MMP26

Matrix metalloproteinase-26 also known as matrilysin-2 and endometase is an enzyme that in humans is encoded by the MMP26 gene.^[3][4][5]

MMP26
Identifiers
Aliases	MMP26, matrix metallopeptidase 26
External IDs	OMIM: 605470; HomoloGene: 49684; GeneCards: MMP26; OMA:MMP26 - orthologs
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11p15.4 Start 4,704,784 bp[1] End 4,992,431 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in buccal mucosa cell testicle endometrium gonad prostate renal cortex myometrium hepatobiliary system skeletal muscle smooth muscle tissue n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function zinc ion binding peptidase activity metalloendopeptidase activity hydrolase activity metallopeptidase activity metal ion binding Cellular component extracellular region extracellular matrix extracellular space Biological process collagen catabolic process negative regulation of inflammatory response proteolysis extracellular matrix organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 56547 n/a Ensembl ENSG00000167346 n/a UniProt Q9NRE1 n/a RefSeq (mRNA) NM_021801 NM_001384608 n/a RefSeq (protein) NP_068573 n/a Location (UCSC) Chr 11: 4.7 – 4.99 Mb n/a PubMed search [2] n/a
Wikidata
View/Edit Human

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 proproteins which are activated when cleaved by extracellular proteinases. The encoded protein degrades type IV collagen, fibronectin, fibrinogen, casein, vitronectin, alpha 1-antitrypsin (A1AT), alpha 2-macroglobulin (A2M), and insulin-like growth factor-binding protein 1 (IGFBP), and activates MMP9 by cleavage. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain.^[5]