| General information | | DisProt: | DP00531 | | Name: | Abscisic stress-ripening protein 1 | | Synonym(s): | ASR1_SOLLC
| | First appeared in release: | Release 3.7 (01/28/2008) | | UniProt: | Q08655 | | UniGene: | Les.17636 | | SwissProt: | ASR1_SOLLC | | TrEMBL: | | | NCBI (GI): | 584786 | | Source organism: | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | | Sequence length: | 115 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MEEEKHHHHH LFHHKDKAEE GPVDYEKEIK HHKHLEQIGK LGTVAAGAYA LHEKHEAKKD - 60
PEHAHKHKIE EEIAAAAAVG AGGFAFHEHH EKKDAKKEEK KKLRGDTTIS SKLLF
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| Functional narrative |
Abscisic acid stress ripening 1 (ASR1) is a low molecular weight plant-specific protein encoded by an abiotic stress-regulated gene. The ASR1 protein possesses a zinc-dependent DNA-binding activity. Tomato (Solanum lycopersicum) leaf soluble ASR1 is unstructured in the absence of added zinc and gains structure upon binding of the metal ion.
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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: | | | Location: | 1 - 115 | | Length: | 115 | | Region sequence: |
MEEEKHHHHHLFHHKDKAEEGPVDYEKEIKHHKHLEQIGKLGTVAAGAYALHEKHEAKKD
PEHAHKHKIEEEIAAAAAVGAGGFAFHEHHEKKDAKKEEKKKLRGDTTISSKLLF | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Metal binding
Protein-DNA binding
| Detection methods:
- Dynamic light scattering (pH: 7.5; NaCl 100 mM; Tris-HCl 20 mM; Zinc chloride 1 mM)
- Size exclusion/gel filtration chromatography (pH: 7; NaCl 100 mM; Tris-HCl 50 mM)
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.5; HEPES-NaOH 20 mM; NaCl 20 mM)
- Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy) (HEPES-NaOH 20 mM)
| References:
- Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. "Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state." Plant Physiol. 2007; 143(2): 617-28. PubMed: 17189335
| Comments:
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| References |
- Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. "Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state." Plant Physiol. 2007; 143(2): 617-28. PubMed: 17189335
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