Amelogenin (IPR004116)

Short name: Amelogenin

Overlapping homologous superfamilies


Family relationships



Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth. They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins [PMID: 8118759].

Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units [PMID: 8454575]: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region [PMID: 2598664]. The beta-spiral offers a probable site for interactions with Ca2+ ions.

Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide [PMID: 7782077].

GO terms

Biological Process

GO:0007275 multicellular organism development

Molecular Function

No terms assigned in this category.

Cellular Component

GO:0062023 collagen-containing extracellular matrix

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.