MMP15

Matrix metalloproteinase 15 also known as MMP15 is an enzyme that in humans is encoded by the MMP15 gene.^[5][6]

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; OMA:MMP15 - orthologs
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16q21 Start 58,025,754 bp[1] End 58,046,901 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8 C5|8 47.12 cM Start 96,078,896 bp[2] End 96,101,708 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon apex of heart right lobe of thyroid gland left lobe of thyroid gland right lobe of liver left ventricle right testis left testis right auricle of heart body of stomach Top expressed in external carotid artery internal carotid artery epithelium of stomach Paneth cell trigeminal ganglion atrium supraoptic nucleus aortic valve conjunctival fornix lumbar spinal ganglion More reference expression data BioGPS n/a
Gene ontology Molecular function zinc ion binding metal ion binding peptidase activity protein binding enzyme activator activity metalloendopeptidase activity hydrolase activity metallopeptidase activity metalloaminopeptidase activity Cellular component integral component of membrane membrane extracellular matrix plasma membrane integral component of plasma membrane extracellular space Biological process response to estradiol endodermal cell differentiation extracellular matrix disassembly collagen catabolic process 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 Chr 8: 96.08 – 96.1 Mb PubMed search [3] [4]
Wikidata
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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. 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.^[7]