MMP14

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. Most MMP's are secreted as inactive proproteins 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 expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion. [provided by RefSeq, Jul 2008]

Matrix Metallopeptidase 14

Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity).

May be involved in actin cytoskeleton reorganization by cleaving PTK7 (PubMed:20837484).

Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2 (PubMed:12714657).

Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (PubMed:22330140).

Angiogenesis Source: Ensembl
Astrocyte cell migration Source: Ensembl
Branching morphogenesis of an epithelial tube Source: Ensembl
Cell motility Source: ParkinsonsUK-UCL
Chondrocyte proliferation Source: Ensembl
Collagen catabolic process Source: GO_Central
Craniofacial suture morphogenesis Source: Ensembl
Embryonic cranial skeleton morphogenesis Source: Ensembl
Endochondral ossification Source: Ensembl
Endodermal cell differentiation Source: UniProtKB
Endothelial cell proliferation Source: Ensembl
Extracellular matrix disassembly Source: Reactome
Extracellular matrix organization Source: GO_Central
Head development Source: Ensembl
Lung development Source: Ensembl
Male gonad development Source: Ensembl
Negative regulation of focal adhesion assembly Source: Ensembl
Negative regulation of Notch signaling pathway Source: UniProtKB
Ovarian follicle development Source: Ensembl
Positive regulation of B cell differentiation Source: UniProtKB
Positive regulation of cell growth Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Positive regulation of macrophage migration Source: Ensembl
Positive regulation of myotube differentiation Source: UniProtKB
Positive regulation of protein processing Source: Ensembl
Protein processing Source: ParkinsonsUK-UCL
Proteolysis Source: ParkinsonsUK-UCL
Regulation of protein localization to plasma membrane Source: UniProtKB
Response to estrogen Source: Ensembl
Response to hypoxia Source: Ensembl
Response to mechanical stimulus Source: Ensembl
Response to odorant Source: Ensembl
Response to organic cyclic compound Source: Ensembl
Response to oxidative stress Source: Ensembl
Skeletal system development Source: GO_Central
Tissue remodeling Source: Ensembl
Zymogen activation Source: UniProtKB

Cytoplasm
Other locations
Membrane
Melanosome
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm.

Winchester syndrome (WNCHRS):
A disease characterized by severe osteolysis in the hands and feet, generalized osteoporosis, bone thinning, and absence of subcutaneous nodules. Various additional features include coarse face, corneal opacities, gum hypertrophy, and EKG changes.

Extracellular: 112-541
Helical: 542-562
Cytoplasmic: 563-582

The precursor is cleaved by a furin endopeptidase.
Tyrosine phosphorylated by PKDCC/VLK.