DP00692_A002: Amelogenin, Isoform 2 of X IsoformFASTA viewXML view

General information
DisProt:DP00692_A002
Name:Amelogenin, Isoform 2 of X Isoform
Synonym(s):AMELX_MOUSE
Leucine-rich amelogenin peptide
LRAP
P63277-2
First appeared in release:Release 6.01 (10/15/2012)
UniProt:P63277
UniGene: 
SwissProt: AMELX_MOUSE
TrEMBL:  
NCBI (GI):  
Source organism:Mus musculus (Mouse)
Sequence length:59
Percent disordered:97%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MPLPPHPGSP GYINLSYEVL TPLKWYQSMI RQPPLSPILP ELPLEAWPAT DKTKREEVD



Functional narrative    

DP00692_A002 is alternatively-spliced product 2 of Amelogenin, X isoform.
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DP00692_A002 is the mature form of amelogenin, with signal peptide removed (aa 1-16 in UniProt record).
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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. Several forms are produced by C-terminal processing. Belongs to the amelogenin family. (UniProt)

Region 1: 2-24 Region 2: 25-32 Region 3: 34-48 Region 4: 49-59

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 - Extended
Name:PPI region
Location:2 - 24
Length:23
Region sequence:

PLPPHPGSPGYINLSYEVLTPLK

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. Nuclear magnetic resonance (NMR) (293 K; pH: 3; NaCl 440 mM; rp(H)LRAP (in 2% CD3CO2,5%D2O/95%H2O) 0.35 mM)

  2. Dynamic light scattering (298 K; pH: 3; acetic acid 2 %; rp(H)LRAP (in 2% CD3CO2,5%D2O/95%H2O) 0.35 mM)
References:
  1. Buchko GW, Tarasevich BJ, Roberts J, Snead ML, Shaw WJ. "A solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein)." Biochim. Biophys. Acta. 2010; 1804(9): 1768-74. PubMed: 20304108
Comments:
According to Buchko et al (2010), LRAP consists of two domains: an N-terminal domain containing the protein-protein interaction region (aa 2-24) and a linker region (aa 25-32) and the C-terminal domain comprised of a hydrophobic segment cleaved by enamelysin (aa 34-48) and a mineral-binding domain (aa 49-59).




Region 2
Type:Disordered
Name:linker region
Location:25 - 32
Length:8
Region sequence:

WYQSMIRQ

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Molecular assembly
Functional subclasses: Flexible linkers/spacers
Detection methods:
  1. Nuclear magnetic resonance (NMR) (293 K; pH: 3; NaCl 440 mM; rp(H)LRAP (in 2% CD3CO2,5%D2O/95%H2O) 0.35 mM)

  2. Dynamic light scattering (298 K; pH: 3; acetic acid 2 %; rp(H)LRAP (in 2% CD3CO2,5%D2O/95%H2O) 0.35 mM)
References:
  1. Buchko GW, Tarasevich BJ, Roberts J, Snead ML, Shaw WJ. "A solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein)." Biochim. Biophys. Acta. 2010; 1804(9): 1768-74. PubMed: 20304108
Comments:
 



Region 3
Type:Disordered - Pre-Molten Globule
Name:hydrophobic segment
Location:34 - 48
Length:15
Region sequence:

PLSPILPELPLEAWP

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Nuclear magnetic resonance (NMR) (293 K; pH: 3; NaCl 440 mM; rp(H)LRAP (in 2% CD3CO2,5%D2O/95%H2O) 0.35 mM)

  2. Dynamic light scattering (298 K; pH: 3; acetic acid 2 %; rp(H)LRAP (in 2% CD3CO2,5%D2O/95%H2O) 0.35 mM)
References:
  1. Buchko GW, Tarasevich BJ, Roberts J, Snead ML, Shaw WJ. "A solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein)." Biochim. Biophys. Acta. 2010; 1804(9): 1768-74. PubMed: 20304108
Comments:
 



Region 4
Type:Disordered - Pre-Molten Globule
Name:mineral-binding domain
Location:49 - 59
Length:11
Region sequence:

ATDKTKREEVD

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises from the pre-molten globule state
Functional classes: Molecular assembly
Functional subclasses: Protein-Biocrystal binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (293 K; pH: 3; NaCl 440 mM; rp(H)LRAP (in 2% CD3CO2,5%D2O/95%H2O) 0.35 mM)

  2. Dynamic light scattering (298 K; pH: 3; acetic acid 2 %; rp(H)LRAP (in 2% CD3CO2,5%D2O/95%H2O) 0.35 mM)
References:
  1. Buchko GW, Tarasevich BJ, Roberts J, Snead ML, Shaw WJ. "A solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein)." Biochim. Biophys. Acta. 2010; 1804(9): 1768-74. PubMed: 20304108
Comments:
 



References

  1. Buchko GW, Tarasevich BJ, Roberts J, Snead ML, Shaw WJ. "A solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein)." Biochim. Biophys. Acta. 2010; 1804(9): 1768-74. PubMed: 20304108



Comments


According to Buchko et al (2010), LRAP seems to have cell signaling properties that full-length amelogenin does not.


Experiments by Buchko et al (2010) were performed on recombinant splice-variant mouse Leucine-Rich Amelogenin Protein (rp(H)LRAP).


According to Buchko et al (2010), LRAP consists of two domains: an N-terminal domain containing the protein-protein interaction region (aa 2-24) and a linker region (aa 25-32) and the C-terminal domain comprised of a hydrophobic segment cleaved by enamelysin (aa 34-48) and a mineral-binding domain (aa 49-59).


AV sent 10/1/2012 (PMID 20304108)


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