Annotations for this protein have been verified by the authors of the corresponding papers


DP00693: AmelogeninFASTA viewXML view

General information
DisProt:DP00693
Name:Amelogenin
Synonym(s):AMEL_PIG
Amelogenin 173A
First appeared in release:Release 5.5 (11/17/2010)
UniProt:P45561
UniGene: 
SwissProt: AMEL_PIG
TrEMBL:  
NCBI (GI):  
Source organism:Sus scrofa (Pig)
Sequence length:173
Percent disordered:99%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MPLPPHPGHP GYINFSYEVL TPLKWYQNMI RHPYTSYGYE PMGGWLHHQI IPVVSQQTPQ - 60
SHALQPHHHI PMVPAQQPGI PQQPMMPLPG QHSMTPTQHH QPNLPLPAQQ PFQPQPVQPQ - 120
PHQPLQPQSP MHPIQPLLPQ PPLPPMFSMQ SLLPDLPLEA WPATDKTKRE EVD



Functional narrative    

Plays a role in the biomineralization of teeth. Seems 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. A number of other isoforms are produced by carboxy-terminal processing. Belongs to the amelogenin family. (UniProt) DP00693 is the mature form of amelogenin, with signal peptide removed (aa 1-16 in UniProt record).

Region 1: 2-22 Region 2: 23-27 Region 3: 28-36 Region 4: 37-45 Region 5: 46-62 Region 6: 63-69 Region 7: 70-89 Region 8: 90-101 Region 9: 102-145 Region 10: 146-173

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered w/ Residual Structure
Name:extended beta-strand
Location:2 - 22
Length:21
Region sequence:

PLPPHPGHPGYINFSYEVLTP

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Dynamic light scattering (283 K; pH: 6; rP172 Amelogenin 75 uM; unbuffered double-distiilled water)

  2. Circular dichroism (CD) spectroscopy, far-UV (283 K; )

  3. Nuclear magnetic resonance (NMR) (283 K; pH: 3.8; D2O (10% v/v); Milli-Q pure deionized distilled water; rP172 Amelogenin 75 uM)
References:
  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004
Comments:
According to Delak et al (2009), amelogenin is divided into three domains: the extended N-terminal TRAP domain (aa 1-45), a central domain (aa 46-156) and the pre-molten globule C-terminal domain (aa 157-173).


Region 2
Type:Disordered w/ Residual Structure
Name:alpha-helix
Location:23 - 27
Length:5
Region sequence:

LKWYQ

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Dynamic light scattering (283 K; pH: 6; rP172 Amelogenin 75 uM; unbuffered double-distiilled water)

  2. Circular dichroism (CD) spectroscopy, far-UV (283 K; )

  3. Nuclear magnetic resonance (NMR) (283 K; pH: 3.8; D2O (10% v/v); Milli-Q pure deionized distilled water; rP172 Amelogenin 75 uM)
References:
  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004
Comments:
According to Delak et al (2009), amelogenin is divided into three domains: the extended N-terminal TRAP domain (aa 1-45), a central domain (aa 46-156) and the pre-molten globule C-terminal domain (aa 157-173).


Region 3
Type:Disordered - Extended
Name:random coil
Location:28 - 36
Length:9
Region sequence:

NMIRHPYTS

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Dynamic light scattering (283 K; pH: 6; rP172 Amelogenin 75 uM; unbuffered double-distiilled water)

  2. Circular dichroism (CD) spectroscopy, far-UV (283 K; )

  3. Nuclear magnetic resonance (NMR) (283 K; pH: 3.8; D2O (10% v/v); Milli-Q pure deionized distilled water; rP172 Amelogenin 75 uM)
References:
  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004
Comments:
According to Delak et al (2009), amelogenin is divided into three domains: the extended N-terminal TRAP domain (aa 1-45), a central domain (aa 46-156) and the pre-molten globule C-terminal domain (aa 157-173).


Region 4
Type:Disordered w/ Residual Structure
Name:beta-turn
Location:37 - 45
Length:9
Region sequence:

YGYEPMGGW

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Dynamic light scattering (283 K; pH: 6; rP172 Amelogenin 75 uM; unbuffered double-distiilled water)

  2. Circular dichroism (CD) spectroscopy, far-UV (283 K; )

  3. Nuclear magnetic resonance (NMR) (283 K; pH: 3; D2O (10% v/v); Milli-Q pure deionized distilled water; rP172 Amelogenin 75 uM)
References:
  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004
Comments:
According to Delak et al (2009), amelogenin is divided into three domains: the extended N-terminal TRAP domain (aa 1-45), a central domain (aa 46-156) and the pre-molten globule C-terminal domain (aa 157-173).


Region 5
Type:Disordered w/ Residual Structure
Name:extended beta-strand
Location:46 - 62
Length:17
Region sequence:

LHHQIIPVVSQQTPQSH

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Dynamic light scattering (283 K; pH: 6; rP172 Amelogenin 75 uM; unbuffered double-distiilled water)

  2. Circular dichroism (CD) spectroscopy, far-UV (283 K; )

  3. Nuclear magnetic resonance (NMR) (283 K; pH: 3; D2O (10% v/v); Milli-Q pure deionized distilled water; rP172 Amelogenin 75 uM)
References:
  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004
Comments:
According to Delak et al (2009), amelogenin is divided into three domains: the extended N-terminal TRAP domain (aa 1-45), a central domain (aa 46-156) and the pre-molten globule C-terminal domain (aa 157-173).


Region 6
Type:Disordered
Name:random coil
Location:63 - 69
Length:7
Region sequence:

ALQPHHH

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Dynamic light scattering (283 K; pH: 6; rP172 Amelogenin 75 uM; unbuffered double-distiilled water)

  2. Circular dichroism (CD) spectroscopy, far-UV (283 K; )

  3. Nuclear magnetic resonance (NMR) (283 K; pH: 3; D2O (10% v/v); Milli-Q pure deionized distilled water; rP172 Amelogenin 75 uM)
References:
  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004
Comments:
According to Delak et al (2009), amelogenin is divided into three domains: the extended N-terminal TRAP domain (aa 1-45), a central domain (aa 46-156) and the pre-molten globule C-terminal domain (aa 157-173).


Region 7
Type:Disordered w/ Residual Structure
Name:PPII helix
Location:70 - 89
Length:20
Region sequence:

IPMVPAQQPGIPQQPMMPLP

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Dynamic light scattering (283 K; pH: 6; rP172 Amelogenin 75 uM; unbuffered double-distiilled water)

  2. Circular dichroism (CD) spectroscopy, far-UV (283 K; )

  3. Nuclear magnetic resonance (NMR) (283 K; pH: 3; D2O (10% v/v); Milli-Q pure deionized distilled water; rP172 Amelogenin 75 uM)
References:
  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004
Comments:
According to Delak et al (2009), amelogenin is divided into three domains: the extended N-terminal TRAP domain (aa 1-45), a central domain (aa 46-156) and the pre-molten globule C-terminal domain (aa 157-173).


Region 8
Type:Disordered w/ Residual Structure
Name:extended beta-strand
Location:90 - 101
Length:12
Region sequence:

GQHSMTPTQHHQ

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Dynamic light scattering (283 K; pH: 6; rP172 Amelogenin 75 uM; unbuffered double-distiilled water)

  2. Circular dichroism (CD) spectroscopy, far-UV (283 K; )

  3. Nuclear magnetic resonance (NMR) (283 K; pH: 3; D2O (10% v/v); Milli-Q pure deionized distilled water; rP172 Amelogenin 75 uM)
References:
  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004
Comments:
According to Delak et al (2009), amelogenin is divided into three domains: the extended N-terminal TRAP domain (aa 1-45), a central domain (aa 46-156) and the pre-molten globule C-terminal domain (aa 157-173).


Region 9
Type:Disordered w/ Residual Structure
Name:PPII helix
Location:102 - 145
Length:44
Region sequence:

PNLPLPAQQPFQPQPVQPQPHQPLQPQSPMHPIQPLLPQPPLPP

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Dynamic light scattering (283 K; pH: 6; rP172 Amelogenin 75 uM; unbuffered double-distiilled water)

  2. Circular dichroism (CD) spectroscopy, far-UV (283 K; )

  3. Nuclear magnetic resonance (NMR) (283 K; pH: 3; D2O (10% v/v); Milli-Q pure deionized distilled water; rP172 Amelogenin 75 uM)
References:
  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004
Comments:
According to Delak et al (2009), amelogenin is divided into three domains: the extended N-terminal TRAP domain (aa 1-45), a central domain (aa 46-156) and the pre-molten globule C-terminal domain (aa 157-173).


Region 10
Type:Disordered - Pre-Molten Globule
Name:random coil
Location:146 - 173
Length:28
Region sequence:

MFSMQSLLPDLPLEAWPATDKTKREEVD

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Molecular assembly
Functional subclasses: Protein-Biocrystal binding
Detection methods:
  1. Dynamic light scattering (283 K; pH: 6; rP172 Amelogenin 75 uM; unbuffered double-distiilled water)

  2. Circular dichroism (CD) spectroscopy, far-UV (283 K; )

  3. Nuclear magnetic resonance (NMR) (283 K; pH: 3; D2O (10% v/v); Milli-Q pure deionized distilled water; rP172 Amelogenin 75 uM)
References:
  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004
Comments:
According to Delak et al (2009), amelogenin is divided into three domains: the extended N-terminal TRAP domain (aa 1-45), a central domain (aa 46-156) and the pre-molten globule C-terminal domain (aa 157-173).


References

  1. Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. "The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form." Biochemistry. 2009; 48(10): 2272-81. PubMed: 19236004

  2. Lakshminarayanan R, Fan D, Du C, Moradian-Oldak J. "The role of secondary structure in the entropically driven amelogenin self-assembly." Biophys J. 2007; 93(10): 3664-74. PubMed: 17704165

  3. Moradian-Oldak J and Lakshminarayanan L. (Bentham Science Publishers, Ltd, e-book). "Intrinsic disorder in amelogenins." Amelogenins: Multifaceted Proteins For Dental And Bone Formation And Repair. 2010; 106-132.



Comments


Experiments by Delak et al (2009) were performed on recombinant porcine amelogenin rP172.


AV 11/03/2010 (PubMed: 19236004)


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