MMP15

 Matrix metalloproteinase 15 also known as MMP15 is an enzyme that in humans is encoded by the MMP15 gene.^[4][5]

MMP15
Identifiers
Aliases	MMP15, MT2-MMP, MTMMP2, SMCP-2, MMP-15, MT2MMP, matrix metallopeptidase 15
External IDs	OMIM: 602261 MGI: 109320 HomoloGene: 20549 GeneCards: MMP15
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16q21 Start 58,025,754 bp[1] End 58,046,901 bp[1]
Gene ontology Molecular function • zinc ion binding • metal ion binding • peptidase activity • GO:0001948 protein binding • GO:0010577 enzyme activator activity • metalloendopeptidase activity • hydrolase activity • metallopeptidase activity • metalloaminopeptidase activity Cellular component • integral component of membrane • membrane • extracellular matrix • cell membrane • integral component of plasma membrane • extracellular Biological process • response to estradiol • endodermal cell differentiation • extracellular matrix disassembly • cellular protein modification process • collagen catabolic process • GO:0048554 positive regulation of catalytic activity • proteolysis • extracellular matrix organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4324	17388
Ensembl	ENSG00000102996	ENSMUSG00000031790
UniProt	P51511	O54732
RefSeq (mRNA)	NM_002428	NM_008609
RefSeq (protein)	NP_002419	NP_032635
Location (UCSC)	Chr 16: 58.03 – 58.05 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

FunctionEdit

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 proenzymes 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; members of this subfamily can be anchored to the extracellular membrane by either a transmembrane domain or glycophosphatidylinositol linkage, suggesting that these proteins are expressed at the cell surface rather than secreted in a soluble form.^[6]

This article uses material from the Wikipedia article  Metasyntactic variable, which is released under the  Creative Commons Attribution-ShareAlike 3.0 Unported License.