matrix metalloproteinase-28; matrixin 28; epilysin (MMP28, UNQ1893/PRO4339)

Function: - can degrade casein - could play a role in tissue homeostasis & repair - precursor is cleaved by a furin endopeptidase Cofactor: - binds 1 Zn⁺² per subunit (putative) - Ca⁺² (putative) Structure: - the conserved Cys present in the cysteine-switch motif binds the catalytic Zn⁺², thus inhibiting the enzyme - dissociation of Cys from Zn⁺² upon activation- peptide release activates the enzyme - belongs to the peptidase M10A family - contains 4 hemopexin-like domains Compartment: - secreted, extracellular space, extracellular matrix Alternative splicing: - named isoforms=1 - at least 2 isoforms may be produced Expression: - expressed at high levels in testes & lung - low levels are detected in kidney, pancreas & skin - also expressed in fetal lung, brain, skeletal muscle & kidney - expressed selectively in keratinocytesis Pathology: - widely expressed in several carcinomas - up-regulated in response to injury in the skin

Properties

SIZE: entity length = 520 aa MW = 59 kD COMPARTMENT: extracellular matrix MOTIF: signal sequence {1-22} Cysteine switch {89-96} MOTIF: Zn+2-binding site SITE: 91-91 N-glycosylation site {N164} Zn+2-binding site SITE: 240-240 glutamate residue {E241} Zn+2-binding site SITE: 244-244 Zn+2-binding site SITE: 250-250 cysteine residue {C324} MODIFICATION: cysteine residue {C510} Hemopexin-like 1 {328-371} MOTIF: N-glycosylation site {N355} Hemopexin-like 2 {373-416} Hemopexin-like 3 {418-464} Hemopexin-like 4 {466-510} MOTIF: cysteine residue {C510} MODIFICATION: cysteine residue {C324}

Database Correlations

OMIM 608417 UniProt Q9H239 PFAM correlations Entrez Gene 79148