matrix metalloproteinase-21; matrixin 21 (MMP21)

Function: - may have specific function in embryogenesis - cleaves alpha-1-antitrypsin - 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 (putative) Expression: - identified in fetal brain, kidney & liver - in adult tissues found primarily in ovary, kidney, liver, lung, placenta, brain & peripheral blood leukocytes Pathology: - may have role in tumor progression - expressed in various cancer cell lines

Properties

SIZE: entity length = 569 aa MW = 65 kD COMPARTMENT: extracellular matrix MOTIF: signal sequence {1-24} Cysteine switch {115-122} MOTIF: Zn+2-binding site SITE: 117-117 Zn+2-binding site SITE: 283-283 glutamate residue {E284} Zn+2-binding site SITE: 287-287 Zn+2-binding site SITE: 293-293 cysteine residue {C329} MODIFICATION: cysteine residue {C560} Hemopexin-like 1 {333-391} MOTIF: N-glycosylation site {N372} Hemopexin-like 2 {394-449} Hemopexin-like 3 {451-499} Hemopexin-like 4 {506-549} cysteine residue {C560} MODIFICATION: cysteine residue {C329}

Database Correlations

OMIM 608416 UniProt Q8N119 PFAM correlations Entrez Gene 118856 Kegg hsa:118856