DP00692_A001: Amelogenin, Isoform 1 of X isoformFASTA viewXML view

General information
DisProt:DP00692_A001
Name:Amelogenin, Isoform 1 of X isoform
Synonym(s):AMELX_MOUSE
LRAP
P63277-1
Leucine-rich amelogenin peptide
First appeared in release:Release 6.01 (10/15/2012)
UniProt:P63277
UniGene: 
SwissProt: AMELX_MOUSE
TrEMBL:  
NCBI (GI):  
Source organism:Mus musculus
Sequence length:180
Percent disordered:100%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MPLPPHPGSP GYINLSYEVL TPLKWYQSMI RQPYPSYGYE PMGGWLHHQI IPVLSQQHPP - 60
SHTLQPHHHL PVVPAQQPVA PQQPMMPVPG HHSMTPTQHH QPNIPPSAQQ PFQQPFQPQA - 120
IPPQSHQPMQ PQSPLHPMQP LAPQPPLPPL FSMQPLSPIL PELPLEAWPA TDKTKREEVD - 180



Functional narrative    

DP00692_A001 is alternatively-spliced product 1 of Amelogenin, X isoform.
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DP00692_A001 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: 1-57 Region 2: 58-151 Region 3: 152-165 Region 4: 166-180

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:N-terminal TRAP domain
Location:1 - 57
Length:57
Region sequence:

MPLPPHPGSPGYINLSYEVLTPLKWYQSMIRQPYPSYGYEPMGGWLHHQIIPVLSQQ

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Modification site
Molecular assembly
Molecular recognition effectors
Functional subclasses: Protein-protein binding
Polymerization
Phosphorylation
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 3; Amelogenin 2 mM; Acetic acid 2 %)

  2. Nuclear magnetic resonance (NMR) (293 K; pH: 3; 2% CD3CO2D; 95% H2O/ 5% D2O; Amelogenin rp(H)M180 (titration end points: 0.1 mM (NaCl), 0.11 mM (CaCl2) ); Sodium chloride or Calcium chloride (titration end points: 300 mM (NaCl), 165 mM (CaCl2) ))

  3. Nuclear magnetic resonance (NMR) (293 K; 2% CD3CO2D; 95% H2O/ 5% D2O; Amelogenin rp(H)M180 0.14 mM; NaOH (pH titrations: 4.5 to 5.0 ) 1 M)

References:
  1. Buchko GW, Bekhazi J, Cort JR, Valentine NB, Snead ML, Shaw WJ. "1H, 13C, and 15N resonance assignments of murine amelogenin, an enamel biomineralization protein." Biomol NMR Assign. 2008; 2(1): 89-91. PubMed: 19081741

  2. Buchko GW, Tarasevich BJ, Bekhazi J, Snead ML, Shaw WJ. "A solution NMR investigation into the early events of amelogenin nanosphere self-assembly initiated with sodium chloride or calcium chloride." Biochemistry. 2008; 47(50): 13215-22. PubMed: 19086270

Comments:
N-terminal TRAP domain comprises a protein-protein interaction domain at aa M1-K24 and a lectin-like binding domain at aa P33-W45. (Moradian-Oldak, 2001, and references within)
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During nanosphere assembly, Buchko et al (2008, Biochemistry) describe dimerization occurring first at E18-Y34, followed by contact at both G8-Q57 and L141-T171.
Additionally, Buchko et al describe increased ionic strength as the driving force for self-assembly. Physiological ionic strength is high during enamel formation in pig (Aoba et al 1987).
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In Amelogenin, both N-terminal and C-terminal domains are highly conserved. Phosporylation site is found at S16. Secondary structure of the TRAP domain is extended beta-sheet/beta-strand.




Region 2
Type:Disordered - Extended
Name:HQP-rich region
Location:58 - 151
Length:94
Region sequence:

HPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPFQ
PQAIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLF

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Molecular assembly
Molecular recognition effectors
Functional subclasses: Metal binding
Polymerization
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 3; Amelogenin 2 mM; Acetic acid 2 %)

  2. Nuclear magnetic resonance (NMR) (293 K; pH: 3; 2% CD3CO2D; 95% H2O/ 5% D2O; Amelogenin rp(H)M180 (titration end points: 0.1 mM (NaCl), 0.11 mM (CaCl2)); Sodium chloride or Calcium chloride (titration end points: 300 mM (NaCl), 165 mM (CaCl2)))

  3. Nuclear magnetic resonance (NMR) (293 K; 2% CD3CO2D; 95% H2O/ 5% D2O; Amelogenin rp(H)M180 0.14 mM; NaOH (pH titrations: 4.5 to 5.0) 1 M)

References:
  1. Buchko GW, Bekhazi J, Cort JR, Valentine NB, Snead ML, Shaw WJ. "1H, 13C, and 15N resonance assignments of murine amelogenin, an enamel biomineralization protein." Biomol NMR Assign. 2008; 2(1): 89-91. PubMed: 19081741

  2. Buchko GW, Tarasevich BJ, Bekhazi J, Snead ML, Shaw WJ. "A solution NMR investigation into the early events of amelogenin nanosphere self-assembly initiated with sodium chloride or calcium chloride." Biochemistry. 2008; 47(50): 13215-22. PubMed: 19086270

Comments:
Buchko et al (2008, Biochemistry) describe that during nanosphere assembly, dimerization occurring first at E18-Y34, followed by contact at both G8-Q57 and L141-T171.

Buchko et al also describe increased ionic strength as the driving force for self-assembly. Physiologic ionic strength is high during enamel formation in pig (Aoba et al 1987).


Secondary structure of the HQP-rich region is extended beta-spiral/polyproline II.




Region 3
Type:Disordered - Extended
Name:C-terminal hydrophibic region
Location:152 - 165
Length:14
Region sequence:

SMQPLSPILPELPL

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Molecular recognition effectors
Molecular assembly
Functional subclasses: Polymerization
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 3; Acetic acid 2 %; Amelogenin 2 mM)

  2. Nuclear magnetic resonance (NMR) (293 K; pH: 3; 2% CD3CO2D; 95% H2O/ 5% D2O; Amelogenin rp(H)M180 (titration end points: 0.1 mM (NaCl), 0.11 mM (CaCl2)); Sodium chloride or Calcium chloride (titration end points: 300 mM (NaCl), 165 mM (CaCl2)))

  3. Nuclear magnetic resonance (NMR) (293 K; 2% CD3CO2D; 95% H2O/ 5% D2O; Amelogenin rp(H)M180 0.14 mM; NaOH (pH titrations: 4.5 to 5.0) 1 M)

References:
  1. Buchko GW, Bekhazi J, Cort JR, Valentine NB, Snead ML, Shaw WJ. "1H, 13C, and 15N resonance assignments of murine amelogenin, an enamel biomineralization protein." Biomol NMR Assign. 2008; 2(1): 89-91. PubMed: 19081741

  2. Buchko GW, Tarasevich BJ, Bekhazi J, Snead ML, Shaw WJ. "A solution NMR investigation into the early events of amelogenin nanosphere self-assembly initiated with sodium chloride or calcium chloride." Biochemistry. 2008; 47(50): 13215-22. PubMed: 19086270

Comments:
Buchko et al (2008, Biochemistry) describe that during nanosphere assembly, dimerization occurring first at E18-Y34, followed by contact at both G8-Q57 and L141-T171.

Buchko et al also describe increased ionic strength as the driving force for self-assembly. Physiologic ionic strength is high during enamel formation in pig (Aoba et al 1987).




Region 4
Type:Disordered
Name:C-terminal hydrophilic region
Location:166 - 180
Length:15
Region sequence:

EAWPATDKTKREEVD

Modification type: Engineered
Monomeric
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Molecular recognition effectors
Molecular assembly
Functional subclasses: Polymerization
Protein-protein binding
Protein-Biocrystal binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 3; Acetic acid 2 %; Amelogenin 2 mM)

  2. Nuclear magnetic resonance (NMR) (293 K; pH: 3; 2% CD3CO2D; 95% H2O/ 5% D2O; Amelogenin rp(H)M180 (titration end points: 0.1 mM (NaCl), 0.11 mM (CaCl2)); Sodium chloride or Calcium chloride (titration end points: 300 mM (NaCl), 165 mM (CaCl2)))

  3. Nuclear magnetic resonance (NMR) (293 K; 2% CD3CO2D; 95% H2O/ 5% D2O; Amelogenin rp(H)M180 0.14 mM; NaOH (pH titrations: 4.5 to 5.0) 1 M)

References:
  1. Buchko GW, Bekhazi J, Cort JR, Valentine NB, Snead ML, Shaw WJ. "1H, 13C, and 15N resonance assignments of murine amelogenin, an enamel biomineralization protein." Biomol NMR Assign. 2008; 2(1): 89-91. PubMed: 19081741

  2. Buchko GW, Tarasevich BJ, Bekhazi J, Snead ML, Shaw WJ. "A solution NMR investigation into the early events of amelogenin nanosphere self-assembly initiated with sodium chloride or calcium chloride." Biochemistry. 2008; 47(50): 13215-22. PubMed: 19086270

Comments:
Buchko et al (2008, Biochemistry) describe that during nanosphere assembly, dimerization occurring first at E18-Y34, followed by contact at both G8-Q57 and L141-T171.

Buchko et al also describe increased ionic strength as the driving force for self-assembly. Physiologic ionic strength is high during enamel formation in pig (Aoba et al 1987).


The hydrophilic C-terminal region is a random coil formation that interacts with apatite crystals during enamel formation (Shaw et al, 2004, 2008, 2008).

NMR experiments by Shaw et al were performed on synthesized bovine LRAP peptide fragments; Shaw et al references appear below in overall protein record references section.




References

  1. Aoba T, Moreno EC. "The enamel fluid in the early secretory stage of porcine amelogenesis: chemical composition and saturation with respect to enamel mineral." Calcif. Tissue Int.. 1987; 41(2): 86-94. PubMed: 3115550

  2. Margolis HC, Beniash E, Fowler CE. "Role of macromolecular assembly of enamel matrix proteins in enamel formation." J. Dent. Res.. 2006; 85(9): 775-93. PubMed: 16931858

  3. Moradian-Oldak J. "Amelogenins: assembly, processing and control of crystal morphology." Matrix Biol.. 2001; 20(5-6): 293-305. PubMed: 11566263

  4. Shaw WJ, Campbell AA, Paine ML, Snead ML. "The COOH terminus of the amelogenin, LRAP, is oriented next to the hydroxyapatite surface." J. Biol. Chem.. 2004; 279(39): 40263-6. PubMed: 15299015

  5. Shaw WJ, Ferris K. "Structure, orientation, and dynamics of the C-terminal hexapeptide of LRAP determined using solid-state NMR." J Phys Chem B. 2008; 112(51): 16975-81. PubMed: 19368031

  6. Shaw WJ, Ferris K, Tarasevich B, Larson JL. "The structure and orientation of the C-terminus of LRAP." Biophys. J.. 2008; 94(8): 3247-57. PubMed: 18192371



Comments


AV sent 10/1/2012 (PMID: 15299015)


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