Description: Homo sapiens matrix metallopeptidase 14 (membrane-inserted) (MMP14), mRNA. RefSeq Summary (NM_004995): 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]. Transcript (Including UTRs) Position: hg19 chr14:23,305,793-23,316,803 Size: 11,011 Total Exon Count: 10 Strand: + Coding Region Position: hg19 chr14:23,306,027-23,315,248 Size: 9,222 Coding Exon Count: 10
ID:MMP14_HUMAN DESCRIPTION: RecName: Full=Matrix metalloproteinase-14; Short=MMP-14; EC=3.4.24.80; AltName: Full=MMP-X1; AltName: Full=Membrane-type matrix metalloproteinase 1; Short=MT-MMP 1; Short=MTMMP1; AltName: Full=Membrane-type-1 matrix metalloproteinase; Short=MT1-MMP; Short=MT1MMP; Flags: Precursor; FUNCTION: Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. CATALYTIC ACTIVITY: Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain. COFACTOR: Binds 1 zinc ion per subunit (By similarity). COFACTOR: Calcium (By similarity). SUBUNIT: Interacts (via C-terminal cytoplasmic tail) with BST2. INTERACTION: Q9BV57:ADI1; NbExp=4; IntAct=EBI-992788, EBI-992807; P53667:LIMK1; NbExp=4; IntAct=EBI-992788, EBI-444403; SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein (Potential). Melanosome. Cytoplasm. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm. TISSUE SPECIFICITY: Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors. INDUCTION: Up-regulated by NANOS1. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. PTM: The precursor is cleaved by a furin endopeptidase (By similarity). SIMILARITY: Belongs to the peptidase M10A family. SIMILARITY: Contains 4 hemopexin-like domains. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mmp14/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P50281
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
