| General information | | DisProt: | DP00715 | | Name: | Aragonite protein AP24 | | Synonym(s): | Q9BP38_HALRU
AP24
| | First appeared in release: | Release 5.9 (02/23/2012) | | UniProt: | Q9BP38 | | UniGene: | | | SwissProt: | Q9BP38_HALRU | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Haliotis rufescens (California red abalone) | | Sequence length: | 171 | | Percent disordered: | 32% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MTWMKMFYLT LAVTAAVLLV TVAAADDDED ASSGLCNQYN QNVTTRPNNK PKMFLRKNIN - 60
FEIISVHNIW RDPNTVYWCD FSLEEEDGIK HWRHYDFNAT HWWVEKGCSG TFVVEECNTK - 120
DITNPGPRST AGKSPMQGTL AAPKPVANWM SIMSRSRFDM GTWDKEGFNM L
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| Functional narrative |
Aragonite is a polymorph form of calcium carbonate; calcite and vaterite are two other forms commonly found in biominerals. "Aragonite protein AP24" is involved in biomineralization and belongs to a class of mineral-interaction polypeptides that are found in the aragonite-containing nacre layer of mollusk shell. Aragonite proteins AP7 (DP00714) and AP24 have been shown to preferentially interfere with calcium carbonate mineral growth in vitro. It is believed that aragonite proteins AP7 and AP24 play an important combined role in aragonite polymorph selection in the mollusk shell. (based on Wustman).
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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 | | Name: | Signal peptide (potential) | | Location: | 1 - 24 | | Length: | 24 | | Region sequence: |
MTWMKMFYLTLAVTAAVLLVTVAA | | Modification type: | Native
| | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | | Detection methods:
| References:
- Michenfelder M, Fu G, Lawrence C, Weaver JC, Wustman BA, Taranto L, Evans JS, Morse DE. "Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains." Biopolymers. 2003; 70(4): 522-33. PubMed: 14648763
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | N-terminal domain | | Location: | 25 - 54 | | Length: | 30 | | Region sequence: |
ADDDEDASSGLCNQYNQNVTTRPNNKPKMF | | Modification type: | Engineered
Fragment
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Modification site
| | Functional subclasses: | Glycosylation
Protein-Biocrystal binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7.4; AP24-1 peptide 7.4 uM; HCl or NaOH)
- Nuclear magnetic resonance (NMR) (293 K; pH: 7.4; 90% H2O, 10% D2O; AP24-1 peptide 850 uM)
| References:
- Michenfelder M, Fu G, Lawrence C, Weaver JC, Wustman BA, Taranto L, Evans JS, Morse DE. "Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains." Biopolymers. 2003; 70(4): 522-33. PubMed: 14648763
- Wustman BA, Morse DE, Evans JS. "Structural characterization of the N-terminal mineral modification domains from the molluscan crystal-modulating biomineralization proteins, AP7 and AP24." Biopolymers. 2004; 74(5): 363-76. PubMed: 15222016
| Comments:Michenfelder et al (2003) identified the N-terminal as a putative calcite binding domain, showing it to "bind strongly to calcite growth steps,...inhibiting calcite growth."
They also describe potential N-glycosylation sites at N42-T44 and N98-T100.
It was found that AP7 and AP24 work in complex together, and in a concentration-dependent manner, for optimal calcite inhibition.
Michenfelder et al (2003) and Wustman et al (2004) used a synthetic construct of mature AP24 N-terminal (residues 25-54 of full-length protein) which they call AP24-1. Detection method used by Michenfelder et al was far-UV CD; Wustman et al used NMR.
Wustman et al (2004) describe areas of random coil character at A25-S33, Q38-N40, N49-K52, and areas of turn/loop/bend character at G34-C36, Q41-N48, M53-F54.
Additionally, they describe a putative mineral or Ca(II) binding domain at D26-D30.
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| References |
- Michenfelder M, Fu G, Lawrence C, Weaver JC, Wustman BA, Taranto L, Evans JS, Morse DE. "Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains." Biopolymers. 2003; 70(4): 522-33. PubMed: 14648763
- Wustman BA, Morse DE, Evans JS. "Structural characterization of the N-terminal mineral modification domains from the molluscan crystal-modulating biomineralization proteins, AP7 and AP24." Biopolymers. 2004; 74(5): 363-76. PubMed: 15222016
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| Comments |
Verification request sent 2-21-2012 (PMID:14648763)
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