| General information | | DisProt: | DP00170 | | Name: | Dehydrin-like protein | | Synonym(s): | Q39805_SOYBN
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | Q39805 | | UniGene: | Gma.33428 | | SwissProt: | Q39805_SOYBN | | TrEMBL: | | | NCBI (GI): | 75281899 | | Source organism: | Glycine max (Soybean) | | Sequence length: | 226 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MASYQKHYDD QGRKVDEYGN VEKQTDEYGN PVHAASVTYV ATRTAAGGYS DDINKQHDTT - 60
NAYGVDTGRQ HSSGGYDGDT NKHHGTTGGY NDDTNRHHGT TGVYGIDTDR QQHGTTGGYA - 120
GDTGRQHGNI GGPYYGTNTA DTGTGPRSGT TGGTGYGGTG GTDYGTTGGT GYGSGTGYGV - 180
NTGGAHTEAG YRKEHRQHDQ SHGDQNEKKG IMDKIKEKLP GGHSDK
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| Functional narrative |
"Late embryogenesis abundant (LEA) proteins are members of a large group of hydrophilic, glycine-rich proteins found in
plants, algae, fungi, and bacteria known collectively as hydrophilins. Group 2 LEA (dehydrins or responsive to abscisic acid) proteins are postulated to
stabilize macromolecules against damage by freezing, dehydration, ionic, or osmotic stress.... Group 2 LEA proteins form a subset of evolutionarily
conserved Gly-rich, hydrophilic proteins associated
with adaptation to hyperosmotic conditions. Dehydrins are induced
typically in maturing seeds or vegetative tissues following
salinity, dehydration, cold, or freezing stress
or abscisic acid (ABA) treatment." (Soulages et al. 2003)
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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: | | | Location: | 1 - 226 | | Length: | 226 | | Region sequence: |
MASYQKHYDDQGRKVDEYGNVEKQTDEYGNPVHAASVTYVATRTAAGGYSDDINKQHDTT
NAYGVDTGRQHSSGGYDGDTNKHHGTTGGYNDDTNRHHGTTGVYGIDTDRQQHGTTGGYA
GDTGRQHGNIGGPYYGTNTADTGTGPRSGTTGGTGYGGTGGTDYGTTGGTGYGSGTGYGV
NTGGAHTEAGYRKEHRQHDQSHGDQNEKKGIMDKIKEKLPGGHSDK | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Stability at thermal extremes (from 0°C to 100°C)
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7; buffer sodium phosphate; increasing temperatures from 12 to 80°C)
| References:
- Soulages JL, Kim K, Arrese EL, Walters C, Cushman JC. "Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure." Plant Physiol. 2003; 131(3): 963-75. PubMed: 12644649
| Comments:
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| References |
- Wise MJ, Tunnacliffe A. "POPP the question: what do LEA proteins do?" Trends Plant Sci. 2004; 9(1): 13-7. PubMed: 14729214
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| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
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