| 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
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MPLPPHPGSP GYINLSYEVL TPLKWYQSMI RQPYPSYGYE PMGGWLHHQI IPVLSQQHPP - 60
SHTLQPHHHL PVVPAQQPVA PQQPMMPVPG HHSMTPTQHH QPNIPPSAQQ PFQQPFQPQA - 120
IPPQSHQPMQ PQSPLHPMQP LAPQPPLPPL FSMQPLSPIL PELPLEAWPA TDKTKREEVD - 180
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| 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)
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| 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.
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| 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:
- Nuclear magnetic resonance (NMR) (298 K; pH: 3; Amelogenin 2 mM; Acetic acid 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) ))
- 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:
- 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
- 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.
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| 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:
- Nuclear magnetic resonance (NMR) (298 K; pH: 3; Amelogenin 2 mM; Acetic acid 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)))
- 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:
- 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
- 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.
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| 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:
- Nuclear magnetic resonance (NMR) (298 K; pH: 3; Acetic acid 2 %; Amelogenin 2 mM)
- 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)))
- 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:
- 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
- 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).
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| 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:
- Nuclear magnetic resonance (NMR) (298 K; pH: 3; Acetic acid 2 %; Amelogenin 2 mM)
- 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)))
- 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:
- 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
- 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.
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| References |
- 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
- 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
- Moradian-Oldak J. "Amelogenins: assembly, processing and control of crystal morphology." Matrix Biol.. 2001; 20(5-6): 293-305. PubMed: 11566263
- 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
- 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
- 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
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| Comments |
AV sent 10/1/2012 (PMID: 15299015)
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