General information | DisProt: | DP00185 | Name: | Late embryogenesis-abundant protein | Synonym(s): | P93165_SOYBN
Em protein
| First appeared in release: | Release 3.0 (02/17/2006) | UniProt: | P93165 | UniGene: | Gma.10 | SwissProt: | P93165_SOYBN | TrEMBL: | | NCBI (GI): | 75101067 | Source organism: | Glycine max (soybean) | Sequence length: | 105 | Percent disordered: | 100% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MASRQNNKQE LDERARQGET VVPGGTGGKS LEAQQHLAEG RSKGGQTRKE QLGTEGYQEM - 60 GRKGGLSTVD KSGEERAQEE GIGIDESKFR TGNNKNQNQN EDQDK
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Functional narrative |
"Late embryogenesis-abundant (LEA) proteins accumulate
to high concentrations in plant embryos
during the latter stages of seed development before
desiccation. LEA proteins also accumulate
in vegetative tissues exposed to exogenous abscisic
acid, as well as dehydration, osmotic, and lowtemperature
stress.... Various functions have been proposed for different
groups of LEA proteins ranging from water binding
to minimize water loss and protein and membrane
stabilization or protection to ion sequestration and
scavenging. LEA proteins also display diverse subcellular
and tissue-specific localization patterns, suggesting
that different groups or group members fulfill
specific functional roles.... However, the exact in planta function
of these different groups of LEA proteins remain
unknown.... The predicted hydrophilic and high degree of random
coil structure of group 1 LEA proteins have led
some researchers to propose these proteins may
serve as water-binding proteins that can minimize
water loss, act as hydration buffers to regulate water status, or interact with
the surface of macromolecules as a water matrix or
replacement to oppose protein denaturation in dehydrating
tissues." (Soulages et al. 2002)
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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 - 105 | Length: | 105 | Region sequence: |
MASRQNNKQELDERARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGTEGYQEM GRKGGLSTVDKSGEERAQEEGIGIDESKFRTGNNKNQNQNEDQDK | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises from the disordered state | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (0.1-cm path-length; 7.7 microM protein solution in 50 mM buffer Na-phosphate; pH 5, 8, and 9; temperature from 10°C to 80°C)
| References:
- Soulages JL, Kim K, Walters C, Cushman JC. "Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean." Plant Physiol. 2002; 128(3): 822-32. PubMed: 11891239
| 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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