amelogenin, X isoform isoform X2 [Felis catus]
Protein Classification
Amelogenin domain-containing protein( domain architecture ID 12220051)
Amelogenin domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Amelogenin | smart00818 | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
15-176 | 1.53e-39 | ||||
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. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: 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. 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. : Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 131.84 E-value: 1.53e-39
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| Name | Accession | Description | Interval | E-value | ||||
| Amelogenin | smart00818 | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
15-176 | 1.53e-39 | ||||
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. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: 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. 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. Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 131.84 E-value: 1.53e-39
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| Amelogenin | pfam02948 | Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ... |
15-176 | 2.59e-33 | ||||
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organization and mineralization of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta. Pssm-ID: 460761 [Multi-domain] Cd Length: 179 Bit Score: 116.39 E-value: 2.59e-33
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| Name | Accession | Description | Interval | E-value | ||||
| Amelogenin | smart00818 | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
15-176 | 1.53e-39 | ||||
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. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: 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. 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. Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 131.84 E-value: 1.53e-39
|
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| Amelogenin | pfam02948 | Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ... |
15-176 | 2.59e-33 | ||||
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organization and mineralization of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta. Pssm-ID: 460761 [Multi-domain] Cd Length: 179 Bit Score: 116.39 E-value: 2.59e-33
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