|Name:||Dehydrin Xero 2|
Low-temperature-induced protein LTI30
| First appeared in release:||Release 5.1 (05/28/2010)|
|SwissProt: ||XERO2_ARATH |
|TrEMBL: || |
|NCBI (GI): ||1169341 |
|Source organism:||Arabidopsis thaliana (Mouse-ear cress)|
10 20 30 40 50 60
| | | | | |
MNSHQNQTGV QKKGITEKIM EKLPGHHGPT NTGVVHHEKK GMTEKVMEQL PGHHGATGTG - 60
GVHHEKKGMT EKVMEQLPGH HGSHQTGTNT TYGTTNTGGV HHEKKSVTEK VMEKLPGHHG - 120
SHQTGTNTAY GTNTNVVHHE KKGIAEKIKE QLPGHHGTHK TGTTTSYGNT GVVHHENKST - 180
|Functional narrative |
Expressed in desiccated pollen grains or seeds, roots, stems, trichomes and the vascular tissues of leaves, and in all tissues of young seedlings.
By low temperature and also less strongly, by water stress or abscisic acid (ABA).
Belongs to the plant dehydrin family.
|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.
|Location:||1 - 193|
|Modification type: ||Native |
|PDB: || |
|Structural/functional type: || |
|Functional classes: || |
|Functional subclasses: || |
|Detection methods: |
- Circular dichroism (CD) spectroscopy, far-UV (277 K; resolution 0.2 nm; scan rate 20 nm/min; sensitivity 20 mdeg; Xero 2 (sample) 1 mg/mL)
- Mouillon JM, Gustafsson P, Harryson P. "Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments." Plant Physiol. 2006; 141: 638-650. PubMed: 16565295
DP00657, DP00658 and DP00689 are from the same author
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