the species Homo sapiens
MMP14
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1BQQ, 1BUV, 2MQS, 3C7X, 3MA2, 4P3C, 4P3D, 4QXU, 3X23

Identifiers
AliasesMMP14, MMP-14, MMP-X1, MT-MMP, MT-MMP 1, MT1-MMP, MT1MMP, MTMMP1, WNCHRS, matrix metallopeptidase 14
External IDsOMIM: 600754; MGI: 101900; HomoloGene: 21040; GeneCards: MMP14; OMA:MMP14 - orthologs
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for MMP14
Genomic location for MMP14
Band14q11.2Start22,836,560 bp[1]
End22,849,041 bp[1]
Gene location (Mouse)
Chromosome 14 (mouse)
Chr.Chromosome 14 (mouse)[2]
Chromosome 14 (mouse)
Genomic location for MMP14
Genomic location for MMP14
Band14 C2|14 27.79 cMStart54,669,069 bp[2]
End54,682,821 bp[2]
RNA expression pattern
Bgee
HumanMouse (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

  • belly 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
SpeciesHumanMouse
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 MbChr 14: 54.67 – 54.68 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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]

See also

References

  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:". 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
  • v
  • t
  • e
  • 1bqq: CRYSTAL STRUCTURE OF THE MT1-MMP--TIMP-2 COMPLEX
    1bqq: CRYSTAL STRUCTURE OF THE MT1-MMP--TIMP-2 COMPLEX
  • 1buv: CRYSTAL STRUCTURE OF THE MT1-MMP-TIMP-2 COMPLEX
    1buv: CRYSTAL STRUCTURE OF THE MT1-MMP-TIMP-2 COMPLEX
Portal:
  • icon Biology


Stub icon

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

  • v
  • t
  • e