Sequence of this protein is as follows: MVARVGLLLR ALQLLLWGHL DAQPAERGGQ ELRKEAEAFL EKYGYLNEQV PKAPTSTRFS DAIRAFQWVS QLPVSGVLDR ATLRQMTRPR CGVTDTNSYA AWAERISDLF ARHRTKMRRK KRFAKQGNKW YKQHLSYRLV NWPEHLPEPA VRGAVRAAFQ LWSNVSALEF WEAPATGPAD IRLTFFQGDH NDGLGNAFDG PGGALAHAFL PRRGEAHFDQ DERWSLSRRR GRNLFVVLAH EIGHTLGLTH SPAPRALMAP YYKRLGRDAL LSWDDVLAVQ SLYGKPLGGS VAVQLPGKLF TDFETWDSYS PQGRRPETQG PKYCHSSFDA ITVDRQQQLY IFKGSHFWEV AADGNVSEPR PLQERWVGLP PNIEAAAVSL NDGDFYFFKV QSV
Epilysin, also known as matrix metalloproteinase-28 (MMP-28), is a secreted protein that belongs to the peptidase M10A family. Matrix metalloproteinase proteins are responsible for the breakdown of the extracellular matrix which is important for normal physiological processes such as tissue remodeling, reproduction and embryonic development. Epilysin is produced by proliferating keratinocytes and is responsible for mediating the degradation of casein. Its expression is upregulated in response to injury of the skin suggesting that Epilysin may be involved in tissue repair and homeostasis. In addition, Epilysin may function predominantly in the nervous system. Incubation of Epilysin with rat embryonic brain tissue results in the degradation of myelin proteins. In Xenopus, Epilysin localizes to nerves and is upregulated during neurulation. This suggests that Epilysin plays an evolutionarily conserved role in neural development and may be involved in modulating the axonal-glial extracellular environment.
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Protein Aliases: Epilysin; matrix metallo protease; matrix metalloprotease MMP25; Matrix metalloproteinase-28; MMP; MMP-28; MMPs; PRO4339; UNQ1893
Gene Aliases: EPILYSIN; MM28; MMP-25; MMP-28; MMP25; MMP28; UNQ1893/PRO4339
UniProt ID: (Human) Q9H239
Entrez Gene ID: (Human) 79148